Mercury & Parkinson’s

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There has been a huge increase in the incidence of degenerative neurological conditions in virtually all Western countries over the last two decades. The increase in Parkinson’s and other motor neuron disease has been over 50%. The primary cause appears to be increased exposures to toxic pollutants, such as toxic metals, pesticides, etc., resulting in brain inflammation and oxidative damage of free radicals. Dental 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 exposed 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 and mood and behavioral disorders. A study found that those with occupational exposure to lead, arsenic, or copper have more than double the incidence of Parkinson’s than normal.

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: silver (mercury) dental fillings, food (mainly fish), vaccinations, and 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 methyl mercury. Mercury in amalgam fillings, because of its high vapor pressure and galvanic action with other metals in the mouth, has been found to be continuously vaporized and released into the body, has been found to be the directly correlated to the number of amalgam surfaces, and is the largest source of mercury in the majority of people, typically between 60 and 90% of the total. 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, saliva, and feces typically rise temporarily but decline between 60 to 90% within six to nine months.

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. 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.

Mechanisms by which Mercury Causes Neurological Conditions Found in Parkinson’s and Neurodegenerative Diseases

Programmed cell death (apoptosis) is documented to be a major factor in degenerative neurological conditions like ALS, Alzheimer’s, MS, 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, DNA fragmentation, and mitochondrial membrane dysfunction. Mitochondrial DNA mutations or dysfunction is fairly common and is found in at least one in every 200 people. Toxicity effects affect this population more than those with less susceptibility to mitochondrial dysfunction. This has been found to be a factor in conditions like Parkinson’s. The mechanisms by which mercury causes (often synergistically along with other toxic exposures) all of these conditions and neuronal apoptosis will be documented.

TNFa (tumor necrosis factor-alpha) is a cytokine that controls a wide range of immune cell response in mammals, including cell death (apoptosis) in neuronal and immune cells. 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 increase, 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 and deplete glutathione, 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 of calcium;
  • inhibition of glucose transport, and of enzyme function, protein transport, and other essential nutrient transport;
  • 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;
  • immune system damage; and
  • induction of inflammatory cytokines.

Oxidative stress and reactive oxygen species (ROS) have been implicated as major factors in neurological disorders including stroke, Parkinson’s disease (PD), Alzheimer’s, ALS, etc. 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 dismustase (SOD). Only a few micrograms of mercury severely disturb cellular function and inhibit nerve growth. Exposure to mercury results in metalloprotein compounds that have genetic effects, having both structural and catalytic effects on gene expression. Mercury inhibits sulfur ligands in MT and, in the case of intestinal cell membranes, inactivates MT that normally binds cuprous ions, thus allowing buildup of copper to toxic levels in many and malfunction of the Zn/Cu SOD function. Mercury also causes displacement of zinc in MT and SOD, which has been shown to be a factor in neurotoxicity and neuronal diseases. 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 have a relation to autoimmune reactions in significant numbers of people. Increased formation of reactive oxygen species (ROS) has also been found to increase formation of advanced glycation end products (AGEs) that have been found to cause activation of glial cells to produce superoxide and nitric oxide; they can be considered part of a vicious cycle, which finally leads to neuronal cell death in the substantia nigra in PD.

Mercury exposure causes high levels of oxidative stress/reactive oxygen species (ROS), which has been found to be a major factor in apoptosis and neurological disease including dopamine or glutamate related apoptosis. 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 congugates are found to be highest in the brain substantia nigra with similar congugates 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. Exposure to mercury vapor and methylmercury is well documented to commonly cause conditions involving tremor and/or ataxia, with populations exposed to mercury experiencing tremor on average proportional to exposure level. One study found higher than average levels of mercury in the blood, urine, and hair of Parkinson’s patients. Another study found blood and urine mercury levels to be very strongly related to Parkinson’s with odds ratios of approximately twenty at high levels of Hg exposure. Other studies that reviewed occupational exposure data found that occupational exposure to manganese and copper have high odds rations for relation to PD, as well as multiple exposures to these and lead, but one study noted that this effect was only seen for exposure of over 20 years. Occupational exposure to mercury has been found to cause Parkinson’s. One study found the EDTA chelation was effective in reducing some of the effects.

Glutamate is the most abundant amino acid in the body and in the CNS acts as excitory neurotransmitter, which also causes inflow of calcium. Astrocytes, cells in the brain and CNS with the task of keeping clean the area around nerve cells, have the function of neutralizing excess glutamate by transforming it to glutamic acid. If astrocytes are not able to rapidly neutralize excess glutamate, then a buildup of glutamate and calcium occurs, causing swelling and neurotoxic effects. 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. This is also a factor in conditions such as CFS, Parkinson’s, and ALS.

Parkinson’s disease involves the aggregation of alpha-synuclein to form fibrils, which are the major constituent of intracellular protein inclusions (lewy bodies and lewy neurites) in dopaminergic neurons of the substantia nigra. Occupational exposure to specific metals, especially manganese, copper, lead, iron, mercury, aluminum, appears to be a risk factor for Parkinson’s disease based on epidemiological studies. Elevated levels of several of these metals have also been reported in the substantia nigra of Parkinson’s disease subjects. Exposure to aluminum hydroxide in vaccines also appears to sometimes cause symptoms similar to Parkinson’s or other neurological conditions.

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 Parkinson’s cases there was an elevation in plasma serum digoxin and a reduction in serum magnesium, 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 PD, 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. It is documented in this paper that mercury is a cause of most of these conditions seen in Parkinson’s.

An EKM System for Evaluating Nerve and Muscle Function Ability Using a Set of 5 Measures (Precision, Imprecision, Tremor, Fitts’ Constant, and Irregularity)

Ninety-six participants—including thirty controls subjects, 36 Cree subjects exposed to mercury, 21 subjects with Parkinson disease, six with presumed cerebellar deficit, and three with essential tremors— participated in the study. An ANOVA on the three largest groups generated significant results for tremor, Fitts’ constant, and irregularity between the Cree and the control subjects and on Fitts’ constant and irregularity between the subjects with Parkinson’s disease and the control subjects. Three subgroups of the same mean age composed of six subjects each were selected. One was composed of Cree subjects with the highest level of mercury exposure, another with Cree subjects having a low level of mercury exposure, and a third with control subjects. An ANOVA on these three groups revealed a significant difference between both groups of Cree subjects and the control group for Fitts’ constant and irregularity. These preliminary results suggest that the EKM system is able to discriminate the performance of different groups of subjects and found significant evidence that mercury exposure is related to nerve and muscle function conditions such as tremor and Parkinson’s.

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, since 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. 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.

Studies have 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 demyelination. 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+ suppresser 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. Mercury penetrates and damages the blood brain barrier, allowing penetration of the barrier by other substances that are neurotoxic. Such damage to the blood brain barrier’s function has been found to be a major factor in chronic neurological diseases such as MS and studies have found mercury related mental effects to be indistinguishable from those of MS patients. MS patients have been found to have much higher levels of mercury in cerebrospinal fluid compared to controls. Large German studies, including studies at German universities, 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. Similarly thousands of MS patients have been documented to have recovered or significantly improved after amalgam replacement.

Mercury has been found to accumulate preferentially in the primary motor function related areas such as the brain stem, cerebellum, rhombencephalon, dorsal root ganglia, and anterior horn motor neurons, which enervate the skeletal muscles. There is considerable indication this may be a factor in development of ALS and other neurodegenerative conditions. Treatment using IV glutathione, vitamin C, and minerals has been found to be very effective in the stabilizing and amelioration of some of these chronic neurological conditions.

