Lp(a) not LDL forms atherosclerotic plaques

The discussion of the Linus Pauling vitamin C/lysine invention for chronic scurvy

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Lp(a) not LDL forms atherosclerotic plaques

Post Number:#1  Post by ofonorow » Tue Apr 28, 2009 6:04 am

Rather than continue this in the OH NO NOT STATINS thread, lets discuss whether ordinary LDL can create atherosclerosis, because it is a key issue.

in 1996, I was wondering why adding proline to the Pauling therapy seemed to have such a positive effect, and I noticed an article by University of Chicago researchers. I contacted them, and they emailed me this response.


"Our study published in JCI demonstrated for the first time that L-proline can inhibit the binding of Lp(a) and apo(a) to fibrinogen in vitro conditions. However, we have no data about the physiological relevance of this finding. It is well established that the binding of Lp(a) to fibrinogen also involves the lysine binding sites of apo(a) (component of Lp(a)), therefore, the presence of lysine and lysine analogue dramatically reduce this binding. Once again, the in vivo relevance of this inhibition is unknown.

Sincerely, Olga Klezovitch, Ph.D. University of Chicago


The Pauling/Rath patent is for Lp(a) binding inhibitors, U. S. Patents # 5,230,996 and # 5,278,189, which they claim can even reverse CVD. Here is the abstract from the U. of Chicago paper. There is a free link to the entire paper.

http://www.ncbi.nlm.nih.gov/pubmed/8690 ... d_RVDocSum

Evidence that the fibrinogen binding domain of Apo(a) is outside the lysine binding site of kringle IV-10: a study involving naturally occurring lysine binding defective lipoprotein(a) phenotypes.

It is now established that the lysine binding site (LBS) of apo(a) kringle IV-10, and particularly Trp72, plays a dominant role in the binding of lipoprotein(a) [Lp(a)] to lysine. To determine the role of the LBS in the binding of Lp(a) to fibrinogen, we examined the binding to plasmin-modified (PM) fibrinogen of human and rhesus monkey Lp(a) species classified as either Lys' or Lys- based on their capacity to bind lysine Sepharose and to have Trp or Arg, respectively, in position 72 of the LBS of kringle IV-10. We also examined the free apo(a)s obtained by subjecting their corresponding parent Lp(a)s to a mild reductive procedure developed in our laboratory. Our results show that both Lyst and Lys- Lp(a)s and their derived apo(a)s, bound to PM-fibrinogen with similar affinities (Kds: 33-100 nM), whereas the B(max) values were threefold higher for apo(a)s. Both the lysine analog epsilon-aminocaproic acid and L-proline inhibited the binding of Lp(a) and apo(a) to PM fibrinogen. We conclude that the LBS of kringle IV-10 is not involved in this process and that apo(a) binds to PM-fibrinogen via a lysine-proline-sensitive domain located outside the LBS and largely masked by the interaction of apo(a) with apoB100. The significant difference in the PM fibrinogen binding capacity also suggests that apo(a) may have a comparatively higher athero-thrombogenic potential than parent Lp(a).



Again, there is no evidence that LDL (without apo(a)) can or will bind to lysine.
Owen R. Fonorow
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