Causes of damage to the endothelium
Stress (physical & oxidative) causes inflammation and ultimatly damage to the endothelium and plaque formation and heart problem.
Prevention and repair of endothelium damage need proper nutrion and aviodance other causative factors as discussed earlier.
Roles of nutrients L-Proline & L-Lysine for removal of plaques.
Damaged endothelial lining has lysine binding sites.
Lipoprotein (Lp(a)) molecule is free flowing in the blood and has two segments: Lipo and protein.
The lipo segments have has attachment site (receptor) to attached both lysine and l-proline to it.
The protein segments have attachment sites (receptor) for both fibrinogen and calcium to adhere to it.
The damaged endothelium is exposed to lumen of the blood vessels and attracts lipoprotiens to attached to it. This is one of the causes of formation of plaque (patch or scab) over damaged endothelium. If this is not corrected, more plaques form and area gets thicker and thicker and obstruct blood flow by itself as a blocker or breaks up as thrombus and obstructs further down the path of blood flow.
L-lysine and l-proline remove and prevent plaque formation two ways.
a) They combined with other nutrients bind with the attached Lp(a) molecules in the plaque. Then they release Lp(a) and other atherogenic lipoproteins from the plaque and breakes away, transpored to the liver, where they are removed.
b) L-lysine and l-proline bind to Lipoprotein Lp(a) molecules at the receptor sites in blood stream. Once this happens, the Lp(a) molecule is blocked. It nolonger can attached to damaged artery wall. L-lysine and l-proline form a protective barrier around the Lp(a) molecules and thus prevent from more plaque formation.
Vitamin C along with other factors are necessary for connective tissue (collagen) formation and to maitain blood vessels health.
Vitamin C deficiency can lead to plaque formation in the blood vessels.
Dr. Linus Pauling & Dr. Matthias Rath Explain How the Pauling Therapy Works
“If your body is suffering from a chronic nutritional deficiency, however, this simple and easy repair job doesn’t get done or it gets done with defective Elastin. Either way the lesions in your endothelium expose lysine binding sites to the blood. The lipo segment of the free floating Lipoprotein(a) molecules, which have lysine residuals attached to it, are deposited at the site of the lesion. The protein segment of the Lp(a) molecules have residuals that encourage both fibrinogen and calcium to adhere to it. This is the etiology [cause] of plaque formation.
“....If you are healthy, your body simply repairs the damage by manufacturing and laying down Elastin [a form of collagen] to make your arteries as good as new."
Hypothesis: Lipoprotein(a) is a Surrogate for Ascorbate. Linus Pauling and Matthias Rath. Proceedings of the National Academy of Sciences USA, 1990, Vol 87, pgs 6204-6207.
Atherosclerosis: Its Primary Cause is Ascorbate Deficiency Leading to the Deposition of Lipoprotein(a) and Fibrinogen/Fibrin in the Vascular Wall. Matthias Rath and Linus Pauling. Journal of Orthomolecular Medicine, 1991, Vol 6, pgs 125-134.
Apoprotein(a) is an Adhesive Protein. Matthias Rath and Linus Pauling. Journal of Orthomolecular Medicine, 1991, Vol 6, pgs 139-143.
A Unified Theory of Human Cardiovascular Disease Leading the Way to the Abolition of this Disease as a Cause for Human Mortality. Matthias Rath and Linus Pauling. Journal of Orthomolecular Medicine, 1992, Vol 7, pgs 5-15.
Plasmin-induced Proteolysis and the Role of Apoprotein(a), Lysine, and Synthetic Lysine Analogs. Matthias Rath and Linus Pauling. Journal of Orthomolecular Medicine, 1992, Vol 7, pgs 17-23.
Lipoprotein(a) Reduction by Ascorbate. Matthias Rath. Journal of Orthomolecular Medicine, 1992, Vol 7, pgs 81-82.
Solution to the Puzzle of Human Evolution. Matthias Rath. Journal of Orthomolecular Medicine, 1992, Vol 7, pgs 73-80.