Low levels of toxic metals have been found to inhibit dihydroteridine reductase, which affects the neural system function by inhibiting brain transmitters 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’s, and MS. Such patients have abnormal inhibition of neurotransmitter production. Supplements that inhibit breach of the blood brain barrier, such as bioflavonoids, have been found to slow such neurological damage.

Clinical tests of patients with MND, ALS, Parkinson’s, Alzheimer’s, Lupus (SLE), and rheumatoid arthritis have found that the patients generally have elevated plasma cysteine to sulfate ratios, with the average being 500% higher than controls, and in general being poor sulfur oxidizers. Mercury has been shown to diminish and block sulfur oxidation and thus reduce glutathione levels. Glutathione is produced through the sulfur oxidation side of this process. Low levels of available glutathione have been shown to increase mercury retention and increase toxic effects, while high levels of free cysteine have been demonstrated to make toxicity due to inorganic mercury more severe. Mercury has also been found to play a part in neuronal problems through blockage of the P-450 enzymatic process. Other toxic metals and toxins, such as pesticides, have also been found to cause the types of damage seen in Parkinson’s and to exposure to have positive correlation to Parkinson’s. Another exposure that affects some appears to be hexane. There are synergistic effects of various toxics that result in conditions like Parkinson’s. Determination of one’s factors by history assessment and tests is a first step in improving the condition.

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 40, whereas those with type APOE-2 readily excrete mercury and are less susceptible. Those with type APOE-3 are intermediate to the other two types.

The Huggins Clinic, using total dental revision (TDR), has successfully treated over a thousand patients with chronic autoimmune conditions like MS, Parkinson’s, Lupus, ALS, AD, diabetes, etc. Jaw bone cavitations were found to be common significant factors in some of these conditions such as Parkinson’s.

Huggins Total Dental Revision Protocol questionnaire and panel of tests:

  • Replace amalgam fillings starting with filling with highest negative current or highest negative quadrant, with supportive vitamin/mineral supplements.
  • Extract all root canaled teeth using proper finish protocol.
  • Test and treat cavitations and amalgam tattoos where relevant.
  • Provide supportive supplementation, periodic monitoring tests, and evaluate need for further treatment (not usually needed).
  • Avoid acute exposures/challenges to the immune system on a weekly 7/14/21 day pattern.

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

  • Element test (low hair mercury level does not indicate low body level)(more than 3 essential minerals out of normal range indicates likely metals toxicity)
  • CBC blood test with differential and platelet count
  • Blood serum profile
  • Urinary mercury (for person with average exposure with amalgam fillings, average mercury level is 3 to 4 ppm; lower test level than this likely means person is poor excretor and accumulating. mercury, often mercury toxic)
  • Fractionated porphyrin urine test (note: test results sensitive to light, temperature, shaking)
  • Individual tooth electric currents (replace high negative current teeth first)
  • Patient questionnaire on exposure and symptom history
  • Specific gravity of urine (test for pituitary function; 1.022 normal; 1.008 consistent with depression and suicidal tendencies)

Note: During initial exposure to mercury, the body marshals immune system and other measures to try to deal with the challenge, so many test indicators will be high; after prolonged exposure the body and immune system inevitably lose the battle and measures to combat the challenge decrease, so some test indicator scores decline. Chronic conditions are common during this phase. Also, high mercury exposure accompanied by low hair mercury or urine mercury levels usually indicates that the body is retaining mercury and likely experiencing a toxicity problem.

Test results indicating mercury/metals toxicity:

  • White blood cell count: 7500 or 4500
  • Hemocrit: 50% or 40%
  • Lymphocyte count: 2800 or 1800
  • Blood protein level: 7.5 gm/100 ml
  • Triglyceride: 150 mg %ml
  • BUN: 18 or 12
  • Hair mercury: 1.5 ppm or .4 ppm
  • Oxyhemoglobin level: 55% saturated
  • Carboxyhemoglubin: 2.5% saturated
  • T lymphocyte count: 2000
  • DNA damage/cancer
  • TSH
  • Hair aluminum: 10 ppm
  • Hair nickel: 1.5 ppm
  • Hair manganese: 0.3 ppm
  • Immune reactive to mercury, nickel, aluminum, etc.
  • High hemoglobin and hemocrit and high alkaline
  • Phosphatase(alk phos) and lactic dehydrogenese(LDA) during initial phases of exposure; with low/marginal hemoglobin and hemocrit plus low oxyhemoglobin during long-term chronic fatigue phase.

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, root canal toxicity, and cavitation toxicity are major factors in these conditions, and most with these conditions improve after TDR if protocol is followed carefully.

There are extensive documented cases (many thousands) where removal of amalgam fillings led to cure of serious health problems such as MS, ALS, Parkinson’s/ muscle tremor, Alzheimer’s, muscular/joint pain/ fibromyalgia, anxiety, mental confusion, CFS, and memory disorders. 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. Some that have been found to be effective in treating metals related autoimmune conditions, such as Parkinson’s, include vitamin B6, CoenzymeQ10, methyl cobalamine (B12), L-carnitine, choline, ginseng, Ginkgo biloba, vitamins C and E, nicotine, octacosanol, phosphatifylserine, and omega 3 fatty acids (fish and flaxseed oil), tumeric, lipoic acid, proteolytic enzymes, and hydergine. Reduced glutathione (GSH) and N-acetyl cysteine(NAC) have been found to be protective against cellular apoptosis seen in Parkinson’s and other neurodegenerative conditions. High levels of vitamins C and E, along with zinc, have also been found protective against oxidative stress and some effects of mercury toxicity including for Parkinson’s. CoQ10 at 600 mg per day was found effective at reducing Parkinson’s effects. IGF-1 treatments have also been found to alleviate some of the symptoms of ALS. There is also evidence that melatonin and curcumin may have beneficial effects on reducing metal toxicity. Turmeric/curcumin has been found to reduce some of the toxic and inflammatory effects of toxic metals.

Lithium supplements (lithium carbonate and lithium oratate) have been found to be effective in protecting neurons and brain function from oxidative and excitotoxic effects. A study demonstrated that combined treatment with lithium and valproic acid elicits synergistic neuroprotective effects against glutamate excitotoxicity in cultured brain neurons.

Doctors affiliated with Life Enhancement Foundation have developed a diet and supplementation protocol to reduce Parkinson’s effects and delay the start time of daily levodopa therapy. Dietary considerations include avoidance of alcohol, sugar, red meats, dairy, gluten, fried foods, aspartame, MSG, and pesticides. Some clinics have found root canals, cavitations, and amalgam tattoos to also be a factor in such autoimmune conditions and that treatment of them improves prognosis in recovery from these conditions.


