Multiple Sclerosis, ALS, Lupus, MCS & Other Conditions

0 Flares Twitter 0 Facebook 0 Google+ 0 LinkedIn 0 0 Flares ×

Proper functioning of the human body and mind depends on interactions of the brain and CNS using neuronal signaling mechanisms with elaborate metabolic and enzymatic processes and respiration that occurs at the cellular level in the various organs and parts of the body, as controlled by low levels of hormones from the endocrine system. Toxic substances, such as mercury, which the body may be chronically exposed to, accumulate in the brain, pituitary gland, CNS, liver, kidneys, etc. and can damage, inhibit, and cause imbalances at virtually any stage of various processes at very low levels of exposure, which can have major neurological, immunological, and metabolic effects on an individual. Multiple sclerosis (MS) is caused by the erosion of myelin, a substance which helps the brain send messages to the body. Metal particles entering the body can bind to this myelin. For those who are hypersensitive, this myelin-metal bond comes under attack from the immune system. This is called autoimmunity. In such cases, the progression of MS can be halted by removing the source of the metal or other toxic factor. MS prevalence has been increasing in recent years and is currently about one in 700, approximately 390,000 in the U.S.

According to the National Lupus Foundation, there are generally four recognized forms or types of lupus: 1) cutaneous (skin) lupus erythematosus, 2) systemic lupus erythematosus (SLE), 3) drug-induced erythematosus, and 4) neonatal lupus. Both genetic susceptibility and environmental factors, such as toxic metals and organic chemicals, have been found to be factors in lupus incidence. The prevalence of lupus is approximately one in every 194 or 1.4 million in the U.S. A large occupational health study found that those exposed to mercury or pesticides occupationally had a significantly higher likelihood of having the autoimmune condition lupus.

Mercury is known to be one of the most toxic substances commonly encountered, and when accompanied by lead and arsenic, these toxic substances adversely affect the largest numbers of people. Dental amalgam is documented by medical studies and medical lab tests to be largest source of both inorganic and methylmercury in most people who have several mercury amalgam fillings. Bacteria, yeasts, and vitamin B12 methylate inorganic mercury to methylmercury in the mouth and intestines, and mercury inhibits functional methylation in the body, a necessary process. The main factors determining whether chronic conditions are induced by metals appear to be exposure and genetic susceptibility, which determines individuals’ immune sensitivity and ability to detoxify metals. Very low levels of exposure have been found to seriously affect relatively large groups of individuals who are immune sensitive to toxic metals, or have an inability to detoxify metals due to such as deficient sulfoxidation or metallothionein function or other inhibited enzymatic processes related to detoxification or excretion of metals.

A large epidemiological study of 35,000 Americans by the National Institute of Health, the nation’s principal health statistics agency, found that there was a significant correlation between having a greater than average number of dental amalgam surfaces and having the a chronic condition such as epilepsy, MS, or migraine headaches. Fewer of those with this condition have zero fillings than those of the general population while significantly more of those with the condition have seventeen or more surfaces than in the general population. MS clusters in areas with high metals emissions from facilities, such as metal smelters, have been documented.

As far back as 1996 it was shown that the lesions produced in the myelin sheath of axons in cases of multiple sclerosis were related to excitatory receptors on the primary cells involved called oligodendroglia. The loss of myelin sheath on the nerve fibers characteristic of the disease is due to the death of these oligodendroglial cells at the site of the lesions (called plaques). Further, these studies have shown that the death of these important cells is as a result of excessive exposure to excitotoxins at the site of the lesions. Most of these excitotoxins are secreted from microglial immune cells in the central nervous system. This not only destroys these myelin-producing cells but it also breaks down the blood-brain barrier (BBB), allowing excitotoxins in the blood stream to enter the site of damage. Some common exposures that cause such proliferation of such excitotoxins, resulting in MS, are mercury and aspartame, with additional effects from MSG and methanol.

Mercury and other toxic metals inhibit astrocyte function in the brain and CNS, causing increased glutamate and calcium-related neurotoxicity which are factors in neural degeneration in MS and ALS. There is evidence that astrocyte damage/malfunction is a major factor in MS. Mercury and increased glutamate activate free radical forming processes, like xanthine oxidase, which produce oxygen radicals and oxidative neurological damage. Nitric oxide-related toxicity (caused by peroxynitrite formed by the reaction of NO with superoxide anions, which results in nitration of tyrosine residues in neurofilaments and manganese Superoxide Dimustase(SOD)) has been found to cause inhibition of the mitochondrial respiratory chain, inhibition of the glutamate transporter, and glutamate-induced neurotoxicity involved in ALS.

It is now known the cause for the destruction of the myelin in the lesions is over activation of the microglia in the region of the myelin. An enzyme that converts glutamine to glutamate called glutaminase increases tremendously, thereby greatly increasing excitotoxicity. Any dietary excitotoxin can activate the microglia, thereby greatly aggravating the injury. This includes the aspartate in aspartame and MSG, which is in many processed foods. The methanol in diet drinks adds to this toxicity as well. Now, the secret to treatment appears to be calming down inflammation of the microglia. Mercury and cadmium inhibit magnesium and zinc levels as well as inhibiting glucose transfer are other mechanisms by which mercury and toxic metals are factors in metabolic syndrome and insulin resistance/diabetes. Reduced levels of magnesium and zinc are related to metabolic syndrome, insulin resistance, and brain inflammation and are protective against these conditions.

According to neurologist Dr. RL Blaylock, the good news is that there are supplements and nutrients that calm the microglia-the most potent are: silymarin, curcumin, and ibuprophen. Phosphatidylcholine helps re-myelinate the nerve sheaths that are damaged, as does B12, B6, B1, vitamin D, folate, vitamin C, natural vitamin E (mixed tocopherols), and L-carnitine. A study
demonstrated the protective effects of methylcobalamin, a vitamin B12 analog, against glutamate-induced neurotoxicity, and similarly for iron in those who are iron deficient, DHA plays a major role in repairing the myelin sheath. Vitamin D may even prevent MS, but it acts as an immune modulator, preventing further damage—the initial dose is 2000 IU a day. Magnesium, as magnesium malate, is needed in a dose of 500 mg 2X a day. They must avoid all excitotoxins, even natural ones in foods-such as soy, red meats, nuts, mushrooms, and tomatoes. Avoid all fluoride and especially all vaccinations since these either inhibit antioxidant enzymes or trigger harmful immune reactions. Intake of 400 IU/day of vitamin D from multivitamins was associated with a reduced risk whereas intake of whole milk, an important source of dietary vitamin D, was associated with an increased risk. It has also been found that the antibiotic minocycline powerfully shuts down the microglia. Dr. Blaylock tried this treatment on a patient who just came down with fulminant MS and was confined to a wheelchair. The patient was placed on minocycline, and now he is able to walk.

The various neurological, immune, and metabolic-related diseases discussed together here are diagnosed and labeled clinically based primarily on symptoms, along with tests for some underlying conditions found common in each disease. Nevertheless, each individual will seem to have their own unique combination of neurological, endocrine, and enzymatic imbalances along with auto-immunities that result in the functional problems that lead to symptoms that are diagnosed as MS, ALS, Alzheimer’s, Parkinson’s, lupus, rheumatoid arthritis, chronic fatigue syndrome (CFS), or oral lichen planus (OLP), etc. However, a lot of commonality among these factors has been documented, both within specific diseases and among the various diseases discussed here. In MS, an autoimmune T-cell attack on CNS myelin sheath results in demyelinated plaques. Activated T-cells, plasma cells, and macrophages have been found in the demyelinated areas. ALS is a systemic motor neuron disease that affects the corticospinal and corticobulbar tracts, ventral horn motor neurons, and motor cranial nerve nuclei. Approximately 10% of ALS cases are of the familial type that has been linked to a mutation of the copper/zinc super oxide dismutase gene (Cu/Zn SOD). The majority of ALS cases are of the sporadic type. There are many toxic substances as well as some common drugs that have been found to be major factors in producing the functional conditions that result in these diseases. However, mercury appears to be the most commonly implicated of these, and, in particular, mercury from amalgam fillings. For the majority of cases, there are now tests to identify the various factors involved in these types of diseases, and once an individual’s underlying causative factors have been identified, high success rates at cure or significant improvement are achieved.

Toxic metals, such as mercury, lead, cadmium, etc., have been documented to be neurotoxic, immunotoxic, reproductive/developmental toxins that according to U.S. Government agencies cause adverse health effects and learning disabilities to millions in the U.S. each year, especially children and the elderly. Exposure of humans and animals to toxic metals is widespread and in many areas increasing. The U.S. Center for Disease Control ranks toxic metals as the number one environmental health threat to children. According to an EPA/ATSDR assessment, the toxic metals mercury, lead, and arsenic are the top three toxics that have the most adverse health effects on the public based on toxicity and current exposure levels in the U.S., with cadmium, nickel and chromium also highly listed.

While there is considerable commonality to the health effects caused by these toxic metals, the effects are cumulative and synergistic in many cases. The public appears to be generally unaware that considerable scientific evidence supports that mercury is the metal causing the most widespread adverse health effects to the public, and amalgam fillings have been well documented to be the number one source of exposure of mercury to most people, with exposure levels often exceeding government health guidelines and levels documented to cause adverse health effects. Much of the direct chronic exposure to toxic metals for persons with the autoimmune diseases discussed here appears to be from use of metals in dental work. The most common dental metals that have been documented to be causing widespread adverse health effects are mercury, nickel, palladium, gold, and copper. Although chronic exposure clearly is affecting a much larger population, nickel has been found to be a major factor in many cases of MS and lupus, with palladium having very similar effects to nickel. Likewise chronic exposures to manganese and copper have been implicated in some cases of Parkinson’s disease. Another group of toxic substance substances with widespread exposure that have been demonstrated to generate reactive oxygen species and have positive correlations to some of the diseases discussed here are the organochlorine pesticides. Toxic metals appear to be only one of the factors involved in chronic autoimmune conditions. Pathogens such as viruses, mycoplasma, bacteria, and parasites have been found to usually be present and a factor to deal with in treating those with chronic degenerative conditions and weakened immune. Studies have found high incidence of EBV and mycoplasma in MS patients, and treatment of such has been a factor in improvement of some according to Dr. Blaylock’s and Dr. Nicholson’s experience and papers.

Documentation of High Common Exposures & Accumulation of Mercury in the Brain & Motor Neurons

Amalgam fillings are the largest source of mercury in most people with daily exposures documented to commonly be above government health guidelines. This is due to continuous vaporization of mercury from amalgam in the mouth, along with galvanic currents from mixed metals in the mouth that deposit the mercury in the gums and oral cavity. Due to the high daily mercury exposure and excretion into home and business sewers of those with amalgam, dental amalgam is also the largest source of the high levels of mercury found in all sewers and sewer sludge, and thus according to government studies a significant source of mercury in rivers, lakes, bays, fish, and crops. People also get significant exposure from vaccinations, fish, and dental office vapor.

When amalgam was placed into teeth of monkeys and rats, within one year, mercury was found to have accumulated in the brain, trigeminal ganglia, spinal ganglia, kidneys, liver, lungs, hormone glands, and lymph glands. People also commonly get exposures to mercury and other toxic metals such as lead, arsenic, nickel, and aluminum from food, water, and other sources. All of these are highly neurotoxic and are documented to cause neurological damage, which can result in chronic neurological conditions over time, as well as ADHD, mood, and behavioral disorders.

Mercury is one of the most toxic substances in existence and is known to bio-accumulate in the body of people and animals that have chronic exposure. Mercury exposure is cumulative and comes primarily from four main sources: 1) silver (mercury) dental fillings, 2) food(mainly fish), 3) vaccinations, and 4) occupational exposure. Whereas mercury exposure from fish is primarily methylmercury and mercury from vaccinations is thimerosal (ethyl mercury), mercury from occupational exposure and dental fillings is primarily from elemental mercury vapor. Developmental and neurological conditions occur at lower levels of exposure from mercury vapor than from inorganic mercury or methylmercury. Mercury in amalgam fillings, because of its relatively high vapor pressure compared to its PEL safety limit and galvanic action with other metals in the mouth, has been found to be continuously vaporized and released into the body. The level of daily exposure of those with several amalgam fillings commonly exceeds the U.S. EPA health guideline for daily mercury exposure of 0.1 ug/kg body weight/day, and the oral mercury level commonly exceeds the mercury MRL of the U. S. ATSDR of 0.2 ug/cubic meter of air. When amalgam fillings are replaced, levels of mercury in the blood, urine, and feces typically rise temporarily but decline between 60 to 85% within 6 to 9 month.

Mercury has been found to accumulate preferentially in the brain, major organs, hormone glands, and primary motor function related areas involved in ALS-such as the brain stem, cerebellum, rhombencephalon, dorsal root ganglia, and anterior horn motor neurons. Mercury, with exposure either to vapor or organic mercury, tends to accumulate in the glial cells in a similar pattern, and the pattern of deposition is the same as that seen from morphological changes. Though mercury vapor and organic mercury readily cross the blood-brain barrier, mercury has been found to be taken up into neurons of the brain and CNS without having to cross the blood-brain barrier because mercury has been found to be taken up and transported along nerve axons as well through calcium and sodium channels and along the olfactory path.

Mercury Toxicity: Summary of Neurological Effects

Mercury has been found to accumulate in the cerebellum and other brain areas, producing reactive oxygen species (ROS), including superoxide that cause damage to those parts of the brain. Mercury was also found to cause a reduction in antioxidant function such as superoxide dismutase (SOD) and glutathione peroxide (GPx) that tries to counter-balance the ROS. Mercury, with exposure either to vapor or organic mercury, tends to accumulate in the glial cells in a similar pattern, and the pattern of deposition is the same as that seen from morphological changes. Mercury (especially mercury vapor or organic mercury) penetrates and damages the blood brain barrier allowing penetration of the barrier by other substances that are neurotoxic (along with reduced amino acid uptake to brain). Such damage to the blood brain barrier’s function has been found to be a major factor in chronic neurological diseases such as MS.

Programmed cell death (apoptosis) is documented to be a major factor in degenerative neurological conditions like MS, ALS, Alzheimer’s, Parkinson’s, etc. Some of the factors documented to be involved in apoptosis of neurons and immune cells include inducement of the inflammatory cytokine Tumor Necrosis Factor-alpha (TNFa), reactive oxygen species and oxidative stress, reduced glutathione levels, liver enzyme effects and inhibition of protein kinase C and cytochrome P450, nitric oxide and peroxynitrite toxicity, excitotoxicity and lipid peroxidation, excess free cysteine levels, excess glutamate toxicity, excess dopamine toxicity, beta-amyloid generation, increased calcium influx toxicity and DNA fragmentation, and mitochondrial membrane dysfunction.

TNFa is a cytokine that controls a wide range of immune cell response in mammals, including cell death (apoptosis). This process is involved in inflammatory and degenerative neurological conditions like ALS, MS, Parkinson’s, rheumatoid arthritis, etc. Cell signaling mechanisms like sphingolipids are part of the control mechanism for the TNFa apoptosis mechanism. Glutathione is an amino acid that is a normal cellular mechanism for controlling apoptosis. When glutathione is depleted in the brain, reactive oxidative species increased, and CNS and cell signaling mechanisms are disrupted by toxic exposures such as mercury, neuronal cell apoptosis results and neurological damage. Mercury has been shown to induce TNFa, deplete glutathione, and increase glutamate, dopamine, and calcium-related toxicity, causing inflammatory effects and cellular apoptosis in neuronal and immune cells. Mercury’s biochemical damage at the cellular level include:

  • DNA damage;
  • inhibition of DNA and RNA synthesis;
  • alteration of protein structure;
  • alteration of the transport and signaling functions of calcium;
  • inhibition of glucose transport, and of enzyme function and other essential nutrients;
  • induction of free radical formation;
  • depletion of cellular glutathione (necessary for detoxification processes);
  • inhibition of glutathione peroxidase enzyme;
  • inhibition of glutamate uptake;
  • induction of peroxynitrite and lipid peroxidation damage;
  • abnormal migration of neurons in the cerebral cortex and immune system damage; and
  • induced inflammatory cytokines and autoimmunity.