Reducing the Risk for Cardiovascular Disease with Nutritional Supplements. Matthias Rath. Journal of Orthomolecular Medicine, 1992, Vol 7, pgs 153-162.
A New Era in Medicine. Matthias Rath. Journal of Orthomolecular Medicine, 1993, Vol 8, pgs 134-135.
Why Animals Don’t Get Heart Attacks – But People Do: The Discovery that Will Eradicate Heart Disease. Matthias Rath, 1999, Matthias Rath Inc., El Dorado Hills , CA .
Journal of Orthomolecular Medicine, 6(3-4): 144-46, 1991.
Case Report: Lysine/Ascorbate-Related Amelioration of Angina Pectoris
"It is gratifying to report the first observation of the amelioration of effort angina by the use of high-dose L-lysine and ascorbate in a man with severe coronary artery disease (CAD). This regimen was based on the hypothesis that, in thrombotic atherosclerosis, lipoprotein(a) [Lp(a)]‹ size-heterogeneous, LDL- like particles d displaying independent risk activity for CAD ‹initiates plaque formation by binding to fibrin in the damaged arterial wall...... It is hoped that the remarkable outcome in this single case will motivate clinicians to examine the efficacy of lysine and ascorbate in additional cases of refractory angina.
Coronary Heart Disease Case History
Effect of the Addition of Lysine
In this predicament and with his history of restenosis, I suggested that he continue ascorbate and add 5 g of L-lysine daily (ca., six times the lysine derived from dietary protein) to try to mitigate the atherosclerotic acitivity of Lp(a).
This severe case of restenosing CAD was a difficult challenge to try to ameliorate by the addition of lysine. While a positive effect was anticipated, lysine had not been tested for activity in inhibiting or reversing Lp(a)-laden atherosclerotic plaques in hypoascorbemic guinea pigs (Rath and Pauling, 1990b). However, it was known that Lp(a) binds to lysine-Sepharose, immobilized fibrin and fibrinogen (Harpel et al., 1989); and the epithelial-cell receptor for plasminogen ( Gonzalez-Gronow et al., 1989). This binding specificity correlates with the genetic linkage on chromosome six and striking homology of apo(a) and plasminogen‹highly conserved multiple kringle-four domains, a kringle-five domain, and a protease domain (McLean et al., 1987). Moreover, using the molecular evolutionary clock, the loss in primates of the ability to synthesize ascorbate (Zuckerkandl and Pauling, 1962; Rath and Pauling, 1990a) and acquisition of Lp(a) (Maeda et al., 1983) both appear to have occurred about 40 million years ago. These observations and the presence of Lp(a) in sclerotic arteries (Rath et al., 1989; Rath and Pauling, 1990b) and in venous grafts (Cushing et al., 1989) indicate that atherosclerosis may be initiated by excess binding of Lp(a) to fibrin in vascular wall clots, thus interfering with normal fibrinolysis by plasmin. This thrombogenic activity, which is postulated to reside in plasmin-homologous domains of Lp(a), may help to stabilize the damaged vascular wall, especially in ascorbate deficiency (Scanu, Lawn, and Berg, 1991; Rath and Pauling, 1990a). Once bound to fibrin, the LDL-like domain of Lp(a) could promote atheromas (Scanu, Lawn, and Berg, 1991). In this scenario, high-dosage lysine could inhibit or reverse plaque accretion by binding to Lp(a). Independently, lysine benefits the heart as a precursor with methionine in the synthesis of L-carnitine, the molecule that carries fat into mitochondria for the synthesis of adenosine triphosphate (ATP) bond energy needed for muscular and other cellular activities...
....Whatever the pathomechanisms of atherosclerosis, the addition of lysine to medications and vitamins, including ascorbate, markedly suppressed angina pectoris in this intractable case of CAD. While a single case is anecdotal, it is hoped that its remarkable success will motivate clinicians to commence studies as soon as possible of the general applicability of lysine and ascorbate in relieving angina pectoris, so as to decrease greatly the amount of human suffering with less dependence on surgical intervention."