  1. 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.
  2. Bulat P. Activity of Gpx and SOD in workers occupationally exposed to mercury. Arch Occup Environ Health. 1998; 71: S37-9.
  3. Stohs SJ, Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radic Biol Med. 1995; 18(2): 321-36.
  4. Jay D. Glutathione inhibits SOD activity of Hg. Arch Inst Cardiol Mex. 1998; 68(6): 457-61.
  5. 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.
  6. Tan S, et al. Oxidative stress induces programmed cell death in neuronal cells. J Neurochem. 1998; 71(1): 95-105.
  7. Matsuda T, Takuma K, Lee E, et al. Apoptosis of astroglial cells. Nippon Yakurigaku Zasshi. 1998; 112(1): 24.
  8. 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.
  9. 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.
  10. Vimy MJ, Takahashi Y, Lorscheider FL. Maternal-fetal distribution of mercury released from dental amalgam fillings. Amer J Physiol. 1990; 258: R939-945.
  11. Boyd ND, Vimy J, et al. Mercury from dental silver tooth fillings impairs sheep kidney function. Am J Physiol. 1991; 261: R1010-R1014.
  12. Hahn L, et al. Distribution of mercury released from amalgam fillings into monkey tissues. FASEB J. 1990; 4: 5536.
  13. Galic N, Ferencic Z, et al. Dental amalgam mercury exposure in rats. Biometals. 1999; 12(3): 227-31.
  14. 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.
  15. McFadden SA. Xenobiotic metabolism and adverse environmental response: sulfur-dependent detox pathways. Toxicology. 1996; 111(1-3): 43-65.
  16. Alberti A, Pirrone P, Elia M, Waring RH, Romano C. Sulphation deficit in “low-functioning” autistic children. Biol Psychiatry. 1999; 46(3): 420-4.
  17. Henriksson J, Tjalve H. Uptake of inorganic mercury in the olfactory bulbs via olfactory pathways in rats. Environ Res. 1998; 77(2): 130-40.
  18. Huggins HA, Levy TE. Uniformed Consent: The Hidden Dangers in Dental Care. Hampton Roads Publishing Company Inc; 1999.
  19. Rodgers JS, Hocker JR, et al. Mercuric ion inhibition of eukaryotic transcription factor binding to DNA. Biochem Pharmacol. 2001; 61(12): 1543-50.
  20. Babich, et al. The mediation of mutagenicity and clastogenicity of heavy metals by physiochemical factors. Environ Res. 1985; 37: 253-286.
  21. Hansen K, et al. A survey of metal induced mutagenicity in vitro and in vivo. J Amer Coll Toxicol. 1984; 3: 381-430.
  22. Knapp LT, Klann E. Superoxide-induced stimulation of protein kinase C via thiol modification and modulation of zinc content. J Biol Chem. 2000.
  23. Jenner P. Oxidative mechanisms in PD. Mov Disord. 1998; 13(1): 24-34.
  24. Rajanna B, et al. Modulation of protein kinase C by heavy metals. Toxicol Lett. 1995; 81(2-3): 197-203.
  25. 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.
  26. Veprintsev DB. Pb2+ and Hg2+ binding to alpha-lactalbumin. Biochem Mol Biol Int. 1996; 39(6): 1255-65.
  27. 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.
  28. Arvidson K. Corrosion studies of dental gold alloy in contact with amalgam. Swed Dent J. 1984; 68:135-139.
  29. 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.
  30. Lund ME, et al. Treatment of acute MeHg poisoning by NAC. J Toxicol Clin Toxicol. 1984; 22(1): 31-49.
  31. Gregus Z. Effect of lipoic acid on biliary excretion of glutathione and metals. Toxicol App Pharmacol. 1992; 114(1): 88-96.
  32. Nicole A, et al. Direct evidence for glutathione as mediator of apoptosis in neuronal cells. Biomed Pharmacother. 1998; 52(9): 349-55.
  33. Spencer JP, et al. Cysteine & GSH in PD: Mechanisms involving ROS. J Neurochem. 1998; 71(5): 2112-22.
  34. 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.
  35. 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.
  36. Offen D, et al. Use of thiols in treatment of PD. Exp Neurol. 1996; 141(1): 32-9.
  37. 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.
  38. 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.
  39. 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.
  40. 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-carboxylic 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.
  41. 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.
  42. Campbell N, Godfrey M. Confirmation of mercury retention and toxicity using DMPS provocation. J Adv Med. 1994; 7(1).
  43. Zander D, et al. Mercury mobilization by DMPS in subjects with and without amalgams. Zentralbl Hyg Umweltmed. 1992; 192(5): 447-54.
  44. Stejskal VDM, et al. MELISA: Tool for the study of metal allergy. Toxicology in Vitro. 1994; 8(5): 991-1000.
  45. Thompson CM, Markesbery WR, et al. Regional brain trace-element studies in Alzheimer’s disease. Neurotoxicology. 1988; 9(1): 1-7.
  46. Hock, et al. Increased blood mercury levels in Alzheimer’s patients. Neural Transm. 1998; 105: 59-68.
  47. Cornett, et al. Imbalances of trace elements related to oxidative damage in Alzheimer’s diseased brain. Neurotoxicolgy. 1998; 19: 339-345.
  48. Ehmann WD, Marksbery WR. A search for longitudinal variations in trace element levels in nails of Alzheimer’s disease patients. Biol Trace Elem Res. 1990; 26-27: 461-70.
  49. 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.
  50. 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.
  51. Weiner JA, et al. The relationship between mercury concentration in human organs and predictor variables. Sci Tot Environ. 1993; 138(1-3): 101-115.
  52. Weiner JA. An estimation of the uptake of mercury from amalgam fillings in Swedish subjects. Sci Tot Environ. 1995; 168(3): 255-265.
  53. Tandon L, et al. Elemental imbalance studies by INAA on ALS patients. J Radioanal Nuclear Chem. 1995; 195(1):13-19.
  54. Mano Y, et al. Mercury in the hair of ALS patients. Rinsho Shinkeigaku. 1989; 29(7): 844-848.
  55. Khare, et al. Trace element imbalances in ALS. Neurotoxicology. 1990; 11: 521-532.
  56. Berglund F. Case Reports Spanning 150 Years on the Adverse Effects of Dental Amalgam. Orland, FL: Bio-Probe, Inc; 1995.
  57. Lichtenberg HJ. Elimination of symptoms by removal of dental amalgam from mercury poisoned patients. J Orthomol Med. 1993; 8:145-148.
  58. 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.
  59. 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.
  60. Redhe O, et al. Recovery from ALS after removal of dental amalgam fillings. Int J Risk & Safety in Med. 1994; 4: 229-236.
  61. Seidler A, et al. Possible environmental factors for Parkinson’s disease. Neurology. 1996; 46(5): 1275-1284.
  62. Ohlson, et al. Parkinson’s disease and occupational exposure to mercury. Scand J Of Work Environment Health. 1981; 7(4): 252-256.
  63. Golota LG. Theraputic properties of unitihiol. Farm Zh. 1980; 1: 18-22.
  64. Miller K, Ochudlo S, Opala G, Smolicha W, Siuda J. Parkinsonism in chronic occupational metallic mercury intoxication. Neurol Neurochir Pol. 2003: 37.