MS patients have been found to have much higher levels of mercury in cerebrospinal fluid compared to controls. German studies have found that MS patients usually have high levels of mercury body burden, with one study finding 300% higher than controls. Most recovered after mercury detox, with some requiring additional treatment for viruses and intestinal dysbiosis. Very high levels of mercury are also found in brain memory areas such as the cerebral cortex and hippocampus of patients with diseases with memory related symptoms. Studies have found mercury related neurological effects to be indistinguishable from those of MS. Mercury has been shown to be a factor that can cause rheumatoid arthritis by activating localized CD4+ T-cells which trigger production of immune macrophages and immunoglobulin (Ig) producing cells in joints.

Mercury Related Neurological Damage: Mechanisms of Causality

Exposure to inorganic mercury has significant effects on blood parameters and liver function. Studies have found that in a dose-dependent manner, mercury exposure causes reductions in oxygen consumption and availability, perfusion flow, biliary secretion, hepatic ATP concentration, and cytochrome P450 liver content, while increasing blood hemolysis products and tissue calcium content and inducing heme oxygenase, porphyria, and platelet aggregation through interfering with the sodium pump. Mercury vapor and methylmercury penetrate and damage the blood brain barrier, facilitating other toxic substances’ penetration of the BBB. Damage to the blood brain barrier’s function has been found to be a major factor in chronic neurological diseases. Mercury also causes high levels of oxidative stress and reactive oxygen species (ROS), which have been implicated as major factors in neurological disorders, including stroke, ALS, PD, Alzheimer’s, CFS, and lupus. Studies have found mercury-related neurological effects to be indistinguishable from those of MS.

Metals like mercury bind to SH-groups (sulphydryl) in sulfur compounds like amino acids and proteins, changing the structure of the compound that it is attached to. This often results in the immune systems T-cells not recognizing sulphydryl as appropriate nutrients and attacking them. Such binding and autoimmune damage has been documented in the fat-rich proteins of the myelin sheaths and collagen, which are both affected in MS. Metals by binding to SH radicals in proteins and other such groups can cause autoimmunity by modifying proteins which via T-cells activate B-cells that target the altered proteins inducing autoimmunity as well as causing aberrant MHC II expression on altered target cells.

Studies have also found mercury and lead cause autoantibodies to neuronal proteins, neurofilaments, and myelin basic protein (MBP). Mercury and cadmium also have been found to interfere with zinc binding to MBP, which affects MS symptoms since zinc stabilizes the association of MBP with brain myelin. MS has also been found to commonly be related to inflammatory activity in the CNS, such as that caused by the reactive oxygen species and cytokine generation caused by mercury and other toxic metals. Antioxidants like lipoic acid which counteract such free radical activity have been found to alleviate symptoms and decrease demyalination. A group of metal exposed MS patients with amalgam fillings were found to have lower levels of red blood cells, hemoglobin, hemocrit, thyroxine, T-cells, and CD8+ suppressor immune cells than a group of MS patients with amalgam replaced, and more exacerbations of MS than those without. Immune and autoimmune mechanisms are thus seen to be a major factor in neurotoxicity of metals

Na(+),K(+)-ATPase is a transmembrane protein that transports sodium and potassium ions across cell membranes during an activity cycle that uses the energy released by ATP hydrolysis. Mercury is documented to inhibit Na(+),K(+)-ATPase function at very low levels of exposure. Studies have found that in MS cases there was an elevation in plasma serum digoxin and a reduction in serum magnesium and RBC membrane Na(+)-K+ ATPase activity. The activity of all serum free-radical scavenging enzymes, concentration of glutathione, alpha tocopherol, iron binding capacity, and ceruloplasmin decreased significantly in Ms, while the concentration of serum lipid peroxidation products and nitric oxide increased. The inhibition of Na+-K+ ATPase can contribute to increase in intracellular calcium and decrease in magnesium, which can result in 1) defective neurotransmitter transport mechanism, 2) neuronal degeneration and apoptosis, 3) mitochondrial dysfunction, and 4) defective golgi body function and protein processing dysfunction.

Autoimmunity has also been found to be a factor in chronic degenerative autoimmune conditions such as MS, ALS, etc., with genetic susceptibility a major factor in who is affected. One genetic factor in Hg-induced autoimmunity is major histocompatibility complex (MHC) linked. Both immune cell type Th1 and Th2 cytokine responses are involved in autoimmunity. One genetic difference found in animals and humans is cellular retention differences for metals related to the ability to excrete mercury. For example, it has been found that individuals with genetic blood factor type APOE-4 do not excrete mercury readily and bio-accumulate mercury, resulting in susceptibility to chronic autoimmune conditions such as Alzheimer’s, Parkinson’s, etc. as early as age forty, whereas those with type APOE-2 readily excrete mercury and are less susceptible. Those with type APOE-3 are intermediate to the other 2 types. The incidence of autoimmune conditions has increased to the extent this is now one of the leading causes of death among women. When a condition has been initiated and exposure levels decline, autoimmune antibodies also decline in animals or humans. Calcium plays a major role in the extreme neurotoxicity of mercury and methylmercury. Both inhibit cellular calcium ATPase and calcium uptake by brain microsomes at very low levels of exposure. Protein Kinase C (PKC) regulates intracellular and extra cellular signals across neuronal membranes, and both forms of mercury inhibit PKC at micromolar levels, as well as inhibiting phorbal ester binding. They also block or inhibit calcium L-channel currents in the brain in an irreversible and concentration dependent manner. Metallic mercury is much more potent than methyl mercury in these actions, with 50 % inhibition.

A direct mechanism involving mercury’s inhibition of cellular enzymatic processes by binding with the hydroxyl radical (SH) in amino acids appears to be a major part of the connection to allergic/immune reactive conditions. The binding of mercury from amalgam to the -SH groups often results in inactivation of sulfur and blocking of enzyme function, producing sulfur metabolites with extreme toxicity that the body is unable to properly detoxify. Sulfur is essential in enzymes, hormones, nerve tissue, and red blood cells. These exist in almost every enzymatic process in the body. Blocked or inhibited sulfur oxidation at the cellular level has been found in most with many of the chronic degenerative diseases, including Parkinson’s, Alzheimer’s, ALS, lupus, rheumatoid arthritis, CFS, FMS, MCS, autism, etc.

Some studies of patients with major neurological or degenerative diseases have found evidence amalgam fillings may play a major role in development of conditions such as MS, ALS, RA, AD, SLE, PD, and many other conditions. Mercury-induced lipid peroxidation has been found to be a major factor in mercury’s neurotoxicity, along with leading to decreased levels of glutathione peroxidation and superoxide dismutase (SOD). Only a few micrograms of mercury severely disturb cellular function.

Mercury exposure causes high levels of oxidative stress/reactive oxygen species (ROS), which have been found to be a major factor in neurological disease. Mercury and quinones form conjugates with thiol compounds such as glutathione and cysteine and cause depletion of glutathione, which is necessary to mitigate reactive damage. Such conjugates are found to be highest in the brain substantia nigra with similar conjugates formed with L-Dopa and dopamine in Parkinson’s disease. Mercury depletion of GSH and damage to cellular mitochondria and the increased lipid peroxidation in protein and DNA oxidation in the brain appear to be a major factor in Parkinson’s disease. A Canadian study found those with fifteen or more amalgam fillings to have more than 250% greater risk of MS than controls, and likewise higher risk for those who have had amalgam fillings more than fifteen years, and another study also found higher mercury body burden in those with more fillings and increased risk of MS with more fillings. Another study found blood and urine mercury levels to be very strongly related to Parkinson’s with odds ratios of approximately twenty.

Exposure to mercury results in metalloprotein compounds that genetics affects, having both structural and catalytic effects on gene expression. Some of the processes affected by such metalloprotein control of genes include cellular respiration, metabolism, enzymatic processes, metal-specific homeostasis, and adrenal stress response systems. Significant physiological changes occur when metal ion concentrations exceed threshold levels. Such metalloprotein formation also appears to cause a change in antigenicity and autoimmune reactions in significant numbers of people. Much mercury in saliva and the brain is also organic, the most neurotoxic form, since mouth bacteria and other organisms in the body methylate inorganic mercury to organic mercury. Dental amalgam has been found to be the largest source of methylmercury in most with mercury amalgam fillings.

Spatial and temporal changes in intracellular calcium concentrations are critical for controlling neurotransmitter release in neurons. Mercury alters calcium homeostasis and calcium levels in the brain and affects neurotransmitter release through its effects on calcium levels. Low levels of toxic metals have been found to inhibit dihydroteridine reductase, which affects the neural system function by inhibiting neurotransmitters through its effect on phenylalanine, tyrosine and tryptophan transport into neurons. This was found to cause severe impaired amine synthesis and hypokinesis. Tetrahydro-biopterin, which is essential in production of neurotransmitters, is significantly decreased in patients with Alzheimer’s, Parkinson’, and MS. Such patients have abnormal inhibition of neurotransmitter production. Mercury at extremely low levels also interferes with formation of tubulin producing neurofibrillary tangles in the brain, similar to those observed in Alzheimer’s patients with high levels of mercury in the brain.

Mercury and the induced neurofibrillary tangles also appear to produce a functional zinc deficiency in AD sufferers, as well as causing reduced lithium levels which is another factor in such diseases. The low Zn levels result in deficient CuZnSuperoxide dismutase (CuZnSOD), which in turn leads to increased levels of superoxide. Lithium protects brain cells against excess glutamate induced excitability and calcium influx. Also mercury binds with cell membranes, interfering with sodium and potassium enzyme functions and causing excess membrane permeability, especially in terms of the blood-brain barrier. Less than 1 ppm mercury in the blood stream can impair the blood-brain barrier. Mercury was also found to accumulate in the mitochondria and interfere with their vital functions, and to inhibit cytochrome C enzymes which affect energy supply to the brain. Persons with extra Apo-E4 gene copies appear especially susceptible to this damage.

Mercury blocks the immune function of magnesium and zinc, whose deficiencies are known to cause significant neurological effects. The low Zn levels result in deficient CuZnSuperoxide dismustase (CuZnSOD), which in turn leads to increased levels of superoxide due to toxic metal exposure. This is in addition to mercury’s effect on metallothionein and copper homeostasis as previously discussed. Copper is an essential trace metal which plays a fundamental role in the biochemistry of the nervous system. Several chronic neurological conditions involving copper metabolic disorders are well documented like Wilson’s disease and Menkes disease. Mutations in the copper/zinc enzyme superoxide dismustase (SOD) have been shown to be a major factor in the motor neuron degeneration in conditions like familial ALS. Exposures to toxic metals, such as mercury and cadmium, have been found to cause such effects, and similar effects on Cu/Zn SOD have been found to be a factor in other conditions such as autism, Alzheimer’s, Parkinson’s, and ALS. This condition can result in zinc deficient SOD and oxidative damage involving nitric oxide, peroxynitrite, and lipid peroxidation, which have been found to affect glutamate mediated excitability and apoptosis of nerve cells and effects on mitochondria. These effects can be reduced by zinc supplementation, as well as supplementation with antioxidants and nitric oxide-suppressing agents and peroxynitrite scavengers such as vitamins E and C, lipoic acid, coenzyme Q10, carnosine, gingko biloba, N-acetylcysteine, etc. Some of the antioxidants, such as ginkgo bilabo, were also found to have protective effects through increasing catalase and SOD action, while reducing lipid peroxidations. Ceruloplasmin in plasma can be similarly affected by copper metabolism dysfunction, like SOD function, and is often a factor in neurodegeneration.

Excess zinc from products such as GSK Superpolygrip (before reformulated) can also cause demyelating conditions with effects similar to MS, demyelinating syndrome, and chronic inflammatory demyelinating polyneuropathy (CIDP). Mercury and other toxic metals inhibit astrocyte function in the brain and CNS, causing increased glutamate and calcium-related neurotoxicity which are responsible for much of the fibromyalgia symptoms and a factor in neural degeneration in MS and ALS. There is some evidence that astrocyte damage/malfunction is the main factor in MS. This is also a factor in conditions such as CFS, Parkinson’s, and ALS. Animal studies have confirmed that increased levels of glutamate (or aspartate, another amino acid excitory neurotransmitter) causes increased sensitivity to pain, as well as higher body temperature-both found in CFS/Fibromyalgia. Mercury and increased glutamate activate free radical forming processes like xanthine oxidase which produce oxygen radicals and oxidative neurological damages. Medical studies and doctors treating fibromyalgia have found that supplements which cause a decrease in glutamate or protect against its effects have a positive effect on fibromyalgia and other chronic neurological conditions. Some that have been found to be effective include CoQ10, ginkgo biloba and pycnogenol, NAC, vitamin B6, methyl cobalamine (B12), L-carnitine, choline, ginseng, vitamins C and E, nicotine, and omega 3 fatty acids (fish and flaxseed oil).

Endocrine System & Metabolic Enzymatic System Impairments

Mercury has been well documented to be an endocrine system-disrupting chemical, affecting hormonal processes and enzyme production processes at very low levels. The pituitary gland, in which mercury has been documented to accumulate, controls many of the body’s endocrine system functions and secretes hormones involved in control of most bodily processes. The hypothalamus regulates body temperature and many metabolic processes. Such hormonal secretions are affected at levels of mercury exposure much lower than the acute toxicity effects normally tested for. Some of the common effects of mercury on the endocrine system include inhibiting human growth hormone, causing hormonal imbalances that affect the reproductive system and body temperature regulation and causing hormonal imbalances that result in imbalances in metabolism of important minerals, such as calcium.

Calcium flux is inhibited in synoptic plasma membranes of the cerebellum and cerebrum cortex. A permanent increase in cytosolic calcium levels appears to be associated with various pathological conditions which result in cell death. All of the effects on hormonal regulation of the various bodily processes add to and reinforce the imbalances caused in the metabolic enzymatic processes. All body functions depend on cellular enzymatic and respiratory processes that use nutrients delivered by the blood, detoxify toxic substances, and eliminate waste products through the cellular respiratory process back through the lymph and blood to the lungs, kidneys, or liver for excretion. Proteins are converted by enzymatic processes to amino acids, such as cysteine, cysteine, glutamic acid, methionine, etc. for cellular metabolic processes and to organic compounds such as glutathione which is necessary to detoxify toxic substances such as mercury. Imbalances or blockages in any of several of these enzymatic processes have been documented to cause major neurological and immune damage that appears to be involved in most of the diseases being discussed here.

In those that are chronically exposed, mercury vapor is continuously released into the blood stream through the lungs and distributed to cells throughout the body, where it creates metal-protein compounds and reactive oxidative species (ROS) such as superoxide, which must be detoxified. Cysteine and glutathione, which are produced and interchanged as required through enzymatic processes, are necessary for detoxification. Blockages or impairments caused by mercury or other toxic substances or processes can then result in cellular toxicity and damage to vital organs such as the brain, CNS, liver, or kidneys.

Clinical tests of patients with motor neuron disease (MND), ALS, PD, AD, SLE, and RA have found that the patients generally have damaged enzymatic processes resulting in elevated plasma cysteine to sulfate ratios, with the average being 500% higher than controls, and in general are poor sulfur oxidizers. High levels of free cysteine have been found to result in major neurological damage to the brain, CNS, and cellular processes. The two main enzymatic processes that down regulate cysteine to taurine, sulfates, and glutathione are cysteine dioxygenase (CDO) and gamma-glutamylcysteine synthetase (GGCS). Impairment in CDO can result in high cysteine levels, high cysteine to sulfate ratio, low taurine levels, and neurological damage. GGCS converts cysteine to glutathione, which has been demonstrated to be necessary to detoxification of toxic substances like mercury. If this enzymatic process is blocked, inhibited, or overloaded by chronic high toxicity levels or autoimmune reactions, there is insufficient glutathione, and toxic damage occurs due to the immune system’s inability to process the metal-organic compounds and the ROS created by exposure to mercury or other toxic substances. Another enzymatic process necessary for proper cellular metabolism is sulfite oxidase (SO), which is involved in conversion of toxic sulfur forms such as sulfites, sulfur dioxide (SO2), hydrogen sulfide(H2S), etc. to nontoxic sulfates. SO can be blocked or inhibited by mercury or other toxic exposures, resulting in more of these very toxic sulfur compounds. SO is commonly found to be totally blocked or inhibited in patients with MND, PD, AD, SLE, RA, etc.

