Executive Summary
Immune Deficiency is Endemic in the Atomic Age
Due to its electronegativity, fluorine atoms have the highest propensity of all elements to attract electrons and to react with trace minerals in skeletal bone. This results in the depletion of trace minerals used in the enzyme repair process of lymphocytes (T-cells, B-cells and NK cells), neutrophils, and monocytes/macrophages.
Not only do fluorides accumulate in skeletal bone, but complexes of fluoride also have a propensity to accumulate in the pineal, pituitary and thyroid glands. The light-transducing pineal gland is responsible for synthesizing the structurally simple hormone melatonin from serotonin. Fluoride is a melatonin receptor (G protein-coupled cell surfaces – Mel1A and Mel1B) antagonist, which is to say, fluoride complexes will bind to active receptor sites reserved for melatonin agonists, disrupting normal neuronal connectivity. The longevity of the fluoride-antagonist-receptor complex is high, due to the electronegativity of fluorides. The ionic non-covalent bond formed between the fluoride complex (cation) and the receptor site (anion) is a strong and long one. Resultantly, as Mel1A and Mel1B-type receptor sites are found in largest concentration in the anterior pituitary, hypothalamus and retina, the antagonistic behavior of fluorides impact reproductive functions and sleep activity in mammals. G protein-coupled cell surface antagonism in the retina also leads to sleep disturbances, as light-dark information is not carried properly from the retina to the pineal gland; this, in-turn, disrupts the pituitary’s thyroid-stimulating hormone (TSH).
The Strontium 90 (90Sr) — Fluoride Connection
90Sr, not to be confused with natural strontium, which is nonradioactive and nontoxic, is a radioactive isotope of strontium produced in nuclear fission that, like calcium, seeks bone, and which is ubiquitous in the environment.
The action of 90Sr in skeletal bone is also similar to the action of fluorides. 90Sr lodged in bone and soft tissue emits high-energy electrons and beta particles. When beta particles strike DNA, spontaneous and irreversible mutations arise. Chronic low-dose beta particle emissions also increase reactive oxygen species formation, which compete for trace minerals in bone.
*** Glutathione on the Butcher Block ***
When fluorides complex with aluminum (AlFx), they create G protein-coupled cell surface antagonists that compete with trace minerals, disrupt basic neuronal and hormonal communication and contribute to the subsequent depletion of glutathione (GSH), a major cellular endogenous antioxidant. Oxidative stress from fluoride exposure is shown as levels of GSH decrease when fluoride levels increase. Concomitantly, levels of oxidized GSH (GSSH) increase, which is the primary indicator of oxidative stress.
Few systems in the body do not depend, in some measure, upon glutathione. It is required for DNA synthesis and repair, an issue already exacerbated by low-dose beta ray emissions from 90Sr; it is required for protein synthesis, prostaglandin synthesis, amino acid transport and enzyme activation. Absent sufficient levels of glutathione, the immune, neurological, pulmonary, and gastrointestinal systems are at risk of collapse.
GSH damage and impairment of Phase I and Phase II glutathione clearance results in the buildup of toxic metals. The loss of the liver-bile pathway places greater metals clearance demand on the kidneys, which sets the stage for a low-pH state, metabolic acidosis and renal failure. Toxic metal buildup causes cellular mitochondria to produce free radicals at an increased rate, which requires the upregulation of the superoxide dimutase enzymes (Mn-SOD). Mn-SOD in turn employ all the trace mineral manganese, which upsets the production of cytokine interferon (IFN) and effective 2-5A[-signaled] RNase L enzymes.
Oxidative stress in the cells results in the mutation of the 2-5A[-signaled] RNase L enzyme from its average 83kDa MW to an ineffective 37kDa MW (the 2-5A [-signaled] RNase L enzyme is the primary enzyme within cells that kills viral RNA by cleaving it, sets up cell apoptosis, and enlists NK and macrophage cells). This mutation thusly permits cancer viruses, HIV, CMV, and EBV to replicate.
N-Acetylcysteine: A Practical Defense (Treatment?)
Magnesium (Mg) is responsible for the production of no fewer than 300 enzymes vital for systemic homeostasis and fluoride (F-) ions are instrumental in critical Mg deficiency. F- has a not inconsiderable affinity for Mg ions, and bonds with Mg to form MgF+ and MgF2, both of which prevent the proper absorption of Mg through intestinal cell walls. Diets deficient in Mg create an opportunistic environment for F- accumulation.
- elevate concentrations of assimilable Mg
- increase urinary fluoride excretion and
- via chelation, prevent the complexing of F- with Mg (the F- ions are the ligands which form metal complexes [coordination complexes] with N-acetylcysteine, boron, and other chelating compounds).
Specifically, N-acetylcysteine in the stomach prevents the complexing of Mg and other trace minerals and elements with electronegative sodium fluoride (NaF) by forming coordination complexes with F- ions, rendering NaF chemically inert. F-, consequently, also is unable to complex with aluminum to form AlFx.
Lastly, F- may additionally act by reacting with adjacent thiol residues (organosulfur compounds) on metabolic enzymes, creating a chelate complex that inhibits the affected enzyme’s activity. N-acetylcysteine, like the anti-Lewisite Dimercaprol or alpha lipoic acid, competes with the thiol groups for binding the F- ion, which is then excreted in the urine.