  65. 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.
  66. D. Cysteine metabolism and metal toxicity. Altern Med Rev. 1998; 3(4): 262-270.
  67. 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.
  68. Berndt WO, et al. Renal glutathione and mercury uptake. Fundam Toxicol. 1985; 5(5): 832-9.
  69. 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.
  70. Clarkson TW, et al. Billiary secretion of glutathione-metal complexes. Fundam Appl Toxicol. 1985; 5(5): 816-31.
  71. 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.
  72. 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.
  73. O’Halloran TV. Transition metals in control of gene expression. Science. 1993; 261(5122): 715-25.
  74. 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.
  75. Boot JH. Effects of SH-blocking compounds on the energy metabolism in isolated rat hepatocytes. Cell Struct Funct. 1995; 20(3): 233-8.
  76. Baauweegers HG, Troost D. Localization of metallothionein in the mammilian central nervous system. Biol Signals. 1994; 3: 181-7.
  77. Ronnback L, et al. Chronic encephalopaties induced by low doses of mercury or lead. Br J Ind Med. 1992; 49: 233-240.
  78. Langauer-Lewowicka H. Changes in the nervous system due to occupational metallic mercury poisoning. Neurol Neurochir Pol. 1997; 31(5): 905-13.
  79. Kim P, Choi BH. Selective inhibition of glutamate uptake by mercury in cultured mouse astrocytes. Yonsei Med J. 1995; 36(3): 299-305.
  80. Brookes N. In vitro evidence for the role of glutatmate in the CNS toxicity of mercury. Toxicology. 1992; 76(3): 245-56.
  81. Borges VC, Santos FW, Rocha JB, Nogueira CW. Heavy metals modulate glutamatergic system in human platelets. Neurochem Res. 2007; 32(6): 953-8.
  82. Wang Y, Bollard ME, Nicholson JK, Holmes E. Exploration of the direct metabolic effects of mercury II chloride on the kidney of sprague-dawley rats using high-resolution magic angle spinning 1H NMR spectroscopy of intact tissue and pattern recognition. Pharm Biomed Anal. 2006; 40(2): 375-81.
  83. Fonfría E, Vilaró MT, Babot Z, Rodríguez-Farré E, Suñol C. Mercury compounds disrupt neuronal glutamate transport in cultured mouse cerebellar granule cells. J Neurosci Res. 2005; 79(4): 545-53.
  84. Ono B, et al. Reduced tyrosine uptake in strains sensitive to inorganic mercury. Genet. 1987; 11(5): 399.
  85. Singh I, Pahan K, Khan M, Singh AK. Cytokine-mediated induction of ceramide production is redox-sensitive. Implications to pro-inflammatory cytokine-mediated apoptosis in demyelinating diseases. J Biol Chem. 1998; 273(32): 20354-62.
  86. 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.
  87. 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.
  88. 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.
  89. 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.
  90. 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.
  91. Kim SH, Johnson VJ, Sharma RP. Mercury inhibits nitric oxide production but activates pro-inflammatory cytokine expression in murine macrophage: Differential modulation of NF-kappaB and p38 MAPK signaling pathways. Nitric Oxide. 2002; 7(1): 67-74.
  92. 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.
  93. 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.
  94. Sallsten G, et al. Mercury in cerebrospinal fluid in subjects exposed to mercury vapor. Environ Res. 1994; 65: 195-206.
  95. 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.
  96. Ariza ME, et al. Mercury mutagenesis. Biochem Mol Toxicol. 1999; 13(2): 107-12.
  97. Ariza ME, et al. Mutagenic effect of mercury. In Vivo. 1994; 8(4): 559-63.
  98. Carpenter DO. Effects of metals on the nervous system of humans and animals. Int J Occup Med Environ Health. 2001; 14(3): 209-18.
  99. Vanacore N, Bonifati V, et al. Epidemiology of multiple system atrophy. ESGAP Consortium. Neurol Sci. 2001; 22(1): 97-9.
  100. Gorell JM, et al. Occupational exposure to mercury, manganese, copper, lead, and the risk of Parkinson’s disease. Neurotoxicology. 1999; 20(2-3): 239-47.
  101. Gorell JM, et al. Occupational exposures to metals as risk factors for Parkinson’s disease. Neurology. 1997; 48(3): 650-8.
  102. Rybicki BA, et al. Parkinson’s disease mortality and the industrial use of heavy metals in Michigan. Mov Disord. 1993; 8(1): 87-92.
  103. Chacon Pena JR, Duran Ferreras E. Parkinsonism probably induced by manganese. Rev Neurol. 2001; 33(5): 434-7.
  104. Chun HS, Lee H, Son JH. Manganese induces endoplasmic reticulum (ER) stress and activates multiple caspases in nigral dopaminergic neuronal cells, SN4741. Neurosci Lett. 2001; 316(1): 5-8.
  105. Discalzi G, Meliga F, et al, Occupational Mn parkinsonism: magnetic resonance imaging and clinical patterns following CaNa2-EDTA chelation. Neurotoxicology. 2000; 21(5): 863-6.
  106. Wood M. Mechanisms for the Neurotoxicity of Mercury in Organotransitional Metal Chemistry. New York: Plenum Publishing Corp; 1987.
  107. Sharma RP, et al. Metals and neurotoxic effects. J of Comp Pathology. 1981.
  108. Casdorph HR. Toxic Metal Syndrome. Avery Publishing Group; 1995.
  109. Choi B, et al. Abnormal neuronal migration of human fetal brain. Journal of Neurophalogy. 1978; 37: 719-733.
  110. Monnet-Tschudi F, et al. Comparison of the developmental effects of 2 mercury compounds on glial cells and neurons in the rat telencephalon. Brain Res. 1996; 741: 52-59.
  111. Chang LW, Hartmann HA. Quantitative cytochemical studies of RNA in experimental mercury poisoning. Acta Neruopathol (Berlin). 1973; 23(1): 77-83.
  112. Larkfors L, et al. Methylmercury induced alterations in the nerve growth factor level in the developing brain. Res Dev Res. 1991; 62(2): 287.
  113. Belletti S, Gatti R. Time course assessment of methylmercury effects on C6 glioma cells: Submicromolar concentrations induce oxidative DNA damage and apoptosis. J Neurosci Res. 2002; 70(5): 703-11.
  114. Wenstrup, et al. Trace element imbalances in the brains of Alzheimer’s patients. Research. 1990; 533: 125-131.
  115. Lorscheider FL, Haley B, et al. Mercury vapor inhibits tubulin binding. FASEB J. 1995; 9(4): A-3485.
  116. de Saint-Georges, et al. Inhibition by mercuric chloride fo the in vitro polymeriztion of microtubules. Soc Biol Fil. 1984; 178(5): 562-6.
  117. 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.
  118. 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.
  119. Siblerud RL. A commparison of mental health of multiple schlerosis patients with silver dental fillings and those with fillings removed. Psychol Rep. 1992; 70(3.2): 1139-51.
  120. Mathieson PW. Mercury: God of TH2 cells. Clinical Exp Immunol. 1995; 102(2): 229-30.
  121. Heo Y, Parsons PJ, Lawrence DA. Lead differentially modifies cytokine production in vitro and in vivo. Toxicol App Pharmacol. 1996; 138:149-57.