Glutathione peroxidase (GPx) is another enzymatic process in this loop that is often affected, as well as the process involved in converting Vitamin B6 through the essential coenzyme pyrodoxal 5-phosphate (P5P) in the synthesis of neurotransmitters. Impairment in this process results in brain neurotransmitter imbalances. Individual patients with any of these diseases who commonly have been shown to have high ratio of cysteine to sulfate can thus have several different individual enzymatic blockages or imbalances that result in such high ratios, and different levels of neurological, immune, and cellular damage due to high cysteine levels or low glutathione levels. Autoimmune reactions have also been found to be commonly involved in such blockages or imbalances, particularly for those with the major diseases being considered here. This aspect will thus be further discussed.

Autoimmunity, Neurological & Immune Diseases, & Mercury

Mercury has been documented to cause autoimmune disease, and many researchers have concluded that autoimmunity is a factor in the major chronic neurological diseases such as MS, ALS, PD, SLE, RA, etc. Mercury and other toxic metals also form inorganic compounds with OH, NH2, CL, in addition to the SH radical, and thus inhibit many cellular enzyme processes, coenzymes, hormones, and blood cells. Mercury has been found to impair conversion of thyroid T4 hormone to the active T3 form as well as causing autoimmune thyroiditis common to such patients. In general, immune activation from toxic metals such as mercury resulting in cytokine release and abnormalities of the hypothalamus-pituitary-adrenal (HPA) axis can cause changes in the brain, fatigue, and severe psychological symptoms, such as profound fatigue, muscoskeletal pain, sleep disturbances, gastrointestinal and neurological problems as are seen in CFS, fibromyalgia, and autoimmune thyroiditis. Such hypersensitivity has been found most common in those with genetic predisposition to heavy metal sensitivity. A significant portion of the population appears to fall in this category.

The enzymatic processes blocked by such toxic substances as mercury also result in chronic formation of metal-protein compounds (HLA antigens or antigen-presenting macrophages) that the body’s immune system (T-lymphocytes) does not recognize, resulting in autoimmune reactions. The metals bind to SH-groups on proteins which can then be recognized as “foreign” and attacked by immune lymphocytes. Such has been extensively documented by studies such as the documentation of the autoimmune function test MELISA, a sophisticated immune/autoimmune test which was developed to test for such reactions.

Very low doses and short term exposures of inorganic Hg (20-200 mug/kg) exacerbate lupus and accelerate mortality in mice. Low dose Hg exposure increases the severity and prevalence of experimental autoimmune myocarditis induced by other factors. A strong significant correlation was found between occupational exposure to mercury (or pesticides) to lupus, with dental personal at a very high risk of developing lupus. In a study of small-scale gold mining that used mercury, there was a positive interaction between Hg autoimmunity and malaria. These results suggest a new model for Hg immunotoxicity as a co-factor in autoimmune disease, increasing the risks and severity of clinical disease in the presence of other triggering events, either genetic or acquired.

Autoimmune reactions to inorganic and methylmercury have been found to be relatively independent, occurring in over 10% of controls. In the population of over 3,000 patients tested by MELISA, the following percentages tested positive for lymphocyte reactivity:

  • Nickel: 34%
  • Inorganic mercury: 22%
  • Phenyl mercury: 15%
  • Methylmercury: 8%
  • Gold: 10%
  • Palladium: 10%
  • Cadmium: 11%
  • Silver: 1%

Groups with autoimmune symptoms, such as oral lichen planus, CFS, MS, and autoimmune thyroiditis, generally have high percentages with lymphocyte reactivity to metals. Among a population of patients being tested for autoimmune problems, 94% of such patients had significant immune reactions to inorganic mercury, and 72% had immune reactions to low concentrations of HgCl2 (0.5 ug/ml). Of a population of 86 patients with CFS symptoms who had amalgam fillings replaced, 78% reported significant health improvement in a relatively short time period after replacement, and MELISA test scores had a significant reduction in lymphocyte reactivity compared to pre-replacement. Similar results were experienced for those with MS, lupus, and autoimmune thyroiditis. The MELISA test has proved successful in diagnosing and treating environmentally caused autoimmune diseases such as MS, SLE, oral lichen planus, CFS, etc.

A high percentage of patients subjectively diagnosed with CNS and systemic symptoms suggestive of mercury intoxication have been found to have immune reactivity to inorganic mercury and likewise for MRI positive patients for brain damage. Controls without CNS problems did not have such positive correlations. Nickel, palladium, and gold have also been found to induce autoimmunity in genetically predisposed or highly exposed individuals. Tests have found a significant portion of people (over 10%) to be in this category and thus more affected by exposure to amalgam than others. Once compromised by a toxic substance that depletes the immune protectors and causes autoimmunity, the immune system is more susceptible to being sensitized to other toxic chemicals, a factor in multiple chemical sensitivity (MCS). Mercury also causes a reduction in thyroid production and an accumulation in the thyroid of radiation. Among those with chronic immune system problems with related immune antibodies, the types showing the highest level of antibody reductions after amalgam removal include glomerular basal membrane, thyroglobulin, and microsomal thyroid antigens.

Mercury and toxic metals block enzymes required to digest milk casein and wheat gluten, resulting in increased IgA and IgG to gluten and IgA to casein, as well as dumping morphine-like substances in the blood that are neurotoxic, as a major factor in schizophrenia, autism, ADHD, and MS. A higher level of milk consumption has been found to be correlated with higher MS incidence. A casein/gluten free diet has been found to result in improvements in conditions like MS and autism.

MS occurs due to a reduction in immune system activity. Specifically, it is the reduction in the number of the suppressor T-cells within the immune system that allows CD4 helper T-cells to do damage. Thus, during an acute relapse the overall number of T-cells is reduced, the normal balance of helper and suppressor T-cells is disrupted, and helper T-cells tend to predominate. This is most pronounced during an acute relapse, but a similar situation occurs although perhaps to a lesser extent, in chronic progressive MS. A double blind study using a potent opiate antagonist, naltrexone (NAL), produced significant reduction in neurological symptomology among the 56% most responsive to opioid effects in a population of autism patients. The behavioral improvements were accompanied by alterations in the distribution of the major lymphocyte subsets, with a significant increase in the T-helper-inducers and a significant reduction of the T-cytotoxic-suppressors and a normalization of the CD4/CD8 ratio. Low dose naltrexone (LDN) has been found to commonly be effective in reducing MS symptoms and exerbations, apparently due its opioid suppressive effects.

Recovery from Chronic Neurological & Immune Related Diseases After Amalgam Removal & Mercury Detoxification

There are extensive documented cases (many thousands) where removal of amalgam fillings led to cure of serious health problems such as MS, SLE, muscular/joint pain/fibromyalgia, depression, rheumatoid arthritis, autoimmune thyroiditis, oral lichen planus, ALS, Parkinson’s/muscle tremor, Alzheimer’s, and many other chronic conditions. In several of the studies, over 75% of those with MS and having amalgams replaced recovered or had significant improvement. Some of the studies reported similar success rates for SLE and autoimmune thyroiditis but with a lower number of cases treated. There is consensus that dental amalgam is the main cause of oral lichen planus, and most recover after amalgam replacement.

In one study, all six of those tested for autoimmunity by the MELISA blood lymphocyte immune reactivity test were found to be immune reactive to mercury, and all had significant improvement in their condition after amalgam replacement, as well as reduction in immune reactivity. Out of fifteen patients with lupus, 73% had significant improvement in health, and out of eight with autoimmune thyroiditis, 75% had significant improvement after amalgam replacement. The patients who did not have significant improvement were found to have immune reactivity to nickel, which did not improve after amalgam replacement as the amalgam was not the source of the nickel exposure.

Clinical studies have found that patch testing is not a good predictor of success of amalgam removal, as a high percentage of those testing negative also recovered from chronic conditions after replacement of fillings. Follow up tests for autoimmune reaction to inorganic mercury after amalgam replacement have found that in most patients tested, the immune reaction as well as most symptoms disappear over time. The level of mercury in the gums is often 1200 ppm near a gold cap on an amalgam filling. These levels are among the highest levels ever measured in tissues of living organisms, exceeding the highest levels found in chronically exposed chloralkali workers, those who died from mercury in Minamata, or animals that died from mercury poisoning. The FDA/EPA action level for warnings of dangerous levels in fish or food is 1 ppm.

Tests & Treatment

In a large German study of MS patients after amalgam revision, extraction resulted in 85% recovery rate versus only 16% for filling replacement alone. Another large clinic in Colorado has likewise found that more seriously affected cases often require more than simple replacement for successful treatment. Other clinics have found that recovery from serious autoimmune diseases, dementia, or cancer may require more aggressive mercury removal techniques than simple filling replacement due to body burden. This appears to be due to migration of mercury into roots and gums that is not eliminated by simple filling replacement. Also toxic metals, formaldehyde, and other toxic substances have been documented to accumulate in the jaw bone and tissue near teeth with multiple metals, as well as in pockets from extracted teeth, and to form cavitations (areas of toxic materials and diseased bone). Such cavitations and toxic bacteria accumulating from root-canaled teeth sometimes must be cleaned out before significant recovery can occur.

The following protocol, Huggins Total Dental Revision Protocol, is perhaps the most used protocol for treating these conditions and has had considerable success. The protocol is composed of:

  1. discussing history questionnaire and taking a panel of tests;
  2. replacing amalgam fillings starting with filling with highest negative current or highest negative quadrant, with supportive vitamin/mineral supplements;
  3. extracting all root canaled teeth using proper finish protocol;
  4. testing and treating cavitations and amalgam tattoos where relevant;
  5. performing supportive supplementation and periodic monitoring tests; and
  6. evaluating need for further treatment (not usually needed).

Note: After treatment of many cases of chronic autoimmune conditions such as MS, ALS, Parkinson’s, Alzheimer’s, CFS, lupus, rheumatoid arthritis, etc., it has been observed that often mercury, along with root canal toxicity or cavitation toxicity, is a major factor in these conditions, and most with these conditions improve after TDR if protocol is followed carefully.

Other measures in addition to TDR that have been found to help in treatment of MS in clinical experience include avoiding milk products, getting lots of sunlight, and supplementing with calcium AEP and alpha lipoic acid. Progesterone creme has been found to promote regrowth of myelin sheaths in animals.

Tests suggested by Huggins/Levy for evaluation and treatment of mercury toxicity:

  1. Hair element test (Note: Low hair mercury level does not indicate low body level. More than 3 essential minerals out of normal range indicates likely metals toxicity.)
  2. CBC blood test with differential and platelet count
  3. Blood serum profile
  4. Urinary mercury (Note: For person with average exposure with amalgam fillings, the average mercury level is 3 to 4 ppm. Lower levels than this likely means person is poor excretor and is probably accumulating mercury, often mercury toxic.)
  5. Fractionated porphyrin (Note: Test results sensitive to light, temperature, and shaking.)
  6. Individual tooth electric currents (Note: Replace high negative current teeth first.)
  7. Patient questionnaire on exposure and symptom history

Based on the known mechanisms of damage found in these conditions, the authors of the study suggest that supplementation with:

  • 100 mg MG,
  • 25 mg vit B6,
  • 10 mg vit B2,
  • 15 mg Zn,
  • 400 IU vit D and E,
  • 100 Se,
  • 180 mg EPA, and
  • 120 mg DHA per day (between 14 and 16 years of age)

may prevent MS and reduce further damage for those with the condition.

An Oregon researcher, Dr. R. Swank, found a significant correlation between MS and dietary fat. He developed a low fat diet, with animal meat mostly replaced by fish or fish oil (with EPA/DHA) and olive oil. Studies found the Swank diet effective at reducing the effects of MS. European studies have confirmed his findings regarding connection of MS to high fat animal diets, and effectiveness of the Swank diet. Studies have also found deficiency in essential fatty acids to be associated with demyelination, again consistent with the Swank findings. Studies have also found protective effects of diets high in vegetable protein, dietary fiber, cereal fiber, vitamin C, vitamin D, thiamin, riboflavin, calcium, potassium, and magnesium. A study found increased vitamin D helpful in reducing MS effects. Additionally curcumin and Acetyl-L-Carnitine were found by studies to be neuroprotective. Both reduce inflammation/oxidative stress. Extracts of green tea (EGCG) and black tea (theaflavins) also have been found to be highly effective at reducing inflammatory effects. A study comparing alternative treatment of MS to conventional treatment found the majority using alternative treatments was satisfied with his or her treatment and much lower adverse health effects from alternative treatments compared to convention treatments. Amalgam replacement was one of the alternatives used by some.


