Townsend Letter to Doctors: Salt/C for Lyme

[Guest guest]

I saw this on and thought some might be interested. I admit

is

sounds too good to be true, but some over there, and on lymestrategies are

finding

benefit, after trying everything else.

I don't have lyme (at least I doubt it!), but I know some of my new friends here

do, so

thought you might want to see this article (I think it's only part of it...it's

all way to

technoscientific for me...)

Dan

* Here is the article in JAN 2005 Townsend letter to Doctors

" 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

LD, 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 H2O2, providing a

source of nascent (atomic) oxygen for the purpose of killing invading

organisms.

Peroxidase-negative granules contain a family of large polypeptides (11 to

19kDa) known as the cathelicidins or, in humans, hCAP-18. A segment of this

larger or precursor protein (aka 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 prtoein 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 microbial peptides has been dubbed

LL-37.

" 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.

Research has shown that, of all the proteins in neutrophil granules, the

only protein capable of releasing the cathelicidin active peptide is

elastase. It has been demonstrated that the activity of elastase is enhanced

by an increased salt concentration. Through oral salt (12g per day, see

Chart 12), combined with large doses of Vit. C, the indirect killing ability

of elastase is dramatically increased.

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, leads to spirochete death. The exact

mechanism by which the human cathelicidin LL-37 kills Bb is unknown.