  122. Parsons RB. Regulation of hepatic glutathione synthesis: Current concepts and controversies. J Hepatol. 1998; 29(4): 595-602.
  123. Zalups RK, et al. Nephrotoxicity of inorganic mercury co-administered with L-cysteine. Toxicology. 1996; 109(1): 15-29.
  124. Perry TL, et al. Hallevorden-Spatz disease: Cysteine accumulation and cysteine dioxygenase deficiency. Ann Neural. 1985; 18(4): 482-489.
  125. Taylor J. A Complete Guide to Mercury Toxicity from Dental Fillings. Scripps Publishing. 1988.
  126. West ES, et al. Textbook of Biochemistry. MacMillan Co; 1957: 853.
  127. 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.
  128. Warren T. Beating Alzheimer’s. Avery Publishing Group; 1991.
  129. Haley B. The toxic effects of mercury on CNS proteins: Similarity to observations in Alzheimer’s disease. IAOMT symposium paper. 1997.
  130. Ziff MF. Documented clinical side effects to dental amalgams. Adv Dent Res. 1992; 1(6): 131-134.
  131. Ziff S. Dentistry without Mercury. 8th ed. Bio-Probe, Inc; 1996.
  132. Golden R, et al. Dementia and Alzheimer’s disease. Minnesota Medicine. 1995; 78: 25-29.
  133. Miller MA, et al. Mercuric chloride induces apoptosis in human T lymphocytes. Toxicol App Pharmacol. 1998; 153(2): 250-7.
  134. Bagentose LM, et al. Mercury induced autoimmunity in humans. Immunol Res. 1999; 20(1): 67-78.
  135. Goering PL, Thomas D, Rojko JL, Lucas AD. Mercuric chloride-induced apoptosis is dependent on protein synthesis. Toxicol Lett. 1999; 105(3): 183-95.
  136. Davis M, ed. Defense Against Mystery Syndromes. Chek Printing Co; 1994.
  137. Berglund F, et al. Improved health after removal of dental amalgam fillings. Swedish Assoc of Dental Mercury Patients. 1998.
  138. Klock, B, Blomgren, J, Ripa, U, Andrup B. Effect of amalgam removal in patients who suspect amalgam poisoning. Tandläkartidningen. 1989; 81: 1297-1302.
  139. Schoeny R. Use of genetic toxicology data in U.S. EPA risk assessment: The mercury study. Environ Health Perspect. 1996; 104(3): 663-73.
  140. Lee CH, et al. Genotoxicity of phenylHg acetate in humans as compared to other mercury compounds. 1997; 392(3): 269-76.
  141. Constantinidis J, et al. Hypothesis regarding amyloid and zinc in the pathogenisis of Alzheiemer disease. Alzheimer Dis Assoc Disord. 1991; 5(1): 31-35.
  142. Bjorklund G. Can mercury cause Alzheimer’s? Tidsskr Nor Laegeforen. 1991.
  143. 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.
  144. Finkelstein Y, et al. The enigma of parkinsonism in chronic borderline mercury intoxication, resolved by challenge with penicillamine. Neurotoxicology. 1996; 17(1): 291-5.
  145. Sorensen FW, Larsen JO, Eide R, Schionning JD. Neuron loss in cerebellar cortex of rats exposed to mercury vapor: a stereological study. Acta Neuropathol (Berl). 2000; 100(1): 95-100.
  146. Shikata E, Mochizuki Y, Oishi M, Takasu T. A case of chronic inorganic mercury poisoning with progressive intentional tremor and remarkably prolonged latency of P300. Rinsho Shinkeigaku. 1998; 38(12): 1064-6.
  147. Yamanaga H. Quantitative analysis of tremor in Minamata disease. Tokhoku J Exp Med. 1983; 141(1): 13-22.
  148. Biernat H, Ellias SA, Grandjean P. Tremor frequency patterns in mercury vapor exposure, compared with early Parkinson’s disease and essential tremor. Neurotoxicology. 1999; 20(6): 945-52.
  149. al-Saleh I, Shinwari N. Urinary mercury levels in females: Influence of dental amalgam fillings. Biometals. 1997; 10(4): 315-23.
  150. 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.
  151. Rice DC. Evidence of delayed neurotoxicity produced by methyl mercury developmental exposure. Neurotoxicology. 1996; 17(3-4): 583-96.
  152. Weiss B, Clarkson TW, Simon W. Silent latency periods in methylmercury poisoning and in neurodegenerative disease. Environ Health Perspect. 2002; 110(5): 851-4.
  153. Smith, et al. Pteridines and mono-amines: relevance to neurological damage. Postgrad Med J. 1986; 62(724): 113-123.
  154. Kay AD, et al. Cerebrospinal fluid biopterin is decreased in Alzheimer’s disease. Arch Neurol. 1986; 43(10): 996-9.
  155. Yamiguchi T, et al. Effects of tyrosine administreation on serum bipterin in patients with Parkinson’s disease and normal controls. Science. 1983; 219(4580): 75-77.
  156. Nagatsu T, et al. Catecholoamine-related enzymes and the biopterin cofactor in Parkinson’s. Neurol. 1984; 40: 467-73.
  157. Haddad, Shannon, Winchester. Clinical Management of Poisoning. 3rd ed. Philadelphia: W. B. Sounders and Company; 1998: 753.
  158. Kay AD, et al. Cerebrospinal fluid biopterin is decreased in Alzheimer’s disease. Arch Neurol. 1986; 43(10): 996-9.
  159. Woods JS, et al. Urinary porphyrin profiles as biomarker of mercury exposure: Studies on dentists. J Toxicol Environ Health. 1993; 40(2-3): 235.
  160. Woods JS. Altered porphyrin metabolites as a biomarker of mercury exposure and toxicity. Physiol Pharmocol. 1996; 74(2): 210-15.
  161. Martin MD, et al. Validity of urine samples for low-level mercury exposure assessment and relationship to porphyrin and creatinine excretion rates. J Pharmacol Exp Ther. 1996.
  162. Woods JS, et al. Effects of porphyrinogenic metals on coproporphrinogen oxidase in liver and kidney. Toxicol App Pharmacol. 1989; 97: 183-190.
  163. 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.
  164. 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.
  165. 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.
  166. Kurup RK, Kurup PA. Hypothalamic digoxin-mediated model for Parkinson’s disease. Int J Neurosci. 2003; 113(4): 515-36.
  167. Kumar AR, Kurup PA. Inhibition of membrane Na+-K+ ATPase activity: A common pathway in central nervous system disorders. J Assoc Physicians India. 2002; 50: 400-6.
  168. Danielsson BR, et al. Behavioral effects of prenatal metallic mercury inhalation exposure in rats. Neurotoxicol Teratol. 1993; 15(6): 391-6.
  169. Fredriksson, et al. Prenatal exposure to metallic mercury vapour and methylmercury produce interactive behavioral changes in adult rats. Neurotoxicol Teratol. 1996; 18(2): 129-34.
  170. Shenker BJ, Low-level MeHg exposure causes human T-cells to undergo apoptosis: evidence of mitochondrial dysfunction. Environ Res. 1998; 77(2): 149-159.
  171. Shenker BJ, Pankoski L, Zekavat A, Shapiro IM. Mercury-induced apoptosis in human lymphocytes: caspase activation is linked to redox status. Antioxid Redox Signal. 2002; 4(3): 379-89.
  172. 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.
  173. Perlingeiro RC, et al. Polymorphonuclear phagentosis in workers exposed to mercury vapor. Int J Immounopharmacology. 1994; 16(12): 1011-7.
  174. Albers JW, et al. Neurological abnormalities associated with remote occupational elemental mercury exposure. Ann Neurol. 1988; 24(5): 651-9.
  175. Soleo L, et al. Effects of low exposure to inorganic mercury on psychological performance. Br J Ind Med. 1990; 47(2): 105-9.