  1. Ruprecht J. Dimaval Scientific Monograph. 6th ed. Heyl Corporation; 1997.
  2. Hussain S, et al. Mercuric chloride-induced reactive oxygen species and its effect on antioxidant enzymes in different regions of rat brain. J Environ Sci Health B. 1997; 32(3): 395-409.
  3. Bulat P. Activity of Gpx and SOD in workers occupationally exposed to mercury. Arch Occup Environ Health. 1998; 71: S37-9.
  4. Stohs SJ, Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radic Biol Med. 1995; 18(2): 321-36.
  5. Jay D. Glutathione inhibits SOD activity of Hg. Arch Inst Cardiol Mex. 1998; 68(6): 457-61.
  6. El-Demerdash FM. Effects of selenium and mercury on the enzymatic activities and lipid peroxidation in brain, liver, and blood of rats. J Environ Sci Health B. 2001; 36(4): 489-99.
  7. Tan S, et al. Oxidative stress induces programmed cell death in neuronal cells. J Neurochem. 1998; 71(1): 95-105.
  8. Matsuda T, Takuma K, Lee E, et al. Apoptosis of astroglial cells. Nippon Yakurigaku Zasshi. 1998; 112 (1): 24.
  9. Lee YW, Ha MS, Kim YK. Role of reactive oxygen species and glutathione in inorganic mercury-induced injury in human glioma cells. Neurochem Res. 2001; 26(11): 1187-93.
  10. Ho PI, Ortiz D, Rogers E, Shea TB. Multiple aspects of homocysteine neurotoxicity: glutamate excitotoxicity, kinase hyperactivation and DNA damage. J Neurosci Res. 2002; 70(5): 694-702.
  11. Nylander M, et al. Mercury concentrations in the human brain and kidneys and exposure from amalgam fillings. Swed Dent J. 1987; 11: 179-187.
  12. Eggleston DW, et al. Correlation of dental amalgam with mercury in brain tissue. J Prosthet Dent. 1987; 58(6): 704-7.
  13. Weiner JA, et al. The relationship between mercury concentration in human organs and predictor variables. Sci Tot Environ. 1993; 138(1-3):101-115.
  14. Scifo R, Marchetti B, et al. Opioid-immune interactions in autism: behavioral and immunological assessment during a double-blind treatment with naltexone. Ann Ist Super Sanita. 1996; 32(3): 351-9.
  15. Eedy DJ, Burrows D, Dlifford T, Fay A. Elevated T cell subpopulations in dental students. J Prosthet Dent. 1990; 63(5): 593-6.
  16. Yonk LJ, et al. CD+4 helper T-cell depression in autism. Immunol Lett. 1990; 25(4): 341-5.
  17. Goyer RA. Toxic effects of metals. In: Cassarett, Doull, eds. Toxicology: The Basic Science of Poisons. 3rd ed. New York: MacMillan Publ. Co; 1986: 582-609.
  18. Galic N, Ferencic Z, et al. Dental amalgam mercury exposure in rats. Biometals. 1999; 12(3): 227-31.
  19. Arvidson B, Arvidsson J, Johansson K. Mercury deposits in neurons of the trigeminal ganglia after insertion of dental amalgam in rats. Biometals. 1994; 7(3): 261-3.
  20. Danscher G, Horsted-Bindslev P, Rungby J. Traces of mercury in organs from primates with amalgam fillings. Exp Mol Pathol. 1990; 52(3): 291-9.
  21. Hahn L, et al. Distribution of mercury released from amalgam fillings into monkey tissues. FASEB J. 1990; 4: 5536.
  22. Cade JR, et al. Autism and schizophrenia linked to malfunctioning enzyme for milk protein digestion. Autism. 1999.
  23. Sun ZJ, Cade JR, et al. Beta-casomorphin induces Fos-like immunoreactivity in discrete brain regions relevant to schizophrenia and autism. Autism. 1999; 3(1): 67-83.
  24. Cade JR, Sun Z. A peptide found in schizophrenia and autism causes behavioral changes in rats. Autism. 1999; 3(1): 85-95.
  25. Leboyer M, et al. Opiate hypothesis in infantile autism? Therapeutic trials with naltrexone. Encephale. 1993; 19(2): 95-102.
  26. Lucarelli S, et al. Food allergy and infantile autism. Panminerva Med. 1995; 37(3): 137-41.
  27. Reichelt KL. Biochemistry and psycholphisiology of autistic syndromes. Tidsskr Nor Laegeforen. 1994; 114(12): 1432-4.
  28. Reichelt KL, et al. Biologically active peptide-containing fractions in schizophrenia and childhood autism. Adv Biochem Psychopharmocol. 1981; 28: 627-43.
  29. Lucarelli S, Cardi E, et al. Food allergy and infantile autism. Panminerva Med. 1995; 37(3): 137-41.
  30. Shel L. Autistic disorder and the endogenous opioid system. Med Hypotheses. 1997; 48(5): 413-4.
  31. Ihara M, Makino F, et al. Gluten sensitivity in Japanese patients with adult-onset cerebellar ataxia. Intern Med. 2006; 45(3): 135-40.
  32. Pengiran Tengah CD, Lock RJ, Unsworth DJ, Wills AJ. Multiple sclerosis and occult gluten sensitivity. Neurology. 2004; 62(12): 2326-7.
  33. Schmidt F, et al. Mercury in urine of employees exposed to magnetic fields. Tidsskr Nor Laegeforen. 1997; 117(2): 199-202.
  34. Sheppard AR, Eisenbud M. Biological Effects of Electric and Magnetic Fields of Extremely Low Frequency. New York University Press; 1977.
  35. Ortendahl T W, Hogstedt P, Holland RP. Mercury vapor release from dental amalgam in vitro caused by magnetic fields generated by CRT’s. Swed Dent J. 1991: 31.
  36. Olssonl S. Release of elements due to electrochemical corrosion of dental amalgam. J of Dental Research. 1994; 73: 33-43.
  37. Markovich, et al. Heavy metals (Hg,Cd) inhibit the activity of the liver and kidney sulfate transporter Sat-1. Toxicol App Pharmacol. 1999; 154(2): 181-7.
  38. McFadden SA. Xenobiotic metabolism and adverse environmental response: Sulfur-dependent detox pathways. Toxicology. 1996; 111(1-3): 43-65.
  39. Langley-Evans SC, et al. SO2: A potent glutathion depleting agent. Comp Biochem Physiol Pharmocol Toxicol Endocrinol. 1996; 114(2): 89-98.
  40. Alberti A, Pirrone P, Elia M, Waring RH, Romano C. Sulphation deficit in “low-functioning” autistic children. Biol Psychiatry. 1999; 46(3): 420-4.
  41. Henriksson J, Tjalve H. Uptake of inorganic mercury in the olfactory bulbs via olfactory pathways in rats. Environ Res. 1998; 77(2): 130- 40.
  42. Huggins HA, Levy TE. Uniformed Consent: The Hidden Dangers in Dental Care. Hampton Roads Publishing Company Inc.; 1999.
  43. Ziff S, Ziff M. Infertility and Birth Defects: Is Mercury from Dental Fillings a Hidden Cause? Orlando, FL: Bio-Probe; 1987.
  44. Rodgers JS, Hocker JR, et al. Mercuric ion inhibition of eukaryotic transcription factor binding to DNA. Biochem Pharmacol. 2001; 61(12): 1543-50.
  45. Hansen K, et al. A survey of metal induced mutagenicity in vitro and in vivo. J Amer Coll Toxicol. 1984; 3: 381-430.
  46. Knapp LT, Klann E. Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J Biol Chem. 2000.
  47. Jenner P. Oxidative mechanisms in PD. Mov Disord. 1998; 13(1): 24-34.
  48. Rajanna B, et al. Modulation of protein kinase C by heavy metals. Toxicol Lett. 1995; 81(2-3): 197-203.
  49. Badou A, et al. HgCl2-induced IL-4 gene expression in T cells involves a protein kinase C-dependent calcium influx through L-type calcium channels. J Biol Chem. 1997; 272(51): 32411-8.
  50. Veprintsev DB. Pb2+ and Hg2+ binding to alpha-lactalbumin. Biochem Mol Biol Int. 1996; 39(6): 1255-65.
  51. Buzard GS, Kasprzak KS. Possible roles of nitric oxide and redox cell signaling in metal-induced toxicity and carcinogenesis: A review. Environ Pathol Toxicol Oncol. 2000; 19(3): 179-99.
  52. Pelletier L, et al. In vivo self-reactivity of mononuclear cells to T cells and macrophages exposed to Hg Cl2. Eur J Immun. 1985: 460-465.
  53. Pelletier L, et al. Autoreactive T cells in mercury induced autoimmune disease. J Immunol. 1986; 137(8): 2548-54.
  54. Kubicka M, et al. Autoimmune disease induced by mercuric chloride. Int Arch Allergy Immunol. 1996; 109(1): 11-20.
  55. Arvidson K. Corrosion studies of dental gold alloy in contact with amalgam. Swed Dent J. 1984; 68: 135-139.
  56. Skinner EW. The Science of Dental Materials. 4th ed. Philadelphia: W. B. Saunders Co. 1957: 284-285.
  57. Kingman A, Albertini T, Brown LJ. Mercury concentrations in urine and blood associated with amalgam exposure in the U.S. military population. J Dent Res. 1998; 77(3): 461-71.
  58. Kawada J, et al. Effects of inorganic and methyl mercury on thyroidal function. J Pharmacobiodyn. 1980; 3(3): 149-59.
  59. Heintze, et al. Methylation of Mercury from dental amalgam and mercuric chloride by oral Streptococci. Scan J Dent Res. 1983; 91: 150-152.
  60. Rowland, Grasso, Davies. The methylation of mercuric chloride by human intestinal bacteria. Experientia Basel. 1975; 31: 1064-1065.
  61. Hamdy MK, et al. Formation of methyl mercury by bacteria. App Microbiol. 1975.
  62. Brun A, Abdulla M, Ihse I, Samuelsson B. Uptake and localization of mercury in the brain of rats after prolonged oral feeding with mercuric chloride. Histochemistry. 1976; 47(1): 23-9.
  63. Ludwicki JK. Studies on the role of gastrointestinal tract contents in the methylation of inorganic mercury compounds. Bull Env Contam Toxicol. 1989; 42: 283-288.
  64. Choi SC, Bartha R. Cobalamin-mediated mercury methylation by Desulfovibrio desulfuricans LS. Appl Environ Microbiol. 1993; 59(1): 290-5.
  65. Wang J, Liu Z. In vitro study of strepcoccus mutans in the plaque on the surface of amalgam fillings on the conversion of inorganic mercury to organic mercury. Shanghai Kou Qiang Yi Xue. 2000; 9(2): 70-2.
  66. Lund ME, et al. Treatment of acute MeHg poisoning by NAC. J Toxicol Clin Toxicol. 1984; 22(1): 31-49.
  67. Livardjani F, Ledig M, Kopp P, Dahlet M, Leroy M, Jaeger A. Lung and blood superoxide dismustase activity in mercury vapor exposed rats: Effect of N-acetylcysteine treatment. Toxicology. 1991; 66(3): 289-95.
  68. Nicole, et al. Direct evidence for glutathione as mediator of apoptosis in neuronal cells. Biomed Pharmacother. 1998; 52(9): 349-55.
  69. Spencer JP, et al. Cysteine & GSH in PD, mechanisms involving ROS. J Neurochem. 1998; 71(5): 2112-22.
  70. Bains JS, et al. Neurodegenerative disorders in humans and role of glutathione in oxidative stress mediated neuronal death. Brain Res Rev. 1997; 25(3): 335-58.
  71. Medina S, Martinez M, Hernanz A. Antioxidants inhibit the human cortical neuron apoptosis induced by hydrogen peroxide, tumor necrosis factor alpha, dopamine and beta-amyloid peptide 1-42. Free Radic Res. 2002; 36(11): 1179-84.
  72. Pocernich CB, et al. Glutathione elevation and its protective role in acrolein-induced protein damage in synaptosomal membranes: relevance to brain lipid peroxidation in neurodegenerative disease. Neurochem Int. 2001; 39(2): 141-9.
  73. Offen D, et al. Use of thiols in treatment of PD. Exp Neurol. 1996; 141(1): 32-9.
  74. Pearce RK, Owen A, Daniel S, Jenner P, Marsden CD. Alterations in the distribution of glutathione in the substantia nigra in Parkinson’s disease. J Neural Transm. 1997; 104(6-7): 661-77.
  75. Shen XM, et al. Neurobehavioral effects of NAC conjugates of dopamine: Possible relevance for Parkinson’s disease. Chem Res Toxicol. 1996; 9(7): 1117-26.
  76. Li H, Shen XM, Dryhurst G. Brain mitochondria catalyze the oxidation of 7-(2-aminoethyl)-3,4-dihydro-5-hydroxy-2H-1,4-benzothiazine-3-carboxyli c acid (DHBT-1) to intermediates that irreversibly inhibit complex I and scavenge glutathione: potential relevance to the pathogenesis of Parkinson’s disease. J Neurochem. 1998; 71(5): 2049-62.
  77. Araragi S, Sato M, et al. Mercuric chloride induces apoptosis via a mitochondrial-dependent pathway in human leukemia cells. Toxicology. 2003; 184(1): 1-9.
  78. Stejskal VDM, et al. MELISA: Tool for the study of metal allergy. Toxicology in Vitro. 1994; 8(5): 991-1000.
  79. Stejskal VD, Danersund A, Lindvall A, et al. Metal-specific lymphocytes: biomarkers of sensitivity in man. Neuroendocrinology Letters. 1998.
  80. Thompson, Markesbery, et al. Regional brain trace-element studies in Alzheimer’s disease. Neurotoxicology. 1988; 9(1): 1-7.
  81. Hock, et al. Increased blood mercury levels in Alzheimer’s patients. Neural Transm. 1998; 105: 59-68.
  82. Bjorkman L, et al. Mercury in saliva and feces after removal of amalgam fillings. J Dent Res. 1996; 75: 38.
  83. Sandborgh-Englund G, et al. Mercury in biological fluids after amalgam removal. J Dental Res. 1998; 77(4): 615-24.
  84. Berglund A, Molin M. Mercury levels in plasma and urine after removal of all amalgam restorations: the effect of using rubber dams. Dent Mater. 1997; 13(5): 297-304.
  85. Begerow J, et al. Long-term mercury excretion in urine after removal of amalgam fillings. Int Arch Occup Health. 1994; 66: 209-212.
  86. Veltman JC, et al. Alterations of heme, cytochrome P-450, and steroid metabolism by mercury in rat adrenal gland. Arch Biochem Biophys. 1986; 248(2): 467-78.
  87. Riedl AG, et al. P450 and hemeoxygenase enzymes in the basal ganglia and their roles in Parkinson’s disease. Adv Neurol. 1999; 80: 271-86.
  88. Zamm AV. Dental mercury: A factor that aggravates and induces xenobiotic intolerance. J Orthmol Med. 1991; 6(2): 67-77.
  89. Itoh K. Defects of cytochrome c oxidase in the substantia nigra of Parkinson’s disease: An immunohistochemical and morphometric study. Mov Disord. 1997; 12(1): 9-16.
  90. Smart ER, et al. Resolution of lichen planus following removal of amalgam restorations. Br Dent J. 1995; 178(3): 108-112.
  91. Markow H. Regression from orticaria following dental filling removal. New York State J Med. 1943: 1648-1652.
  92. Sasaki G, et al. Three cases of oral lichenosis caused by metallic fillings. J Dermatol. 1996; 12: 890-892.
  93. Bratel J, et al. Effect of replacement of dental amalgam on OLR. Journal of Dentistry. 1996; 24(1-2): 41-45.
  94. Ostman PO, et al. Clinical & histologic changes after removal of amalgam. Oral Surgery, Oral Medicine, and Endodontics. 1996; 81(4): 459-465.
  95. Koch P, et al. Oral lesions and symptoms related to metals. J Dermatol. 1999; 41(3): 422-430.
  96. Freeman S, et al. Oral lichenoid lesions caused by allergy to mercury in amalgam. Contact Dermatitis. 1995; 33(6): 423-7.
  97. Jolly M, et al. Amalgam related chronic ulceration of oral mucosa. Br Dent J. 1986; 160: 434-437.
  98. Camisa C, et al. Contact hypersensitivity to mercury. Cutis. 1999; 63(3): 189.
  99. Lindqvist B, et al. Effects of removing amalgam fillings from patients with diseases affecting the immune system. Med Sci Res. 1996; 24(5): 355-356.
  100. Tandon L, et al. Elemental imbalance studies by INAA on ALS patients. J Radioanal Nuclear Chem. 1995; 195(1): 13-19.
  101. Mano Y, et al. Mercury in the hair of ALS patients. Rinsho Shinkeigaku. 1989; 29(7): 844-848.
