Oral Salt Therapy
Certain white blood cells (WBC) display several distinct mechanisms that may be employed for the purpose of killing invading microorganisms. One of these deserves particular attention in relation to killing the causative agent of Lyme disease, namely, the spirochete Borrelia burgdorferi.
Neutrophils (a class of WBC) contain two essentially different types of storage granules, peroxidase-positive granules and peroxidase-negative granules. Peroxidase-positive granules contain myeloperoxidase, an enzyme that uses hypochlorous acid (HOCl) in conjunction with hydrogen peroxide, providing a source of nascent (atomic) oxygen for the purpose of killing invading microorganisms.11
Peroxidase-negative granules contain a family of large polypeptides (11 to 19 kDa) (Dalton, the unit of molecular weight) known as the cathelicidins or, in humans, hCAP-18. A segment of this larger or precursor protein (also known as a Bacteriacidal Permeability-Increasing (BPI) protein) is proteolytically removed by the enzyme elastase found in peroxidase-positive granules. The better-known substrate of elastase is the elastic protein elastin, found in skin and other tissues requiring elasticity. By incorporating elastase inhibitors into skin creams, attempts are made to inhibit the activity of this enzyme, thereby decreasing the ageing of skin. In Lyme therapy there is an advantage (described below) to increasing the activity of this enzyme, thereby stimulating the natural antimicrobial system. These short peptides, ranging from 12 to 100 amino acids, have the ability to assemble into larger units that form pores in the membrane surrounding microorganisms, thereby increasing the permeability of those membranes. In humans, one of these antimicrobial peptides has been dubbed LL-37.11 See photo of a neutrophil granule precursor antimicrobial protein and peptide, 31KB .pdf, courtesy of Blood 96 (8) 2000.
Both of these proteins, the cathelicidin and elastase, meet in the phagocytic vacuole, the cytoplasmic chamber in which resides the phagocytized microorganism. Within this chamber, elastase removes a short peptide capable of forming a molecular pore in the surface membrane of the microorganism. The pore formed from a group of the cathelicidins allows the efflux of potassium ions from the organism, resulting in swelling and eventual lysis.12
Research has shown that, of all the proteins in neutrophil granules, the only protein capable of releasing the cathelicidin active peptide is elastase.13 It has been demonstrated that the activity of elastase is enhanced by an increased salt concentration.14 Through oral salt (12 g per day, see Chart 12), combined with large doses of vitamin C, the indirect killing ability of elastase is dramatically increased.15
Increasing the sodium concentration surrounding the spirochete may also facilitate cell killing by allowing sodium ions to enter the spirochete through the pore created by the antimicrobial peptide. An increased intracellular sodium concentration, combined with a decreased potassium concentration, leads to spirochete death. The exact mechanism by which the human cathelicidin LL-37 kills Bb is unknown. See Chart 8, Oral Salt Therapy for Lyme Disease. (58KB .pdf)
Post Edited (KeepHope) : 3/8/2009 1:52:04 AM (GMT-7)