  176. Smith PJ, et al. Effect of exposure to elemental mercury on short term memory. Br J Ind Med. 1983; 40(4): 413-9.
  177. Hua MS, et al. Chronic elemental mercury intoxication. Brain Inj. 1996; 10(5): 377-84.
  178. Gunther W, et al. Repeated neurobehavioral investigations in workers. Neurotoxicology. 1996; 17(3-4): 605-14.
  179. Lai M, et al. Sensitivity of MS detections by MRI. Journal of Neurology, Neurosurgery, and Psychiatry. 1996; 60(3): 339-341.
  180. 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.
  181. 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.
  182. 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.
  183. Anner BM, Moosmayer M. Mercury inhibits Na-K-ATPase primarily at the cytoplasmic side. Am J Physiol. 1992; 262(5.2): F84308.
  184. Wagner CA, Waldegger S, et al. Heavy metals inhibit Pi-induced currents through human brush-border NaPi-3 cotransporter in Xenopus oocytes. Am J Physiol. 1996; 271(4.2): F926-30.
  185. 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.
  186. 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.
  187. Hobson M, Rajanna B. Influence of mercury on uptake of dopamine and norepinephrine. Toxicol Letters. 1985; 27(2-3): 7-14.
  188. 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.
  189. 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.
  190. Hoyt KR, et al. Mechanisms of dopamine-induced cell death and differences from glutamate induced cell death. Exp Neurol. 1997; 143(2): 269-81.
  191. Offen D, et al. Antibodies from ALS patients inhibit dopamine release mediated by L-type calcium channels. Neurology. 1998; 51(4):1100-3.
  192. Huggins HA, Levy TE. Cerebrospinal fluid protein changes in MS after dental amalgam removal. Alternative Med Rev. 1998; 3(4): 295-300.
  193. Huggins H, Goldberg B. Chronic Fatigue Fibromyalgia & Environmental Illness. Future Medicine Publishing, Inc;1998: 197.
  194. Dorffer U. Anorexia hydragyra. Monatsschr Kinderheilkd. 1989; 137(8): 472.
  195. Bennett, Plum. Cecil Textbook of Medicine. 20th ed. Philadelphia: W.B. Saunders and Company; 1996: 69.
  196. Leikin, Palouchek. Poisoning & Toxicology Compendium. Cleveland: Lexi-Comp; 1998.
  197. 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.
  198. 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.
  199. 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.
  200. Verschaeve L, et al. Comparative in vitro cytogenetic studies in mercury-exposed human lymphocytes. Muta Res. 1985; 157(2-3): 221-6.
  201. Verschaeve L. Genetic damage induced by low level mercury exposure. Envir Res. 1976; 12: 306-10.
  202. Chang LW. Neurotoxic effects of mercury. Environ Res. 1977; 14(3): 329-73.
  203. Chang LW. Ultrastructural studies of the nervous system after mercury intoxication. Acta Neuropathol (Berlin). 1972; 20(2): 122-38.
  204. Klinghardt D, Mercola J. Mercury toxicity and systemic elimination agents. J of Nutritional and Environmental Medicine. 2001; 11: 53-62.
  205. Soederstroem S, et al. The effect of mercury vapor on cholinergic neurons in the fetal brain. Developmental Brain Research. 1995; 85(1): 96-108.
  206. 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.
  207. Chang LW, Hartmann HA. Blood-brain barrier dysfunction in experimental mercury. Acta Neuropathol (Berl). 1972; 21(3):179-84.
  208. Ware RA, Chang LW, Burkholder PM. An ultrastructual study on the blood-brain barrier dysfunction following mercury intoxication. Acta Neurolpathol (Berlin). 1974; 30(3): 211-214.
  209. Chang LW, et al. Prenatal and neonatal toxicology and pathology of heavy metals. Adv Pharmacol Chemother. 1980; 17: 195-231.
  210. Stejskal VDM, et al. Mercury-specific Lymphocytes: An indication of mercury allergy in man. J of Clinical Immunology. 1996; 16(1): 31-40.
  211. Shenker BJ, et al. Immunotoxic effects of mercuric compounds on human lymphocytes and monocytes: Alterations in B-cell function and viability. Immunopharmacol Immunotoxicol. 1993; 15(1): 87-112.
  212. Daum JR. Immunotoxicology of mercury and cadmium on B-lymphocytes. Int J Immunopharmacol. 1993; 15(3): 383-94.
  213. Johansson U, et al. The genotype determines the B cell response in mercury-treated mice. Int Arch Allergy Immunol. 1998; 116(4): 295-305.
  214. Zinecker S. Amalgam: Quecksilberdamfe bis ins Gehirn. Der Kassenarzt. 1992,; 32(4): 23.
  215. Malt UF, et al. Physical and mental problems attributed to dental amalgam fillings. Psychosomatic Medicine. 1997; 59: 32-41.
  216. Engel P. Beobachtungen uber die gesundheit vor und nach amalgamentfernug, Separatdruck aus schweiz. Monatsschr Zahnm. 1998; 108(8).
  217. Bangsi D, et al. Dental amalgam and multiple sclerosis. International J of Epidemiology. 1998; 27(4): 667-71.
  218. Mauch E, et al. Umweltgifte und multiple sklerose. Der Allgremeinarzt. 1996; 20: 2226-2220.
  219. Su M, et al. Selective involvement of large motor neurons in the spinal cord of rats treated with methyl mercury. J Neurol Sci. 1998; 156(1): 12-7.
  220. Moller, Madsen, Danscher. Localization of mercury in CNS of the rat. Environ Res. 1986; 41: 29-43.
  221. Baasch E. Is multiple sclerosis a mercury allergy? Schweiz arch Neurol Neurochir Psichiatr. 1966; 98: 1-19.
  222. Clausen J. Mercury and MS. Acta Neurol Scand. 1993; 87: 461.
  223. Le Quesne P. Metal-induced diseases of the nervous system. Br J Hosp Med. 1982; 28: 534.
  224. Danscher G, et al. Localization of mercury in the CNS. Environ Res. 1986; 41: 29-43.
  225. Danscher G, Horsted-Bindslev P, Rungby J. Traces of mercury in organs from with amalgam fillings. Exp Mol Pathol. 1990; 52(3): 291-9.
  226. Danscher G, et al. Ultrastructural localization of mercury after exposure to mercury vapor. Prog Histochem Cytochem. 1991; 23: 249-255.
  227. Pamphlett R, Coote P. Entry of low doses of mercury vapor into the nervous system, Neurotoxicology. 1998; 19(1): 39-47.
  228. Pamphlett, et al. Oxidative damage to nucleic acids in motor neurons containing Hg. J Neurol Sci. 1998; 159(2): 121-6.
  229. Pamphlett R, Waley P. Motor neuron uptake of low dose inorganic mercury. J Neurological Sciences. 1996; 135: 63-67.
  230. 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.
  231. 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.
  232. Arvidson B. Inorganic mercury is transported from muscular nerve terminasl to spinal and brainstem motorneurons. Muscle Nerve. 1992; 15: 1089-94.
  233. Arvidson B, et al. Retograde axonal transport of mercury in primary sensory neurons. Acta Neurol Scand. 1990; 82: 324-237.
  234. Candura SM, et al. Effects of mercuryic chloride and methylmercury on cholinergic neuromusular transmission. Pharmacol Toxicol. 1997; 80(5): 218-24.
  235. Castoldi AF, et al. Interaction of mercury compounds with muscarinic receptor subtypes in the rat brain. Neurotoxicology. 1996; 17(3-4): 735-41.