  102. Khare, et al. Trace element imbalances in ALS. Neurotoxicology. 1990; 11: 521-532.
  103. Carpenter DO. Effects of metals on the nervous system of humans and animals. Int J Occup Med Environ Health. 2001; 14(3): 209-18.
  104. Berglund F. Case Reports Spanning 150 Years on the Adverse Effects of Dental Amalgam. Orlando, FL: Bio-Probe; 1995.
  105. Lichtenberg HJ. Elimination of symptoms by removal of dental amalgam from mercury poisoned patients. J Orthomol Med. 1993; 8:145-148.
  106. Lichtenberg HJ. Symptoms before and after proper amalgam removal in relation to serum-globulin reaction to metals. J Orthomol Med. 1996; 11(4): 195-203.
  107. Goldberg AF, et al. Effect of amalgam restorations on whole body potassium and bone mineral content in older men. Gen Dent. 1996; 44(3): 246-8.
  108. Schirrmacher K. Effects of lead, mercury, and methyl mercury on gap junctions and [Ca2+]I in bone cells. Calcif Tissue Int. 1998; 63(2): 134-9.
  109. Redhe O, et al. Recovery from ALS after removal of dental amalgam fillings. Int J Risk & Safety in Med. 1994; 4: 229-236.
  110. Seidler, et al. Possible environmental factors for Parkinson’s disease. Neurology. 1996; 46(5): 1275-1284.
  111. Nylander M, et al. Mercury and selenium concentrations and their interrelations in organs from dental staff and the general population. Br J Ind Med. 1991; 48(11): 729-34.
  112. Siblerud RL, et al. Evidence that mercury from silver fillings may be an etiological factor in multiple sclerosis. Sci Total Environ. 1994; 142(3): 191-205.
  113. Siblerud RL, Kienholz E. Evidence that mercury from dental amalgam may cause hearing loss in MS patients. J Orthomol Med. 1997; 12(4): 240-4.
  114. Rothwell JA, Boyd PJ. Amalgam dental fillings and hearing loss. International Journal of Audiology. 2008; 47: 770-776.
  115. Siblerud RL, et al. Psychometric evidence that mercury from dental fillings may be a factor in depression, anger, and anxiety. Psychol Rep. 1994; 74(1).
  116. Quig D. Cysteine metabolism and metal toxicity. Altern Med Rev. 1998; 3(4): 262-270.
  117. de Ceaurriz J, et al. Role of gamma-glutamyltraspeptidase(GGC) and extracellular glutathione in dissipation of inorganic mercury. J Appl Toxicol. 1994; 14(3): 201.
  118. Berndt WO, et al. Renal glutathione and mercury uptake. Fundam Appl Toxicol. 1985; 5(5): 832-9.
  119. Zalups RK, Barfuss DW. Accumulation and handling of inorganic mercury in the kidney after co-administration with glutathione. J Toxicol Environ Health. 1995; 44(4): 385-99.
  120. Clarkson TW, et al. Billiary secretion of glutathione-metal complexes. Fundam Appl Toxicol. 1985; 5(5): 816-31.
  121. Glavinskiaia TA, et al. Complexons in the treatment of lupus erghematousus. Dermatol Venerol. 1980; 12: 24-28.
  122. Cooper GS, Parks CG, et al. Occupational risk factors for the development of systemic lupus erythematosus. J Rheumatol. 2004; 31(10): 1928-33.
  123. Aschner M, et al. Metallothionein induction in fetal rat brain by in utero exposure to elemental mercury vapor. Brain Res. 1997; 778(1): 222-32.
  124. Aschner M, Rising L, Mullaney KJ. Differential sensitivity of neonatal rat astrocyte cultures to mercuric chloride (MC) and methylmercury (MeHg): Studies on K+ and amino acid transport and metallothionein (MT) induction. Neurotoxicology. 1996; 17(1): 107-16.
  125. O’Halloran TV. Transition metals in control of gene expression. Science. 1993; 261(5122): 715-25.
  126. Matts RL, Schatz JR, Hurst R, Kagen R. Toxic heavy metal ions inhibit reduction of disulfide bonds. J Biol Chem. 1991; 266(19):12695-702.
  127. Boot JH. Effects of SH-blocking compounds on the energy metabolism in isolated rat hepatocytes. Cell Struct Funct. 1995; 20(3): 233-8.
  128. Baauweegers HG, Troost D. Localization of metallothionein in the mammilian central nervous system. Biol Signals. 1994; 3:181-7.
  129. Tibbling L, et al. Immunolocial and brain MRI changes in patients with suspected metal intoxication. Int J Occup Med Toxicol. 1995; 4(2): 285-294.
  130. Ronnback L, et al. Chronic encephalopaties induced by low doses of mercury or lead. Br J Ind Med. 1992; 49: 233-240.
  131. Langauer-Lewowicka H. Changes in the nervous system due to occupational metallic mercury poisoning. Neurol Neurochir Pol. 1997; 31(5): 905-13.
  132. Kim P, Choi BH. Selective inhibition of glutamate uptake by mercury in cultured mouse astrocytes. Yonsei Med J. 1995; 36(3): 299-305.
  133. Brookes N. In vitro evidence for the role of glutatmate in the CNS toxicity of mercury. Toxicology. 1992; 76(3): 245-56.
  134. Albrecht J, Matyja E. Glutamate: A potential mediator of inorganic mercury toxicity. Metab Brain Dis. 1996; 11: 175-84.
  135. Singh I, Pahan K, Khan M, Singh AK. Cytokine-mediated induction of ceramide production is redox-sensitive. Implications to proinflammatory cytokine-mediated apoptosis in demyelinating diseases. J Biol Chem. 1998; 273(32): 20354-62.
  136. Pahan K, Raymond JR, Singh I. Inhibition of phosphatidylinositol 3-kinase induces nitric-oxide synthase in lipopolysaccharide- or cytokine-stimulated C6 glial cells. J Biol Chem. 1999; 274: 7528-7536.
  137. Xu J, Yeh CH, et al. Involvement of de novo ceramide biosynthesis in tumor necrosis factor-alpha/cycloheximide-induced cerebral endothelial cell death. J Biol Chem. 1998; 273(26): 16521-6.
  138. Dbaibo GS, El-Assaad W, et al. Ceramide generation by two distinct pathways in tumor necrosis factor alpha-induced cell death. FEBS Lett. 2001; 503(1): 7-12.
  139. Liu B, Hannun YA, et al. Glutathione regulation of neutral sphingomyelinase in tumor necrosis factor-alpha-induced cell death. J Biol Chem. 1998; 273(18): 11313-20.
  140. Noda M, Wataha JC, et al. Sublethal, 2-week exposures of dental material components alter TNF-alpha secretion of THP-1 monocytes. Dent Mater. 2003; 19(2): 101-5.
  141. Kim SH, Johnson VJ, Sharma RP. Mercury inhibits nitric oxide production but activates proinflammatory cytokine expression in murine macrophage: Differential modulation of NF-kappaB and p38 MAPK signaling pathways. Nitric Oxide. 2002; 7(1): 67-74.
  142. Dastych J, Metcalfe DD, et al. Murine mast cells exposed to mercuric chloride release granule-associated N-acetyl-beta-D-hexosaminidase and secrete IL-4 and TNF-alpha. J Allergy Clin Immunol. 1999; 103(6): 1108-14.
  143. Tortarolo M, Veglianese P, et al. Persistent activation of p38 mitogen-activated protein kinase in a mouse model of familial amyotrophic lateral sclerosis correlates with disease progression. Mol Cell Neurosci. 2003; 23(2): 180-92.
  144. Enestrom S, et al. Does amalgam affect the immune system? Int Arch Allergy Immunol. 1995; 106: 180-203.
  145. Sallsten G, et al. Mercury in cerebrospinal fluid in subjects exposed to mercury vapor. Environ Research. 1994; 65: 195-206.
  146. Ariza ME. Bijur GN, Williams MV. Lead and mercury mutagenesis: Role of H2O2, superoxide dismutase, and xanthine oxidase. Environ Mol Mutagen. 1998; 31(4): 352-61.
  147. Ariza ME, et al. Mercury mutagenisis. Biochem Mol Toxicol. 1999; 13(2): 107-12.
  148. Ariza ME, et al. Mutagenic effect of mercury. In Vivo. 1994; 8(4): 559-63.
  149. Langworth, et al. Effects of low exposure to inorganic mercury on the human immune system. Scand J Work Environ Health. 1993; 19(6): 405-413.
  150. Walum E, et al. Use of primary cultures to study astrocytic regulatory functions. Clin Exp Pharmoacol Physiol. 1995; 22: 284-7.
  151. Kerkhoff H, Troost D, Louwerse ES. Inflammatory cells in the peripheral nervous system in motor neuron disease. Acta Neuropathol. 1993; 85: 560-5.
  152. Appel Sh, Smith RG. Autoimmunity as an etiological factor in amyotrophic lateral sclerosis. Adv Neurol. 1995; 68: 47-57.
  153. Pons S, Torres-Aleman I. Insulin-like growth factor-I stimulates dephosphorylation of ikappa B through the serine phosphatase calcineurin. J Biol Chem. 2000; 275(49): 38620-5.
  154. Wenstrup, et al. Trace element imbalances in the brains of Alzheimer’s patients. Research. 1990; 533: 125-131.
  155. Lorscheider FL, Haley B, et al. Mercury vapor inhibits tubulin binding. FASEB J. 1995; 9(4): A-3485.
  156. Koller LD. Immunotoxicity of heavy metals. Int J of Immunopharmacology. 1980; 2: 269.
  157. Basun H, et al. Metals in plasma and cerebrospinal fluid in normal aging and Alzheimer’s disease. J Neural Transm Park Dis Dement Sect. 1991; 3(4): 231-58.
  158. Ngim CH, et al. Epidemiologic study on the association between body burden mercury level and idiopathic Parkinson’s disease. Neuroepidemiology. 1989; 8(3): 128-41.
  159. Siblerud RL. A comparison of mental health of multiple sclerosis patients with silver dental fillings and those with fillings removed. Psychol Rep. 1992; 70(3.2): 1139-51.
  160. Heo Y, Parsons PJ, Lawrence DA. Lead differentially modifies cytokine production in vitro and in vivo. Toxicol Appl Pharmacol. 1996; 138: 149-57.
  161. Murdoch RD, Pepys J. Enhancement of antibody and IgE production by mercury and platinum salts. Int Arch Allergy Appl Immunol. 1986; 80: 405-11.
  162. Ingalls TH. Clustering of multiple sclerosis in Galion, Ohio, 1982-1985. Amer J Forensic Med Pathol. 1989; 10: 213-5.
  163. Lu SC. Regulation of hepatic glutathione synthesis: current concepts and controversies. FASEB J. 1999; 13(10): 1169-83.
  164. Zulups RK, et al. Nephrotoxicity of inorganic mercury co-administered with L-cysteine. Toxicology. 1996; 109(1): 15-29.
  165. Perry TL, et al. Hallevorden-Spatz disease: Cysteine accumulation and cysteine dioxygenase deficiency. Ann Neural. 1985; 18(4): 482-489.
  166. Fabbri E, Caselli F, Piano A, Sartor G, Capuzzo A. Fluctuation of trace elements during methylmercury tox and chelation therapy. Hum Exp Toxicol. 1994; 13(12): 815-23.
  167. Danielsson BRG, et al. Ferotoxicity of inorganic mercury: Distribution and effects of nutrient uptake by placenta and fetus. Biol Res Preg Perinatal. 1984; 5(3): 102-109.
  168. Warren T. Beating Alzheimer’s. Avery Publishing Group; 1991.
  169. Palkiewicz P, Zwiers H, Lorscheider FL. ADP-ribosylation of brain neuronal proteins is altered by in vitro and in vivo exposure to inorganic mercury. Journal of Neurochemistry. 1994; 62(5): 2049-2052.
  170. Ziff M. Documented clinical side effects to dental amalgam. Adv Dent Res. 1992; 1(6): 131-134.
  171. Ziff S. Dentistry without Mercury. 8th ed. Orlando, FL: Bio-Probe, Inc.; 1996.
  172. Seidler, et al. Possible environmental or occupational factors for Parkinson’s disease. Neurology. 1996; 46(5): 1275-84.
  173. Sellars WA, Sellars R. Methyl mercury in dental amalgams in the human mouth. Journal of Nutritional & Environmental Medicine. 1996; 6(1): 33-37.
  174. Schofield P. Dementia associated with toxic causes and autoimmune disease. Int Psychogeriatr. 2005; 17(1): S129-47.
  175. Daunderer M. Improvement of nerve and immunological damages after amalgam removal. Amer J of Probiotic Dentistry and Medicine. 1991.
  176. Nicholson JK, et al. Cadmium and mercury exposure and nephrotoxicity. Nature. 1983; 304(5927): 633-5.
  177. Shenker BJ, et al. Immunotoxic effects of mercuric compounds on human lymphocytes and monocytes: Alterations in cell viability. Immunopharmacologicol Immunotoxical. 1992; 14(3): 555-77.
  178. Miller MA, et al. Mercuric chloride induces apoptosis in human T lymphocytes. Toxicol App Pharmacol. 1998; 153(2): 250-7.
  179. Rossi AD, Viviani B, Vahter M. Inorganic mercury modifies Ca2+ signals, triggers apoptosis, and potentiates NMDA toxicity in cerebral granule neurons. Cell Death and Differentiation. 1997; 4(4): 317-24.
  180. Goering PL, Thomas D, Rojko JL, Lucas AD. Mercuric chloride-induced apoptosis is dependent on protein synthesis. Toxicol Lett. 1999; 105(3): 183-95.
  181. Kantarjian A. A syndrome clinically resembling amyotrophic lateral sclerosis following chronic mercurialism. Neurology. 1961; 11: 639-644.
  182. Berglund F, Bjerner-Helm, Klock, et al. Improved health after removal of dental amalgam fillings. Swedish Assoc Of Dental Mercury Patients. 1998.
  183. Cooper GS, Dooley MA., et al. NIEHS: Occupational risk factors for the development of systemic lupus erythematosus. J Rheumatol. 2004; 31(10): 1928-33.
  184. Bigazzi PE. Autoimmunity and heavy metals. Lupus. 1994; 3: 449-453.
  185. Pollard KM, Pearson Dl, Hultman P. Lupus-prone mice as model to study xenobiotic-induced autoimmunity. Environ Health Perspect. 1999; 107(5): 729-735.
  186. Nielsen JB, Hultman P. Experimental studies on genetically determined susceptibility to mercury-induced autoimmune response. Ren Fail. 1999; 21(3-4): 343-8.
  187. Hultman P, Enestrom S. Mercury induced antinuclear antibodies in mice. Clinical and Exper Immunology. 1988; 71(2): 269-274.
  188. Robbins SM, Quintrell NA, Bishop JM. Mercuric chloride activates the Src-family protein tyrosine kinase, Hck in myelomonocytic cells. Eur J Biochem. 2000; 267(24): 7201-8.
  189. Via CS, Nguyen P, Silbergeld EK, et al. Low-dose exposure to inorganic mercury accelerates disease and mortality in acquired murine lupus. Environ Health Perspect. 2003; 111(10): 1273-7.
  190. Silbergeld EK, Silva IA, Nyland JF. Mercury and autoimmunity: implications for occupational and environmental health. Toxicol App Pharmacol. 2005 Sep 1; 207(2 Suppl):282-92.
  191. Constantinidis J, et al. Hypothesis regarding amyloid and zinc in the pathogenisis of Alzheimer’s disease. Alzheimer Dis Assoc Disord. 1991; 5(1): 31-35.
  192. Bjorklund G. Can mercury cause Alzheimer’s? Tidsskr Nor Laegeforen. 1991.
  193. Basun H, et al. Trace metals in plasma and cerebrospinal fluid in Alzheimer’s disease. J Neural Transm Park Dis Dement Sect. 1991; 3(4): 231.
  194. Finkelstein Y, et al. The enigma of Parkinsonism in chronic borderline mercury intoxication, resolved by challenge with penicillamine. Neurotoxicology. 1996; 17(1): 291-5.
  195. Gorell JM, et al. Occupational exposures to metals as risk factors for Parkinson’s disease. Neurology. 1997; 48(3): 650-8.
  196. Rybicki RA, et al. Parkinson’s disease mortality and the industrial use of heavy metals in Michigan. Mov Disord. 1993; 8(1): 87-92.
  197. Yamanaga H. Quantitative analysis of tremor in Minamata disease. Tokhoku J Exp Med. 1983; 141(1): 13-22.
  198. Shenker BJ, et al. Immunotoxic effects of mercuric compounds on human lymphoctes and monocytes: Alterations in cellular glutathione content. Immunopharmacol Immunotoxicol. 1993; 15(2.3): 273-90.