1. Cederblad G and Linstedt S: Metabolism of labeled carnitine in the rat. Archives of Biochemistry and Biophysics 175:173-182, 1976.
2. Cushing GL, Gaubatz JW, Nava ML, Burdick BJ, Bocan TMA, Guyton JR, Weilbaecher D, DeBakey ME, Lawrie GM and Morrisett JD: Quantitation and localization of lipoprotein(a) and B in coronary artery bypass vein grafts resected at re-operation. Arteriosclerosis 9:593-603, 1989.
3. Gonzalez-Gronow M, Edelberg J M and Pizzo SV: Further characterization of the cellular plasminogen binding site: Evidence that plasminogen 2 and lipoprotein(a) compete for the same site. Biochemistry 28:2374-2377, 1989.
4. Harpel PC, Gordon BR and Parker TS: Plasminogen catalyzes binding of lipoprotein(a) to immobilized fibrinogen and fibrin. Proc. Natl. Acad. Sci. USA 86:3847-3851, 1989.
5. Maeda N, Bliska JB and Smithies O: Recombination and balanced chromosome polymorphism suggested by DNA sequences 5' to the human deltaglobin gene. Proc. Natl. Acad. Sci. USA 80:5012-5016, 1983.
6. McLean JW, Tomlinson JE, Kuang WJ et al.: cDNA sequence of human apolipoprotein(a) is homologous to plasminogen. Nature 330:132-137, 1987.
7. Myllyla R, Majamaa K, Gunzler V, Hanuska-Abel HM and Kivirikko KI: Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl-4-hydroxylase and Iysyl hydroxylase. Journal of Biological Chemistry 259:5403-5405, 1984.
8. Rath M, Niendorf A, Reblin T, Dietel M, Krebber HJ and Beisiegel U: Detection and quantification of lipoprotein(a) in the arterial wall of 107 coronary bypass patients. Arteriosclerosis 9:579-592, 1989.
9. Rath M and Pauling L: Hypothesis: Lipoprotein(a) is a surrogate for ascorbate. Proc.. Natl. Acad. Sci. USA 87:6204-6207, 1990a.
10. Rath M and Pauling L: Immunological evidence for the accumulation of lipoprotein(a) in the atherosclerotic lesion of the hypoascorbemic guinea pig. Proc. Natl. Acad. Sci. USA 87:9388-9390, 1990b.
11. Scanu M, Lawn RM and Berg K: Lipoprotein(a) and atherosclerosis. Annals of Internal Medicine 115:209-218, 1991.
12.Zuckerkandl E and Pauling L: Molecular disease, evolution, and genic heterogeneity. In: Horizons in Biochemistry, eds. Kasha M. and Pullman B. (Academic Press, New York) pp. 189-225, 1962.
Lysine & Atherosclerosis
ARTERIOSCLEROSIS CAN BE REVERSED
PART 1 of 2
Anti-atherogenic effects of a mixture of ascorbic acid, lysine, proline, arginine, cysteine, and green tea phenolics in human aortic smooth muscle cells.
Dr. Rath Research Institute, 1260 Memorex Drive, Santa Clara, California 95050, USA.
Certain drastic behavioral modifications by arterial wall smooth muscle cells (SMC) have been considered key steps in the formation of atherosclerotic lesions: massive migration of SMC from the media to the intima layer of the vessel, dedifferentiation of SMC to proliferating phenotype, and increased secretion of inflammatory cytokines as a response to inflammatory stimuli. We investigated the anti-atherogenic effects of naturally occurring compounds (ascorbic acid, green tea extract, lysine, proline, arginine, and N-acetyl cysteine) using the model of cultured aortic SMC....data suggest that the NM of ascorbic acid, tea phenolics, and selected amino acids has potential in blocking the development of atherosclerotic lesions by inhibiting atherogenic responses of vascular SMC to pathologic stimuli and warrants in vivo studies."