  236. Wilkinson LJ, Waring RH. Cysteine dioxygenase: modulation of expression in human cell lines by cytokines and control of sulphate production. Toxicol In Vitro. 2002; 16(4): 481-3.
  237. Tanner CM, et al. Abnormal liver enzyme metabolism in Parkinson’s. Neurology. 1991; 41(5.2): 89-92.
  238. 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.
  239. Pean A, et al. Pathways of cysteine metabolism in MND/ALS. J Neurol Sci. 1994; 124: 59-61.
  240. Steventon GB, et al. Xenobiotic metabolism in motor neuron disease. Lancet. 1988: 644-47.
  241. Gordon C, et al. Abnormal sulphur oxidation in systemic lupus erythrmatosus (SLE). Lancet. 1992; 339: 8784-6.
  242. Emory P, et al. Poor sulphoxidation in patients with rheumatoid arthritis. Ann Rheum Dis. 1992; 1(3): 318-20.
  243. 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.
  244. Freitas AJ, et al. Effects of Hg2+ and CH3Hg+ on Ca2+ fluxes in the rat brain. Brain Res. 1996; 738(2): 257-64.
  245. 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.
  246. Chavez E, et al. Mitochondrial calcium release by Hg+2. J Biol Chem. 1988; 263(8): 3582.
  247. Szucs, 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.
  248. Busselberg D. Calcium channels as target sites of heavy metals. Toxicol Lett. 1995; 82-83: 255-61.
  249. Rossi AD, et al. Modifications of Ca2+ signaling by inorganic mercury in PC12 cells. FASEB J. 1993; 7: 1507-14.
  250. Benga G. Water exchange through erythrocyte membranes. Neurol Neurochir Pol. 1997; 31(5): 905-13.
  251. Kistner A. Quecksilbervergiftung durch amalgam: Diagnose und therapie. ZWR. 1995; 104(5): 412-417.
  252. Maas C, Bruck W. Study on the significance of mercury accumulation in the brain from dental amalgam fillings through direct mouth-nose-brain transport. Zentralbl Hyg Umweltmed. 1996; 198(3): 275-91.
  253. Villegas J, Martinez R, Andres A, Crespo D. Accumulation of mercury in neurosecretory neurons of mice after long-term exposure to oral mercuric chloride. Neurosci Lett. 1999; 271: 93-96.
  254. Kozik MB, Gramza G. Histochemical changes in the neurosecretory hypothalic nuclei as a result of an intoxication with mercury compounds. Acta Histochem. 1980; 22: 367-80.
  255. Kostler W. Beeinflubung der zellularen immunabwehr drch quecksilberfreisetzung, forum prakt. Allgem Arzt. 1991; 30(2): 62-3.
  256. Reinhardt JW. Side effects: Mercury contribution to burden from dental amalgam. Adv Dent Res. 1992; 6: 110-3.
  257. Stejskal VDM, Danersund A, Lindvall A, et al. Metal-specific memory lymphoctes: Biomarkers of sensitivity in man. Neuroendocrinology Letters. 1999.
  258. Prochazkova J, Kucerova H, Bartova J, Stejskal VD. The beneficial effect of amalgam replacement on health in patients with autoimmunity. Neuroendocrinology Letters. 2004; 23(3): 211-8.
  259. Sterzl I, Prochazkova J, Stejaskal VDM, et al. Mercury and nickel allergy: risk factors in fatigue and autoimmunity. Neuroendocrinology Letters. 1999; 20: 221-228.
  260. Atchison WD. Effects of neurotoxicants on synaptic transmission. Neuroltoxicol Teratol. 1998; 10(5): 393-416.
  261. Melchart D, Wuhr E, Weidenhammer W, Kremers L. A multicenter survey of amalgam fillings and subjective complaints in non-selected patients in the dental practice. Eur J Oral Sci. 1998; 106: 770-77.
  262. Gebbart E. Chromosone damage in individuals exposed to heavy metals. Curr Top Environ Toxicol Chem. 1985; 8: 213-25.
  263. Fleming L, et al. Parkinson’s disease and brain levels of organochlorine pesticides (dieldren). Annals of Neurology. 1994; 36(1): 100-03.
  264. Hileman, Bette. The environment and Parkinson’s. Chemical & Engineering News. 2001.
  265. Nasuti C, Cantalamessa F. Dopaminergic system modulation, behavioral changes, and oxidative stress after neonata. Toxicology. 2007; 229(3): 194-205.
  266. Müller-Mohnssen H, Hahn K. A new method for early detection of neurotoxic diseases (exemplified by pyrethroid poisoning). Gesundheitswesen. 1995; 57(4): 214-22.
  267. McDaniel KL, Moser VC. Utility of a neurobehavioral screening battery for differentiating the effects of two pyrethroids, permethrin and cypermethrin. Neurotoxicol Teratol. 1993; 15(2):71-83.
  268. Stejskal J, Stejskal V. The role of metals in autoimmune diseases and the link to neuroendocrinology. Neuroendocrinology Letters. 1999; 20: 345-358.
  269. 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.
  270. 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.
  271. Leigh PN. Pathologic mechanisms in ALS and other motor neuron diseases. In: Calne DB, eds. Neurodegenerative Diseases. Philadelphia: W. B. Saunder Co; 1997: 473-88.
  272. 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.
  273. Kim P, Choi BH. Selective inhibition of glutamate uptake by mercury in cultured mouse astrocytes. Yonsei Med J. 1995; 36(3): 299-305.
  274. Albrecht J, Matyja E. Glutamate: A potential mediator of inorganic mercury toxicity. Metab Brain Dis. 1996; 11: 175-84.
  275. 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.
  276. 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.
  277. 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.
  278. 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.
  279. Munch G, Gerlach M, Sian J, Wong A, Riederer P. Advanced glycation end products in neurodegeneration: More than early markers of oxidative stress? Ann Neurol. 1998; 44(3.1): S85-8.
  280. Crinnion WJ. Environmental toxins and their common health effects. Altern Med Rev. 2000; 5(3): 209-23.
  281. 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.
  282. Salinska E, Kuznicki J. Calcium ions in neuronal degeneration. IUBMB Life. 2008; 60(9): 575-90.
  283. Olanow CW, Arendash GW. Metals and free radicals in neurodegeneration. Curr Opin Neurol. 1994; 7(6): 548-58.
  284. Troy CM, Shelanski ML. Down-regulation of copper/zinc superoxide dismutase causes apoptotic death in PC12 neuronal cells. Proc Nat Acad Sci, USA. 1994; 91(14): 6384-7.
  285. Rothstein JD, Dristol LA, Hosier B, Brown RH, Kunci RW. Chronic inhibition of superoxide dismutase produces apoptotic death of spinal neurons. Proc Nat Acad Sci, USA. 1994; 91(10): 4155-9.
  286. Beal MF. Coenzyme Q10 administration and its potential for treatment of neurodegenerative diseases. Biofactors. 1999; 9(2-4): 262-6.
  287. DiMauro S, Moses LG. CoQ10 use leads to dramatic improvements in patients with muscular disorder. Neurology. 2001.
  288. Schultz C, et al. CoQ10 slows progression of Parkinson’s disease. Archives of Neurology. 2002.
  289. Matthews RT, Yang L, Browne S, Baik M, Beal MF. Coenzyme Q10 administration increases brain mitochondrial concentrations and exerts neuroprotective effects. Proc Nat Acad Sci, USA. 1998; 95(15): 8892-7.
  290. 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.