  199. Al-Saleh I, Shinwari N. Urinary mercury levels in females: Influence of dental amalgam fillings. Biometals. 1997; 10(4): 315-23.
  200. Zabinski Z, Dabrowski Z, Moszczynski P, Rutowski J. The activity of erythrocyte enzymes and basic indices of peripheral blood erythrocytes from workers chronically exposed to mercury vapors. Toxicol Ind Health. 2000; 16(2): 58-64.
  201. Eggar C, et al. Effect of lead on tetrahydrobiopterin metabolism: A mechanism for neurotoxicity. Clin Chim Acta. 1986; 161(1): 103-109.
  202. Smith I, et al. Pteridines and mono-amines: Relevance to neurological damage. Postgrad Med J. 1986; 62(724): 113-123.
  203. Kay AD, et al. Cerebrospinal fluid biopterin is decreased in Alzheimer’s disease. Arch Neurol. 1986; 43(10): 996-9.
  204. Yamiguchi T, et al. Effects of tyrosine administration on serum bipterin in patients with Parkinson’s disease and normal controls. Science. 1983; 219(4580): 75- 77.
  205. Woods JS, et al. Altered porphyrin metabolites as a biomarker of mercury exposure and toxicity. Physiol Pharmocol. 1996; 74(2): 210-15.
  206. Strubelt O, Kremer J, et al. Comparative studies on the toxicity of mercury, cadmium, and copper toward the isolated perfused rat liver. J Toxicol Environ Health. 1996; 47(3): 267-83.
  207. Kaliman PA, Nikitchenko IV, Sokol OA, Strel’chenko EV. Regulation of heme oxygenase activity in rat liver during oxidative stress induced by cobalt chloride and mercury chloride. Biochemistry (Mosc). 2001; 66(1): 77-82.
  208. Kumar SV, Maitra S, Bhattacharya S. In vitro binding of inorganic mercury to the plasma membrane of rat platelet affects Na+-K+-Atpase activity and platelet aggregation. Biometals. 2002; 15(1): 51-7.
  209. Chang LW. Neurotoxic effects of mercury. Environ Res. 1977; 14: 329.
  210. Kumar AR, Kurup PA. Inhibition of membrane Na+-K+ ATPase activity: A common pathway in central nervous system disorders. J Assoc Physicians India. 2002: 400-6.
  211. Kumar AR, Kurup PA. Membrane Na+ K+ ATPase inhibition related dyslipidemia and insulin resistance in neuropsychiatric disorders. Indian J Physiol Pharmacol. 2001; 45(3): 296-304.
  212. Danielsson BR, et al. Behavioral effects of prenatal metallic mercury inhalation exposure in rats. Neurotoxicol Teratol. 1993; 15(6): 391-6.
  213. Fredriksson A, et al. Prenatal exposure to metallic mercury vapour and methylmercury produce interactive behavioral changes in adult rats. Neurotoxicol Teratol. 1996; 18(2): 129-34.
  214. Robinson CJG, et al. Mercuric chloride induced anti-nuclear antibodies in mice. Toxicol App Pharmacol. 1986; 86:159-169.
  215. Andres P. IgA-IgG disease in the intestines of rats ingesting HgCl. Clin Immun Immunopath. 1984; 30: 488-494.
  216. Cossi, et al. Beneficial effect of human therapeutic IV-Ig in mercury induced autoimmune disease. Clin Exp Immunol. 1991.
  217. El-Fawai HA, Waterman SJ, De Feo A, Shamy MY. Neuroimmunotoxicology: Humoral Assessment of Neurotoxicity and Autoimmune Mechanisms. Contact Dermatitis. 1999; 41(1): 60-1.
  218. Eggleston DW. Effect of dental amalgam and nickel alloys on T-lympocytes. J Prosthet Dent. 1984; 51(5): 617-623.
  219. Tan XX, Tang C, Castoldi AF, Costa Lg. Effects of inorganic and organic mercury on intracellular calcium levels in rat T lymphocytes. J Toxicol Environ Health. 1993; 38(2): 159-70.
  220. Shenker BJ. Low-level MeHg exposure causes human T-cells to undergo apoptosis: evidence of mitochondrial dysfunction. Environ Res. 1998; 77(2): 149-159.
  221. Insug O, et al. Mercuric compounds inhibit human monocyte function by inducing apoptosis: Evidence for formation of reactive oxygen species(ROS), development of mitochondrial membrane permeability, and loss of reductive reserve. Toxicology. 1997; 124(3): 211-24.
  222. Knorr C, Geiger H, Flachenecker P. Complementary and alternative medicine for multiple sclerosis. Mult Scler. 2008; 14(8):1113-9.
  223. Nonaka S, et al. Lithium treatment protects neurons in CNS from glutamate induced excitibility and calcium influx. Neurobiology. 1998; 95(5): 2642-2647.
  224. Perlingeiro RC, et al. Polymorphonuclear phagentosis in workers exposed to mercury vapor. Int J Immounopharmacology. 1994; 16(12): 1011-7.
  225. Lai M, et al. Sensitivity of MS detections by MRI. Journal of Neurology, Neurosurgery, and Psychiatry. 1996; 60(3): 339-341.
  226. Newland MC, et al. Behavioral consequences of in utero exposure to mercury vapor in squirrel monkeys. Toxicol App Pharmacol. 1996; 139: 374-386.
  227. Warfvinge K, et al. Mercury distribution in neonatal cortical areas after exposure to mercury vapor. Environ Res. 1994; 67: 196-208.
  228. Hisatome I, Kurata Y, et al. Block of sodium channels by divalent mercury: role of specific cysteinyl residues in the P-loop region. Biophys J. 2000; 79(3): 1336-45.
  229. Bhattacharya S, Sen S et al. Specific binding of inorganic mercury to Na(+)-K(+)-ATPase in rat liver plasma membrane and signal transduction. Biometals. 1997; 10(3): 157-62.
  230. Anner BM, Moosmayer M, Imesch E. Mercury blocks Na-K-ATPase by a ligand-dependent and reversible mechanism. Am J Physiol. 1992; 262(5.2): F830-6.
  231. Anner BM, Moosmayer M. Mercury inhibits Na-K-ATPase primarily at the cytoplasmic side. Am J Physiol. 1992; 262(5.2): F84308.
  232. Wagner CA, Waldegger S, et al. Heavy metals inhibit Pi-induced currents through human brush-border NaPi-3 cotransporter in Xenopu oocytes. Am J Physiol. 1996; 271(4.2): F926-30.
  233. Lewis RN, Bowler K. Rat brain (Na+-K+) ATPase: Modulation of its ouabain-sensitive K+-PNPPase activity by thimerosal. Int J Biochem. 1983; 15(1): 5-7.
  234. Rajanna B, Hobson M, Harris L, Ware L, Chetty CS. Effects of cadmium and mercury on Na(+)-K(+) ATPase and uptake of 3H-dopamine in rat brain synaptosomes. Arch Int Physiol Biochem. 1990; 98(5): 291-6.
  235. Hobson M, Rajanna B. Influence of mercury on uptake of dopamine and norepinephrine. Toxicol Letters. 1985; 27(2-3): 7-14.
  236. McKay SJ, Reynolds JN, Racz WJ. Effects of mercury compounds on the spontaneous and potassium-evoked release of [3H] dopamine from mouse striatal slices. Can J Physiol Pharmacol. 1986; 64(12):1507-14.
  237. Scheuhammer AM, Cherian MG. Effects of heavy metal cations, sulfhydryl reagents and other chemical agents on striatal D2 dopamine receptors. Biochem Pharmacol. 1985; 34(19): 3405-13.
  238. Hoyt KR, et al. Mechanisms of dopamine-induced cell death and differences from glutamate induced cell death. Exp Neurol. 1997; 143(2): 269-81.
  239. Offen D, et al. Antibodies from ALS patients inhibit dopamine release mediated by L-type calcium channels. Neurology. 1998; 51(4): 1100-3.
  240. Mai J, Sorensen PS, Hansen JC. High dose antioxidant supplementation to MS patients. Effects on glutathione peroxidase, clinical safety, and absorption of selenium. Biol Trace Elem Res. 1990; 24(2): 109-17.
  241. Huggins HA, TE Levy. Cerebrospinal fluid protein changes in MS after dental amalgam removal. Alternative Med Rev. 1998; 3(4): 295-300.
  242. Bucio L, et al. Uptake, cellular distribution and DNA damage produced by mercuric chloride in a human fetal hepatic cell line. Mutat Res. 1999; 423(1-2): 65-72.
  243. Ho PI, Ortiz D, Rogers E, Shea TB. Multiple aspects of homocysteine neurotoxicity: Glutamate excitotoxicity, kinase hyperactivation and DNA. J Neurosci Res. 2002; 70(5): 694-702.
  244. Snyder RD, Lachmann PJ. Thiol involvement in the inhibition of DNA repair by metals in mammalian cells. Source Mol Toxicol. 1989; 2(2): 117-28.
  245. Verschaeve L, et al. Comparative in vitro cytogenetic studies in mercury-exposed human lymphocytes. Muta Res. 1985; 157(2-3): 221-6.
  246. Verschaeve L. Genetic damage induced by low level mercury exposure. Envir Res. 1976; 12: 306-10.
  247. Hock C, et al. Increased blood mercury levels in patients with Alzheimer’s disease. J Neural Transm. 1998; 105(1): 59-68.
  248. Chang LW. Neurotoxic effects of mercury. Environ Res. 1977; 14(3): 329-73.
  249. Klinghardt D, Mercola J. Mercury toxicity and systemic elimination agents. J of Nutritional and Environmental Medicine. 2001; 11: 53-62.
  250. Soderstrom S, Fredriksson A, Dencker L, Ebendal T. The effect of mercury vapor on cholinergic neurons in the fetal brain. Brain Research & Developmental Brain Res. 1995; 85: 96-108.
  251. Abdulla EM, et al. Comparison of neurite outgrowth with neurofilament protein levels in neuroblastoma cells following mercuric oxide exposure. Clin Exp Pharmocol Physiol. 1995; 22(5): 362-3.
  252. Leong CC, Syed NI, Lorscheider FL. Retrograde degeneration of neurite membrane structural integrity of nerve growth cones following in vitro exposure to mercury. Neuroreport. 2001; 12(4): 733-7.
  253. Stejskal VDM, et al. Mercury-specific Lymphocytes: an indication of mercury allergy in man. J of Clinical Immunology. 1996; 16(1): 31-40.
  254. Kubicka-Muranyi M, et al. Systemic autoimmune disease induced by mercuric chloride. Int Arch Allergy Immunol. 1996; 109(1):11-20.
  255. Goldman M, et al. Chemically induced autoimmunity. Immunology Today. 1991; 12: 223.
  256. Warfyinge K, et al. Systemic autoimmunity due to mercury vapor exposure in genetically susceptible mice. Toxicol App Pharmacol. 1995; 132(2): 299-309.
  257. Bagenstose LM, et al. Mercury induced autoimmunity in humans. Immunol Res. 1999; 20(1): 67-78.
  258. Daum JR. Immunotoxicology of mercury and cadmium on B-lymphocytes. Int J Immunopharmacol. 1993; 15(3): 383-94.
  259. Johansson U, et al. The genotype determines the B cell response in mercury-treated mice. Int Arch Allergy Immunol. 1998; 116(4): 295-305.
  260. Malt UF, et al. Physical and mental problems attributed to dental amalgam fillings. Psychosomatic Medicine. 1997; 59: 32-41.
  261. Engel P. Beobachtungen uber die gesundheit vor und nach amalgamentfernug. Schweiz Monatschr Zuhbmed. 1998; 108(8).
  262. Aminzadeh KK, Etminan M. Dental amalgam and multiple sclerosis: a systematic review and meta-analysis. J Public Health Dent. 2007; 67(1): 64-6.
  263. Bangsi D, Krewski D. Dental amalgam and multiple sclerosis: A case-control study in Montreal, Canada. Int J Epidemiol. 1998; 27(4): 667-71.
  264. McGrother CW, Baird WO. Multiple sclerosis, dental caries and fillings: A case-control study. Br Dent J. 1999; 187(5): 261-264.
  265. Mauch E, et al. Umweltgifte und multiple sklerose. Der Allgremeinarzt. 1996; 20: 2226-2220.
  266. Arvidson B. Inorganic mercury is transported from muscular nerve terminals to spinal and brainstem motorneurons. Muscle Nerve. 1992; 15(10):1089-94.
  267. Mitchell JD. Heavy metals and trace elements in amyotrophic lateral sclerosis. Neurol Clin. 1987; 5(1): 43-60.
  268. Su M, et al. Selective involvement of large motor neurons in the spinal cord of rats treated with methylmercury. J Neurol Sci. 1998; 156(1):12-7.
  269. Baasch E. Is multiple sclerosis a mercury allergy? Schweiz arch Neurol Neurochir Psichiatr. 1966; 98: 1-19.
  270. Clausen J. Mercury and MS. Acta Neurol Scand. 1993; 87: 461-464.
  271. Le Quesne P. Metal-induced diseases of the nervous system. Br J Hosp Med. 1982; 28: 534-38.
  272. Danscher G, et al. Localization of mercury in the CNS. Environ Res. 1986; 41: 29-43.
  273. Danscher G, Horsted-Bindslev P, Rungby J. Traces of mercury in organs from primates with amalgam fillings. Exp Mol Pathol. 1990; 52(3): 291-9.
  274. Pamphlett R, et al. Entry of low doses of mercury vapor into the nervous system. Neurotoxicology. 1998; 19(1): 39-47.
  275. Pamphlett R, et al. Oxidative damage to nucleic acids in motor neurons containing Hg. J Neurol Sci. 1998; 159(2):121-6.
  276. Pamphlett R, Waley P. Motor neuron uptake of low dose inorganic mercury. J Neurol Sci. 1996; 135: 63-67.
  277. Schionning JD, Danscher G. Autometallographic inorganic mercury correlates with degenerative changes in dorsal root ganglia of rats intoxicated with organic mercury. APMIS. 1999; 107(3): 303-10.
  278. McKeever P, et al. Patterns of antigenic expression in human glioma cells. Crit Rev Neurobiology. 1991; 6: 119-147.
  279. Arvidson B, Arvidsson J, Johansson K. Mercury deposits in neurons of the trigeminal ganglia after insertion of dental amalgam in rats. Biometals. 1994; 7 (3): 261-263.
  280. Arvidson B. Inorganic mercury is transported from muscular nerve terminasl to spinal and brainstem motorneurons. Muscle Nerve. 1992; 15: 1089-94.
  281. Arvidson B, et al. Retograde axonal transport of mercury in primary sensory neurons. Acta Neurol Scand. 1990; 82: 324-237.
  282. Candura SM, et al. Effects of mercuric chloride and methyl mercury on cholinergic neuromuscular transmission. Pharmacol Toxicol. 1997; 80(5): 218-24.
  283. Castoldi AF, et al. Interaction of mercury compounds with muscarinic receptor subtypes in the rat brain. Neurotoxicology. 1996; 17(3-4): 735-41.
  284. Wilkinson LJ, Waring RH. Cysteine dioxygenase: modulation of expression in human cell lines by cytokines and control of sulfate production. Toxicol In Vitro. 2002; 16(4): 481-3.
  285. Heafield MT, et al. Plasma cysteine and sulfate levels in patients with motor neuron disease, Parkinson’s disease, and Alzheimer’s disease. Neurosci Lett. 1990; 110(1-2): 216-20.
  286. Pean, et al. Pathways of cysteine metabolism in MND/ALS. J Neurol Sci. 1994; 124: 59-61.
  287. Steventon GB, et al. Xenobiotic metabolism in motor neuron disease. Lancet. 1988: 644-47.
  288. Gordon C, et al. Abnormal sulphur oxidation in systemic lupus erythrmatosus (SLE). Lancet. 1992; 339: 8784-6.
  289. Emory P, et al. Poor sulphoxidation in patients with rheumatoid arthritis. Ann Rheum Dis. 1992; 51: 318-20.
  290. Bradley H, et al. Sulfate metabolism is abnormal in patients with rheumatoid arthritis. Confirmation by in vivo biochemical findings. J Rheumatol. 1994; 21(7): 1192-6.
  291. Freitas AJ, et al. Effects of Hg2+ and CH3Hg+ on Ca2+ fluxes in the rat brain. Brain Res. 1996; 738(2): 257-64.
  292. Yallapragoda PR, et al. Inhibition of calcium transport by Hg salts in rat cerebellum and cerebral cortex. J App Toxicol. 1996; 164(4): 325-30.
  293. Chavez E, et al. Mitochondrial calcium release by Hg+2. J Biol Chem. 1988; 263: 8, 3582.
