Lyme eats collagen, here is how to rebuild collagen

Somebody said...
Borrelia burgdorferi binds strongly to the extracellular matrix and cells of the connective tissue, a binding apparently mediated by specific proteins and proteoglycans. We investigated the interactions between B. burgdorferi cells and intact type I collagen using hydrated lattices that reproduce features of in vivo collagen matrices. B. burgdorferi cells of several strains adhered avidly to these acellular matrices by a mechanism that was not mediated by decorin or other proteoglycans. Moreover, following adhesion to these matrices, B. burgdorferi grew and formed microcolonies.

Somebody said...


Both scurvy and Lobstein’s are basically collagen shortage diseases. But, interestingly, guess what doesn’t work for either scurvy or Lobstein’s? Eating collagen. That’s because collagen is a protein: a triple-helix, long chain protein. It’s the product of an elaborate synthesis process that occurs throughout the body.

When we consume collagen, usually in the form of food, the long chain proteins are broken down during digestion to their original amino acids. Only then can they be absorbed. Once absorbed, these amino acids are available as building blocks to support collagen synthesis throughout the body. So from a dietary perspective, your body doesn’t care (and can’t tell) if you ate a collagen supplement, cheese, quinoa, beef, or chick peas — they’re all sources of protein, and indistinguishable by the time they hit the bloodstream.

The body doesn’t treat amino acids derived from collagen any differently than any other protein source. For this reason, the idea that collagen supplementation can be an effective treatment for joint pain, osteoarthritis, or any other condition, is highly implausible, if not impossible in principle.

Somebody said...
Linus Pauling's specific therapy for cardiovascular and heart diseases are high dosages of two essential nutrients; vitamin C and the amino acid lysine.

Vitamin C is required to strengthen arteries so that the body does not try to patch arteries with "plaster casts" (atherosclerosis).

Lysine is an Lp(a) binding inhibitor, meaning at sufficient dosage it can reverse the plaster cast build-up (atherosclerotic plaques.) Lp(a) is the sticky form of LDL cholesterol that Pauling/Rath identified as the primary risk factor.


"Knowing that lysyl residues are what causes Lp(a) to stick to the wall of the artery and form atherosclerotic plaques, any physical chemist would say at once that to prevent that put the amino acid lysine in the blood to a greater extent than it is normally. – 92-year-old Linus Pauling

Somebody said...


Collagenase inhibitors: rationale for their use in treating corneal ulceration.

Berman.

Abstract

Tissue collagenases have been implicated in corneal ulceration in human corneal disease and in ulceration of the rabbit cornea that has served as a model system. Such enzymes from the rabbit and human cornea are inhibited by metal-binding agents of the EDTA type, by thiols, and by the human serum antiprotease alpha2-macroglobulin.

Determination of the relative efficacies of collagenase inhibitors indicates that EDTA and Ca-EDTA are about one hundred times more effective on a molar basis than L-cysteine and its derivatives, N-acetyl-L-cysteine and D-penicillamine.

The alpha2-macroglobulin on a molar basis, is superior as an inhibitor to the metal-binding agents and thiols. Although Ca may be a necessary cofactor of the corneal collagenases, such a requirement has not been established unequivocally. Inhibition and isotope studies do indicate a requirement for Zn. Thiols are thought to inhibit corneal collagenases by binding to or removing an intrinsic metal cofactor (Zn), and/or possibly by reducing one or more disulfide bonds. Inhibition by both EDTA-type agents and thiols is largely reversible by dialysis. The human alpha2-macroglobulin appears to inhibit corneal colleagenases irreversibly by forming tight complexes with them. Ca-EDTA, cysteine, and acetylcysteine, given as eyedrops, are able to prevent or retard ulceration in the alkali-burned rabbit cornea. They appear to have some efficacy in the prevention of corneal ulceration in humans. EDTA-type compounds are quite stable under routine storage, while acetylcysteine is more stable than cysteine. EDTA is quite toxic and should not be used as eye medication. Ca-EDTA has a low toxicity, and cysteine and acetylcysteine have even lower toxicity. It is not yet certain which inhibitor has the most favorable therapeutic index for clinical use, or is the optimal mode of drug delivery known. However, the collagenase inhibitors seem to have therapeutic promise in the prevention of corneal ulceration.

Post Edited (Lapis_29) : 11/3/2017 5:00:16 PM (GMT-6)