  291. 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.
  292. Gooch C, et al. Eleanor & Lou Gehrig MDA/ALS center at columbia-presbyterian medical center in New York. ALS Newsletter. 2001; 6(3).
  293. 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.
  294. 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.
  295. Ho PI, Collins SC, et al. Homocysteine potentiates beta-amyloid neurotoxicity: role of oxidative stress. J Neurochem. 2001; 78(2): 249-53.
  296. van Benschoten MM. Acupoint energetics of mercury toxicity and amalgam removal with case studies. American Journal of Acupuncture. 1994; 22(3): 251-262.
  297. Landner L, Lindestrom L. Copper in Society and the Environment. 2nd ed. Swedish Environmental Research Group (MFG); 1999.
  298. White AR, Cappai R, Neurotoxicity from glutathione depletion is dependent on extracellular trace copper. J Neurosci Res. 2003; 71(6): 889-97.
  299. Kobayashi MS, Han D, Packer L. Antioxidants and herbal extracts protect HT-4 neuronal cells against glutamate-induced cytotoxicity. Free Radical Research. 2000; 32(2):115-24.
  300. Ferrante RJ, Klein AM, Dedeoglu A, Beal MF. Therapeutic efficacy of EGb761 (Gingko biloba extract) in a transgenic mouse model of amyotrophic lateral sclerosis. J Mol Neurosci. 2001; 17(1): 89-96.
  301. 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.
  302. Li Y, Liu L, Barger SW, Mrak RE, Griffin WS. Vitamin E suppression of microglial activation is neuroprotective. J Neurosci Res. 2001; 66(2): 163-70.
  303. Prasad KN, Cole WC, Kumar B. Multiple antioxidants in the prevention and treatment of Parkinson’s disease. Journal of the American College of Nutrition. 1999; 18(5): 413-423.
  304. Mishra S, Palanivelu K. The effect of curcumin (turmeric) on Alzheimer’s disease: An overview. Annals of Indian Academy of Neurology. 2008; 11(1): 13-19.
  305. Baum L, Ng A. Curcumin interaction with copper and iron suggests one possible mechanism of action in Alzheimer’s disease animal models. Alzheimer’s Dis. 2004; 6: 367-77.
  306. Daniel S, Limson JL, Dairam A, Watkins GM, Daya S. Through metal binding, curcumin protects against lead- and cadmium-induced lipid peroxidation in rat brain homogenates and against lead-induced tissue damage in rat brain. J Inorg Biochem. 2004; 98: 266-75.
  307. Canesi M, Perbellini L, Pezzoli G. Poor metabolization of n-hexane in Parkinson’s disease. J Neurol. 2003; 250(5): 556-60.
  308. Leistevuo J, Pyy L, Osterblad M. Dental amalgam fillings and the amount of organic mercury in human saliva. Caries Res. 2001; 35(3): 163-6.
  309. Appel SH, Beers D, Siklos L, Engelhardt JI, Mosier DR. Calcium: The Darth Vader of ALS. Amyotroph Lateral Scler Other Motor Neuron Disord. 2001; 2(1): S47-54.
  310. Earl C, Chantry A, Mohammad N. Zinc ions stabilize the association of basic protein with brain myelin membranes. J Neurochem. 1988; 51: 718-24.
  311. Riccio P, Giovanneli S, Bobba A. Specificity of zinc binding to myelin basic protein. Neurochem Res. 1995; 20: 1107-13.
  312. 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.
  313. 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.
  314. Yasui M, Kihira T, Ota K, Mukoyama M, Adachi K. Aluminum deposition in the central nervous system tissues of patients with Parkinson’s disease. Rinsho Shinkeigaku. 1991; 31(10): 1095-8.
  315. Oyanagi K, Kawakami E, Yasui M. Magnesium deficiency over generations in rats with special references to the pathogenesis of the Parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam. Neuropathology. 2006; 26(2): 115-28.
  316. Garruto RM. Yanagihara R, Salazar AM, Amyx HL, Gajdusek DC. Low-calcium, high-aluminum diet-induced motor neuron pathology in cynomolgus monkeys. Acta Neuropathol. 1989; 78(2): 210-9.
  317. Yasui M, Yoshida M, Tamaki T, Taniguchi Y, Ota K. Similarities in calcium and magnesium metabolism between amyotrophic lateral sclerosis and Parkinsonian-dementia and calcification of the spinal cord in the Kii Peninsula ALS focus. No To Shinkei. 1997; 49(8): 745-51.
  318. 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.
  319. 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.
  320. 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.
  321. Anuradha B, Varalakshmi P. Protective role of DL-alpha-lipoic acid against mercury-induced neural lipid peroxidation. Pharmacol Res. 1999; 39(1): 67-80.
  322. Uversky VN, Li J, Fink AL. Metal-triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein. A possible molecular NK between Parkinson’s disease and heavy metal exposure. J Biol Chem. 2001; 276(47): 44284-96.
  323. Uversky VN, Li J, Bower K, Fink AL. Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: implications for Parkinson’s disease. Neurotoxicology. 2002; 23(4-5): 527-36.
  324. Beuter A, de Geoffroy A, Edwards R. Quantitative analysis of rapid pointing movements in Cree subjects exposed to mercury and in subjects with neurological deficits. Environ Res. 1999; 80(1): 50-63.
  325. Packer L, Tritschler HJ, Wessel K. Neuroprotection by the metabolic antioxidant alpha-lipoic acid. Free Radic Biol Med. 1997; 22(1-2): 359-78.
  326. McCarty MF. Versatile cytoprotective activity of lipoic acid may reflect its ability to activate signalling intermediates that trigger the heat-shock and phase II responses. Med Hypotheses. 2001; 57(3): 313-7.
  327. 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; 37(1): 74-6.
  328. Patrick L. Mercury toxicity and antioxidants: Part 1: Role of glutathione and alpha-lipoic acid in the treatment of mercury toxicity. Altern Med Rev. 2002; 7(6): 456-71.
  329. Gregus Z, et al. Effect of lipoic acid on biliary excretion of glutathione and metals. Toxicol App Pharmacol. 1992; 114(1): 88-96.
  330. Pritchard C, et al. Pollutants appear to be the cause of the huge rise in degenerative neurological conditions. Public Health. 2004.
  331. Leng Y, Ma CH, Zhang J, Ren M, Chuang DM. Combined lithium and valproate treatment delays disease onset, reduces neurological deficits and prolongs survival in an amyotrophic lateral sclerosis mouse model. Neuroscience. 2008; 155(3): 567-72.
  332. Limson J, Nyokong T, Daya S. The interaction of melatonin and its precursors with aluminum, cadmium, copper, iron, lead, and zinc: an adsorptive voltammetric study. J Pineal Res. 1998; 24(1): 15-21.
  333. Waly M, et al. Activation of methionine synthase by insulin-like growth factor-1 and dopamine: A target for neurodevelopmental toxins and thimerosal. Molecular Psychiatry. 2004: 1-13.
  334. Wojcik DP, Godfrey ME, Christie D, Haley BE. Mercury toxicity presenting as chronic fatigue, memory impairment and depression: Diagnosis, treatment, susceptibility, and outcomes in a New Zealand general practice setting (1994–2006). Neuroendocrinology Letters. 2006; 27(4).
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