  294. Szucs A, et al. Effects of inorganic mercury and methylmercury on the ionic currents of cultured rat hippocampal neurons. Cell Mol Neurobiol. 1997; 17(3): 273-8.
  295. Busselberg D. Calcium channels as target sites of heavy metals. Toxicol Lett. 1995; 82-83: 255-61.
  296. Rossi AD, et al. Modifications of Ca2+ signaling by inorganic mercury in PC12 cells. FASEB J. 1993; 7: 1507-14.
  297. Eggleton P, et al. Pathophysicological roles of calreticulin in autoimmune disease. Scand J Immunol. 1999; 49(5): 466-73.
  298. Hill GS. Drug associated glomerulopathies. Toxicol Pathol. 1986; 14(1): 37-44.
  299. Boadi WY, et al. In vitro effect of mercury on enzyme activities and its accumulation in the first-trimester human placenta. Environ Res. 1992; 57(1): 96-106.
  300. Urbach J, et al. Effect of inorganic mercury on in vitro placental nutrient transfer and oxygen consumption. Reprod Toxicol. 1992; 6(1): 69-75.
  301. Karp WB, et al. Correlation of human placental enzymatic activity with tracemetal concentration in placenta. Environ Res. 1977; 13: 470-477.
  302. Boot JH. Effects of SH-blocking compounds on the energy metabolism and glucose uptake in isolated rat hepatocytes. Cell Struct Funct. 1995; 20(3): 233-8.
  303. Iioka H, et al. The effect of inorganic mercury on placental amino acid transport. Nippon Sanka Fujinka Gakkai Zasshi. 1987; 39(2): 202-6.
  304. Stejskal VDM, Danersund A, Lindvall A, et al. Metal-specific memory lymphocytes: Biomarkers of sensitivity in man. Neuroendocrinology Letters. 1999; 20: 289-98.
  305. Yaqob A, Danersund A, Stejskal VD, Lindvall A, Hudecek R, Lindh U. Metal-specific lymphocyte reactivity is down-regulated after dental metal replacement. Neuroendocrinology Letters. 2006; 27(1-2): 189-97.
  306. Bigazzi PL. Autoimmunity induced by metals. In: Chang L, ed. Toxicology of Metals. Lewis Publishers, CRC Press Inc; 1996: 835-52.
  307. Caron GA, et al. Lymphocytes transformation induced by inorganic and organic mercury. Int Arch Allergy. 1970; 37: 76-87.
  308. Nielsen NH, et al. The relationship between IgE-mediated and cell-mediated hypersensities. The Glostrup Allergy Study, Denmark. British J of Dermatol. 1996.
  309. Clauw DJ. The pathogenesis of chronic pain and fatigue syndromes: Fibromyalgia. Med Hypothesis. 1995; 44: 369-78.
  310. Sterzl I, Prochazkova J, Stejskal VDM, et al. Mercury and nickel allergy: risk factors in fatigue and autoimmunity. Neuroendocrinology Letters. 1999; 20: 221-228.
  311. Prochazkova J, Sterzl I, Kucerova H, Bartova J, Stejskal VD. The beneficial effect of amalgam replacement on health in patients with autoimmunity. Neuroendocrinology Letters. 2004; 25(3): 211-8.
  312. Scaronterzl I, Prochazkov J, Hrda P, Matucha P, Bartov J, Stejskal VDM. Removal of dental amalgam decreases anti-TPO and anti-Tg autoantibodies in patients with autoimmune thyroiditis. Neuroendocrinology Letters. 2006; 27(1): 25-30.
  313. Atchison WD. Effects of neurotoxicants on synaptic transmission. Neuroltoxicol Teratol. 1998; 10(5): 393-416.
  314. MacDonald EM, Mann AH, Thomas HC. Interferons as mediators of psychiatric morbidity. Lancet. 1978: 1175-78.
  315. Hickie I, Lloyd A. Are cytokines associated with neuropsychiatric syndrome in humans? Int J Immunopharm. 1995; 4: 285-294.
  316. Komaroff AL, Buchwald DS. Chronic fatigue syndrome: An update. Ann Rev Med. 1998; 49: 1-13.
  317. Buchwald DS, Wener MH, Kith P. Markers of inflammation and immune activation in CFS. J Rheumatol. 1997; 24: 372-76.
  318. Demitrack MA, Dale JK. Evidence for impaired activation of the hypothalamic-pituitary-adrenal axis in patients with chronic fatigue syndrome. J Clin Endocrinol Metabol. 1991; 73:1224-1234.
  319. Turnbull AV, Rivier C. Regulation of the HPA axis by cytokines. Brain Behav Immun. 1995; 20: 253-75.
  320. Ng TB, Liu WK. Toxic effect of heavy metals on cells isolated from the rat adrenal and testis. In Vitro Cell Dev Biol. 1990; 26(1): 24-8.
  321. Sterzl I, Fucikova T, Zamrazil V. The fatigue syndrome in autoimmune thyroiditis with polyglandular activation of autoimmunity. Vnitrni Lekarstvi. 1998; 44: 456-60.
  322. Sterzl I, Hrda P, Prochazkova J, Bartova J. Reactions to metals in patients with chronic fatigue and autoimmune endocrinopathy. Vnitrni Lekarstvi. 1999; 45(9): 527-31.
  323. Kolenic J, Palcakova D, Benicky L, Kolenicova M. The frequency of auto antibody occurrence in occupational risk (mercury). Prac Lek. 1993; 45(2): 75-77.
  324. Saito K. Analysis of a genetic factor of metal allergy-polymorphism of HLA-DR-DO gene. Kokubyo Gakkai Zasschi. 1996; 63: 53-69.
  325. Prochazkova J, Ivaskova E, Bartova J, Stejskal VDM. Immunogentic findings in patients with altered tolerance to heavy metals. Eur J Human Genet. 1998; 6:175.
  326. Prochazkova J, Bartova J, Ivaskova E, Kupkova L, Sterzl I, Stejskal VD. HLA-association in patients with intolerance to mercury and other metals in dental materials. Dis Markers. 2000; 16(3-4): 135-8.
  327. Prochazkova J, Bartova J, et al. HLA-association in patients with intolerance to mercury and other metals in dental materials. Dis Markers. 2000; 16(3-4): 135-8.
  328. Ionescu G. Heavy metal load with atopic dermatitis and psoriasis. Biol Med. 1996; 2: 65-68.
  329. Ionescu G. A subset of patients with common variable immunodeficiency. Blood. 1993; 82(1): 192-20.
  330. Stejskal J, Stejskal V. The role of metals in autoimmune diseases and the link to neuroendocrinology. Neuroendocrinology Letters. 1999. 20: 345-358.
  331. Plaitakis A, Constantakakis E. Altered metabolism of excitatory amino acids, N-acetyl-aspartate and acetyl-aspartyl-glutamate in amyotrophic lateral sclerosis. Brain Res Bull. 1993; 30(3-4): 381-6.
  332. Rothstein JD, Martin LJ, Kuncl RW. Decreased glutamate transport by the brain and spinal cord in ALS. New Engl J Med. 1992; 326: 1464-8.
  333. Leigh PN. Pathologic mechanisms in ALS and other motor neuron diseases. In: Calne DB, ed. Neurodegenerative Diseases. Philadelphia: WB Saunder Co; 1997: 473-88.
  334. Froissard P, et al. Role of glutathione metabolism in the glutamate-induced programmed cell death of neuronal cells. Eur J Pharmacol. 1997; 236(1): 93-99.
  335. Kim P, Choi BH. Selective inhibition of glutamate uptake by mercury in cultured mouse astrocytes. Yonsei Med J. 1995; 36(3): 299-305.
  336. Brookes N. In vitro evidence for the role of glutatmate in the CNS toxicity of mercury. Toxicology. 1992; 76(3): 245-56.
  337. Albrecht J, Matyja E. Glutamate: A potential mediator of inorganic mercury toxicity. Metab Brain Dis. 1996; 11: 175-84.
  338. Tirosh O, Sen CK, Roy S, Packer L. Cellular and mitochondrial changes in glutamate-induced HT4 neuronal cell death. Neuroscience. 2000; 97(3): 531-41.
  339. Folkers K, et al. Biochemical evidence for a deficiency of vitamin B6 in subjects reacting to MSL-Glutamate. Biochem Biophys Res Comm. 1981; 100: 972.
  340. Felipo V, et al. L-carnatine increases the affinity of glutamate for quisqualate receptors and prevents glutamate neurotoxicity. Neurochemical Research. 1994; 19(3): 373-377.
  341. Akaike A, et al. Protective effects of a vitamin-B12 analog (methylcobalamin, against glutamate cytotoxicity in cultured cortical neurons). European J of Pharmacology. 1993; 241(1):1-6.
  342. Adams CR, et al. Mercury intoxication simulating ALS. JAMA. 1983; 250(5): 642-5.
  343. Barber T. Inorganic mercury intoxication similar to ALS. J of Occup Med. 1978; 20: 667-9.
  344. Hu H, Abedi-Valugerdi M, Moller G. Pretreatment of lymphocytes with mercury in vitro induces a response in T cells from genetically determined low-responders and a shift of the interleukin profile. Immunology. 1997; 90(2):198-204.
  345. Hu H, Moller G, Abedi-Valugerdi M. Major histocompatibility complex class II antigens are required for both cytokine production and proliferation induced by mercuric chloride in vitro. J Autoimmun. 1997; 10(5): 441-6.
  346. Hu H, Moller G, Abedi-Valugerdi M. Mechanism of mercury-induced autoimmunity: both T helper 1- and T helper 2-type responses are involved. Immunology. 1999; 96(3): 348-57.
  347. HultmanP, Johansson U, Turley SJ. Adverse immunological effects and autoimmunity induced by dental amalgam in mice. FASEB J. 1994; 8: 1183-90.
  348. Pollard KM, Lee DK, Casiano CA. The autoimmunity-inducing xenobiotic mercury interacts with the autoantigen fibrillarin and modifies its molecular structure ad antigenic properties. J Immunol. 1997; 158: 3421-8.
  349. Hultman P, Nielsen JB. The effect of toxicokinetics on murine mercury-induced autoimmunity. Environ Res. 1998; 77(2): 141-8.
  350. Chetty CS, McBride V, Sands S, Rajanna B. Effects in vitro on rat brain Mg(++)-ATPase. Arch Int Physiol Biochem. 1990; 98(5): 261-7.
  351. Fukino H, Hirai M, Hsueh YM, Yamane Y. Effect of zinc pretreatment on mercuric chloride-induced lipid peroxidation in the rat kidney. Toxicol App Pharmacol. 1984; 73(3): 395-401.
  352. Sutton KG, McRory JE, Guthrie H, Snutch TP. P/Q-type calcium channels mediate the activity-dependent feedback of syntaxin-1A. Nature. 1999; 401(6755): 800-4.
  353. Godfrey ME, Wojcik DP, Krone CA. Apolipoprotein E genotyping as a potential biomarker for mercury neurotoxicity. J Alzheimer’s Dis. 2003; 5(3): 189-95.
  354. Olanow CW, Arendash GW. Metals and free radicals in neurodegeneration. Curr Opin Neurol. 1994; 7(6): 548-58.
  355. Beal MF. Coenzyme Q10 administration and its potential for treatment of neurodegenerative diseases. Biofactors. 1999; 9(2-4): 262-6.
  356. DiMauro S, Moses LG. CoQ10 use leads to dramatic improvements in patients with muscular disorder. Neurology. 2001.
  357. Matthews RT, Yang L, Browne S, Baik M, Beal MF. Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects. Proc Natl Acad Sci, USA. 1998; 95(15): 8892-7.
  358. Schulz JB, Matthews RT, Henshaw DR, Beal MF. Neuroprotective strategies for treatment of lesions produced by mitochondrial toxins: Implications for neurodegenerative diseases. Neuroscience. 1996; 71(4): 1043-8.
  359. Nagano S, Ogawa Y, Yanaghara T, Sakoda S. Benefit of a combined treatment with trientine and ascorbate in familial amyotrophic lateral sclerosis model mice. Neurosci Lett. 1999; 265(3): 159-62.
  360. Gooch C, et al. Eleanor & Lou Gehrig MDA/ALS Center at Columbia-Presbyterian Medical Center in New York. ALS Newsletter. 2001; 6(3).
  361. Levin LI, Munger KL, O’Reilly EJ, Falk KI, Ascherio A. Primary infection with the Epstein-Barr virus and risk of multiple sclerosis. Ann Neurol. 2010; 67(6): 824-30.
  362. Tai AK, O’Reilly EJ, Alroy KA, Simon KC, Munger KL, Huber BT. Human endogenous retrovirus-K18 Env as a risk factor in multiple sclerosis. Ascherio A Mult Scler. 2008; 14(9): 1175-80.
  363. Thacker EL, Mirzaei F, Ascherio A. Infectious mononucleosis and risk for multiple sclerosis: A meta-analysis. Ann Neurol. 2006; 59(3): 499-503.
  364. Ascherio A, Munger K. Epidemiology of multiple sclerosis: From risk factors to prevention. Semin Neurol. 2008; 28(1):17-28.
  365. Walsh SJ, Rau LM. Autoimmune disease overlooked as a leading cause of death in women. Am J Public Health. 2000; 90: 1463-1466.
  366. Panasiuk J. Peripheral blood lymphocyte transformation test in various skin diseases of allergic origin. Przegl Dermatol. 1980; 67(6): 823-9.
  367. Barnett JH. Discoid lupus erythematosus exacerbated by contact dermatitis. Cutis. 1990; 46(5): 430-2.
  368. Rasmussen HH, Mortensen PB, Jensen IW. Depression and magnesium deficiency. Int J Psychiatry Med. 1989; 19(1): 57-63.
  369. Bekaroglu M, Aslan Y, Gedik Y, Karahan C. Relationships between serum free fatty acids and zinc with ADHD. J Child Psychol Psychiatry. 1996; 37(2): 225-7.
  370. Maes M, Vandoolaeghe E, Neels H, et al. Lower serum zinc in major depression is a sensitive marker of treatment resistance and of the immune/inflammatory response in that illness. Biol Psychiatry. 1997; 42(5): 349-358.
  371. Olivieri G, Brack C, Muller-Spahn F, et al. Mercury induces cell cytotoxicity and oxidative stress and increases beta-amyloid secretion and tau phosphorylation in SHSY5Y neuroblastoma cells. J Neurochem. 2000; 74(1): 231-6.
  372. Tabner BJ, Turnbull S, El-Agnaf OM, Allsop D. Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer’s disease and Parkinson’s disease. Free Radic Biol Med. 2002; 32(11): 1076-83.
  373. Ho PI, Collins SC, et al. Homocysteine potentiates beta-amyloid neurotoxicity: Role of oxidative stress. J Neurochem. 2001; 78(2): 249-53.
  374. Johnson S. The possible role of gradual accumulation of copper, cadmium, lead and iron and depletion of zinc, magnesium, selenium, vitamins B2, B6, D, and E and essential fatty acids in multiple sclerosis. Med Hypotheses. 2000; 55(3): 239-41.
  375. Ascherio A, et al. Dietary intake of vitamin D during adolescence and risk of multiple sclerosis. J Neurol. 2011; 258(3): 479-85.
  376. Ascherio A, Munger KL, Simon KC. Diet, vitamin D and multiple sclerosis. Lancet Neurol. 2010; 9(6): 599-612.
  377. Landner L, Lindestrom. L Copper in Society and the Environment. 2nd ed. Swedish Environmental Research Group(MFG). 1999.
  378. Ganser AL, Kirschner DA. The interaction of mercurials with myelin: Comparison of in vitro and in vivo effects. Neurotoxicol. 1985; 6(1): 63-77, 1985.
  379. Windebank AJ. Specific inhibition of myelination by lead in vitro: Comparison with arsenic, thallium, and mercury. Exp Neurol. 1986; 94(1): 203-12.
  380. Hulda C. The cure fro all diseases part II. Consumer Health. 1995; 18(9).</li>
  381. Waggoner DJ, Bartnikas TB, Gitlin JD. The role of copper in neurodegenerative disease. Neurobiol Dis. 1999; 6(4): 221-30.
  382. Torsdottir G, Kristinsson J, Gudmundsson G, Snaedal J, Johannesson T. Copper, ceruloplasmin and superoxide dismutase (SOD) in amyotrophic lateral sclerosis. Pharmacol Toxicol. 2000; 87(3): 126-30.
  383. Estevez AG, Beckman JS, et al. Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science. 1999; 286(5449): 2498-500.
  384. Cookson MR, Shaw PJ. Oxidative stress and motor neurons disease. Brain Pathol. 1999; 9(1): 165-86.
  385. Shibata N, Nagai R, Kobayashi M. Morphological evidence for lipid peroxidation and protein glycoxidation in spinal cords from sporadic amyotrophic lateral sclerosis patients. Brain Res. 2001; 917(1): 97-104.
  386. Cookson MR, Shaw PJ. Oxidative stress and motor neurons disease. Brain Pathol. 1999; 9(1): 165-86.
  387. Kobayashi MS, Han D, Packer L. Antioxidants and herbal extracts protect HT-4 neuronal cells against glutamate-induced cytotoxicity. Free Radic Res. 2000; 32(2): 115-24.
  388. Bridi R, Crossetti FP, Steffen VM, Henriques AT. The antioxidant activity of standardized extract of Ginkgo biloba (EGb 761) in rats. Phytother Res. 2001; 15(5): 449-51.
  389. Kang JH, Eum WS. Enhanced oxidative damage by the familial amyotrophic lateral sclerosis-associated Cu, Zn-superoxide dismutase mutants. Biochem Biophys Acta. 2000; 1524(2-3): 162-70.
  390. Liu H, Zhu H, Eggers DK, Nersissian AM, et al. Copper(2+) binding to the surface residue cysteine 111 of His46Arg human copper-zinc superoxide dismutase, a familial amyotrophic lateral sclerosis mutant. Biochemistry. 2000; 39(28): 8125-32.
  391. Wong PC, Gitlin JD, et al. Copper chaperone for superoxide dismustase is essential to activate mammalian Cu/Zn superoxide dismutase. Proc Natl Acad Sci, USA. 2000; 97(6): 2886-91.
  392. Kruman II, Pedersen WA, Springer JE, Mattson MP. ALS-linked Cu/Zn-SOD mutation increases vulnerability of motor neurons to excitotoxicity by a mechanism involving increased oxidative stress and perturbed calcium homeostasis. Exp Neurol. 1999; 160(1): 28-39.
  393. Doble A. The role of excitotoxicity in neurodegenerative disease: Implications for therapy. Pharmacol Ther. 1999; 81(3): 163-221.
  394. Urushitani M, Shimohama S. N-methyl-D-aspartate receptor-mediated mitochondrial Ca(2+) overload in acute excitotoxic motor neuron death: a mechanism distinct from chronic neurotoxicity after Ca(2+) influx. J Neurosci Res. 2001; 63(5): 377-87.
  395. Cookson MR, Shaw PJ. Oxidative stress and motor neurons disease. Brain Pathol. 1999; 9(1): 165-86.
  396. Torres-Aleman I, Barrios V, Berciano J. The peripheral insulin-like growth factor system in amyotrophic lateral sclerosis and in multiple sclerosis. Neurology. 1998; 50(3): 772-6.
  397. Dall R, Sonksen PH, et al. The effect of four weeks of supraphysiological growth hormone administration on the insulin-like growth factor axis in women and men. GH-2000 Study Group. J Clin Endocrinol Metab. 2000; 85(11): 4193-200.
  398. Pons S, Torres-Aleman I. Insulin-like growth factor-I stimulates dephosphorylation of ikappa B through the serine phosphatase calcineurin. J Biol Chem. 2000; 275(49): 38620-5.
  399. Lai EC, Rudnicki SA. Effect of recombinant human insulin-like growth factor-I on progression of ALS. A placebo-controlled study. Neurology. 1997; 49(6): 1621-30.
  400. Yuen EC, Mobley WC. Therapeutic applications of neurotrophic factors in disorders of motor neurons and peripheral nerves. Mol Med Today. 1995; 1(6): 278-86.
  401. Dore S, Kar S, Quirion R. Rediscovering an old friend, IGF-I: Potential use in the treatment of neurodegenerative diseases. Trends Neurosci. 1997; 20(8): 326-31.
  402. Couratier P, Vallat JM. Therapeutic effects of neurotrophic factors in ALS. Rev Neurol (Paris). 2000; 156(12): 1075-7.
  403. Leistevuo J, Pyy L, Osterblad M. Dental amalgam fillings and the amount of organic mercury in human saliva. Caries Res. 2000; 35(3): 163-6.
  404. Niebroj-Dobosz I, Jamrozik Z, Janik P, Hausmanowa-Petrusewicz I, Kwiecinski H. Anti-neural antibodies in serum and cerebrospinal fluid of amyotrophic lateral sclerosis (ALS) patients. Acta Neurol Scand. 1999; 100(4): 238-43.
  405. Appel SH, Stockton-Appel V, Stewart SS, Kerman RH. Amyotrophic lateral sclerosis: Associated clinical disorders and immunological evaluations. Arch Neurol. 1986; 43(3): 234-8.
  406. Pestronk A, Choksi R. Multifocal motor neuropathy. Serum IgM anti-GM1 ganglioside antibodies in most patients detected using covalent linkage of GM1 to ELISA plates. Neurology. 1997; 49(5): 1289-92.
  407. Pestronk A, Adams RN, Cornblath D, Kuncl RW, Drachman DB, Clawson L. Patterns of serum IgM antibodies to GM1 and GD1a gangliosides in amyotrophic lateral sclerosis. Ann Neurol. 1989; 25(1): 98-102.
  408. Kikuchi M, Kashii S, Honda Y, Tamura Y, Kaneda K, Akaike A. Protective effects of methylcobalamin, a vitamin B12 analog, against glutamate- induced neurotoxicity in retinal cell culture. Invest Ophthalmol Vis Sci. 1997; 38(5): 848-54.
  409. van Rensburg SJ, Kotze MJ, Hon D, et al. Iron and the folate-vitamin B12-methylation pathway in multiple sclerosis. Metab Brain Dis. 2006; 21(2-3): 121-37.
  410. Waly M, Olteanu H, Deth RC, et al. Activation of methionine synthase by insulin-like growth factor-1 and dopamine: A target for neurodevelopmental toxins and thimerosal. Mol Psychiatry. 2004; 9(4): 358-70.
  411. Clausen J. Mercury and multiple sclerosis. Acta Neurol Scand. 1993; 87(6): 461-4.
  412. Imura N, Pan SK, Ukita T, et al. Chemical methylation of inorganic mercury with methylcobalamin, a vitamin B12 analog. Science. 1971; 172(989): 1248-9.
  413. Choi SC, Bartha R. Cobalamin-mediated mercury methylation by desulfovibrio desulfuricans LS. Appl Environ Microbiol. 1993; 59(1): 290-5.
  414. Loubinoux J, Bisson-Boutelliez C, Miller N, Le Faou AE. Isolation of the provisionally named Desulfovibrio fairfieldensis from human periodontal pockets. Oral Microbiology and Immunology. 2002; 17(5): 321-323.
  415. Chen M, von Mikecz A. Specific inhibition of rRNA transcription and dynamic relocation of fibrillarin induced by mercury. Exp Cell Res. 2000; 259(1): 225-238.
  416. Dieter MP, Luster MI, Boorman GA, Jameson CW, Dean JH, Cox JW. Immunological and biochemical responses in mice treated with mercuric chloride. Toxicol App Pharmacol .1983; 68(2): 218-228.
  417. Hansson M, Djerbi M, et al. Exposure to mercuric chloride during the induction phase and after the onset of collagen-induced arthritis enhances immune/autoimmune responses and exacerbates the disease in DBA/1 mice. Immunology. 2005; 114(3): 428-37.
  418. Fritzler MJ, Ahn C, Holian A. Urinary mercury levels in patients with autoantibodies to U3-RNP (fibrillarin). J Rheumatol. 2000; 27(2): 405-10.
  419. Kusaka Y. Occupational diseases caused by exposure to sensitizing metals. Sangyo Igaku. 1993; 35: 75-87.
  420. Parnham M, Blake D. Antioxidants as antirheumatics. Agents Actions Suppl. 1993; 44: 189-95.
  421. Karatas GK, Tosun AK, Karacehennem E, Sepici V. Mercury poisoning: an unusual cause of polyarthritis. Clin Rheumatol. 2002; 21(1): 73-5.
  422. Casspary EA. Lymphocyte sensitization to basic protein of brain in multiple sclerosis and other neurological diseases. J Neurol Neurosurg Psychiatry. 1974; 37: 701-3.
  423. el-Fawal HA, Gong Z, Little AR. Exposure to methyl mercury results in serum autoantibodies to neuro typic and gliotypic proteins. Neurotoxicology. 1996; 17: 267-76.
  424. Schwyzer RU, Henzi H. Multiple sclerosis: Plaques caused by 2-step demyelization? Med Hypothesis. 1983; 12: 129-42.
  425. Fassbender K, Schmidt R, Mossner R. Mood disorders and dysfunction of the hypothalamic-pituitary-adrenal axis in conditions such as MS: association with cerebral inflammation. Arch Neurol. 1998; 55: 66-72.
  426. Wilder RL. Neuroendocrine-immune system interactions and autoimmunity. Annu Rev Immunol. 1995; 13: 307-38.
  427. Earl C, Chantry A, Mohammad N. Zinc ions stabilize the association of basic protein with brain myelin membranes. J Neurochem. 1988; 51: 718-24.
  428. Riccio P, Giovanneli S, Bobba A. Specificity of zinc binding to myelin basic protein. Neurochem Res. 1995; 20: 1107-13.
  429. Sanders B. The role of general and metal-specific cellular responses in protection and repair of metal-induced damage: stress proteins and metallothioneins. In: Chang L, ed. Toxicology of Metals. Lewis Publishers, CRC Press Inc; 1996: 835-52.
  430. Mendez-Alvarez E, Soto-Otero R, et al. Effects of aluminum and zinc on the oxidative stress caused by 6-hydroxydopamine autoxidation: Relevance for the pathogenesis of Parkinson’s disease. Biochim Biophys Acta. 2002; 1586(2): 155-68.
  431. Kong J, Xu Z. Mitochondrial degeneration in motor neurons triggers the onset of ALS in mice expressing a mutant SOD1 gene. J Neurosci. 1998; 18: 3241-50.
  432. Cassarino DS, Bennett JPJ. Mitochondrial mutations and oxidative pathology, protective nuclear responses, and cell death in neurodegeneration. Brain Res Brain Res Rev. 1999; 29: 1-25.
  433. Guermonprez L, Ducrocq C, Gaudry-Talarmain YM. Inhibition of acetylcholine synthesis and tyrosine nitration induced by peroxynitrite are differentially prevented by antioxidants. Mol Pharmacol. 2001; 60(4): 838-46.
  434. Mahboob M, Shireen KF, Atkinson A, Khan AT. Lipid peroxidation and antioxidant enzyme activity in different organs of mice exposed to low level of mercury. J Environ Sci Health B. 2001; 36(5): 687-97.
  435. Miyamoto K, Nakanishi H, et al. Involvement of enhanced sensitivity of N-methyl-D-aspartate receptors in vulnerability of developing cortical neurons to methylmercury neurotoxicity. Brain Res. 2001; 901(1-2): 252-8.
  436. Anuradha B, Varalakshmi P. Protective role of DL-alpha-lipoic acid against mercury-induced neural lipid peroxidation. Pharmacol Res. 1999; 39(1): 67-80.
  437. Urushitani M, Shimohama S. The role of nitric oxide in amyotrophic lateral sclerosis. Amyotroph Lateral Scler Other Motor Neuron Disord. 2001; 2(2): 71-81.
  438. Torreilles F, Salman-Tabcheh S, Guerin M, Torreilles J. Neurodegenerative disorders: the role of peroxynitrite. Brain Res Brain Res Rev. 1999; 30(2):153-63.
  439. Aoyama K, Matsubara K, Kobayashi S. Nitration of manganese superoxide dismutase in cerebrospinal fluids is a marker for peroxynitrite-mediated oxidative stress in neurodegenerative diseases. Ann Neurol. 2000; 47(4): 524-7.
  440. Guermonprez L, Ducrocq C, Gaudry-Talarmain YM. Inhibition of acetylcholine synthesis and tyrosine nitration induced by peroxynitrite are differentially prevented by antioxidants. Mol Pharmacol. 2001; 60(4): 838-46.
  441. Ahlbom II, Cardis E, Green A, Linet M, Savitz D, Swerdlow A. Review of the epidemiologic literature on EMF and health. Environ Health Perspect. 2001;109(6): 911-933.
  442. Mercola J. Learn how mercury is affecting you and the ones you love.
  443. Behan P, Chaudhuri A. Astrocyte malfunction as cause of MS. Journal of the Royal College of Physicians of Edinburgh. 2002.
  444. Packer L, Tritschler HJ, Wessel K. Neuroprotection by the metabolic antioxidant alpha-lipoic acid. Free Radic Biol Med. 1997; 22(1-2): 359-78.
  445. McCarty MF. Versatile cytoprotective activity of lipoic acid may reflect its ability to activate signaling intermediates that trigger the heat-shock and phase II responses. Med Hypotheses. 2001; 57(3): 313-7.
  446. Whiteman M, Tritschler H, Halliwell B. Protection against peroxynitrite-dependent tyrosine nitration and alpha 1-antiproteinase inactivation by oxidized and reduced lipoic acid. FEBS Lett. 1996; 379(1): 74-6.
  447. Gregus Z, et al. Effect of lipoic acid on biliary excretion of glutathione and metals. Toxicol App Pharmacol. 1992; 114(1): 88-96.
  448. Sannchez-Gomez MV, Malute C. AMPA and kainate receptors each mediate excitotoxicity in oligodendroglial cultures. Neurobiology of Disease. 1999; 6: 475-485.
  449. Yoshika A, et al. Pathophysiology of oligodendroglial excitotoxicity. J Neuroscience Research. 1996; 46: 427-437.
  450. Singh P, et al. Prolonged glutamate excitotoxicity: effects on mitochondrial antioxidants and antioxidant enzymes. Molecular Cell Biochemistry. 2003; 243: 139-145.
  451. Leuchtmann EA, et al. AMPA receptors are the major mediators of excitotoxin death in mature oligodendrocytes. Neurobiology of Disease. 2003; 14: 336-348.
  452. Takahashi JL, et al. Interleukin1 beta promotes oligodendrocyte death through glutamate excitotoxicity. Annal Neurology. 2003; 53: 588-595.
  453. Pitt D, et al. Glutamate uptake by oligodendrocytes: implications for excitotoxicity in multiple sclerosis. Neurology. 2003; 61: 1113-1120.
  454. Soto A, et al. Excitotoxic insults to the optic nerve alter visual evoked potentials. Neuroscience. 2004; 123: 441-449.
  455. Blaylock RL. Interactions of cytokines, excitotoxins and reactive nitrogen and oxygen species in autism spectrum disorders. Journal of American Nutraceutical Association. 2003; 6: 21-35.
  456. Blaylock RL. Chronic microglial activation and excitotoxicity secondary to excessive immune stimulation: Possible factors in Gulf War syndrome and autism. Journal American Physicians and Surgeons. 2004.
  457. Bechtold DA, Smith KJ. Sodium-mediated axonal degeneration in inflammatory demyelinating disease. J Neurol Sci. 2005; 233(1-2): 27-35.
  458. Mutter J, et al. Alzheimer disease: Mercury as pathogenetic factor and apolipoprotein E as a moderator. Neuroendocrinology Letters. 2004; 25(5): 331-339.
  459. Mutter J, Daschner F, et al. Amalgam risk assessment with coverage of references up to 2005. Gesundheitswesen. 2005; 67(3): 204-16.
  460. Rayssiguier Y, Gueux E, et al. High fructose consumption combined with low dietary magnesium intake may increase the incidence of the metabolic syndrome by inducing inflammation. Magnes Res. 2006; 19(4): 237-43.
  461. Bo S, Durazzo M, Pagano G, et al. Dietary magnesium and fiber intakes and inflammatory and metabolic indicators in middle-aged subjects from a population-based cohort. Am J Clin Nutr. 2006; 84(5): 1062-9.
  462. Guerrero-Romero F, Rodriguez-Moran. Hypomagnesemia, oxidative stress, inflammation, and metabolic syndrome. Diabetes Metab Res Rev. 2006; 22(6): 471-6.
  463. Dandona P. Effects of antidiabetic and antihyperlipidemic agents on C-reactive protein. Mayo Clin Proc. 2008; 83(3): 333-42.
  464. Vasdev S, Gill V, Singal P. Role of advanced glycation end products in hypertension and atherosclerosis: Therapeutic implications. Cell Biochem Biophys. 2007; 49(1): 48-63.
  465. Barnes DM, Kircher EA; Effects of inorganic HgCl2 on adipogenesis. Toxicol Sci. 2003; 75(2): 368-77.
  466. Barnes DM, Hanlon PR, Kircher EA. Heavy metal-induced inhibition of active transport in the rat small intestine in vitro: Interaction with other ions. Comp Biochem Physiol C. 1986; 84(2): 363-8.
  467. Iturri SJ, Pentilde A. Interaction of the sugar carrier of intestinal brush-border membranes with HgCl2. Biochim Biophys Acta. 1980; 598(1):100-14.
Print Friendly, PDF & Email