What is it about?
Homocysteine (Hcy) is an important amino acid in living organisms. However, excess Hcy damages connective tissues in the heart and bones leading to disease. We have shown that Hcy chemically binds to collagen, the major component of connective tissues. The binding of Hcy involves specific lysine residues that are normally involved in formation of collagen crosslinks essential for connective tissue stability and mechanical properties. This mechanism was confirmed by findings showing that increased Hcy binding is accompanied by reduced collagen crosslinking.
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Why is it important?
We identified for the first time specific chemical mechanism, which explains how excess Hcy damages connective tissues. Our findings are important for understanding the pathophysiology induced by excess Hcy and suggest that targeting Hcy metabolite that causes collagen damage might be a good strategy to prevent Hcy-related connective tissue abnormalities.
Perspectives
Writing this article was a great pleasure as it has co-authors with whom I have had long standing collaborations. It was also satisfying as it provided an experimental proof for my hypothesis proposed some time ago regarding mechanisms underlying the Hcy-related pathophysiology.
Hieronim Jakubowski Jakubowski
Rutgers The State University of New Jersey
Read the Original
This page is a summary of: N-Homocysteinylation impairs collagen cross-linking in cystathionine -synthase-deficient mice: a novel mechanism of connective tissue abnormalities, The FASEB Journal, August 2016, Federation of American Societies For Experimental Biology (FASEB),
DOI: 10.1096/fj.201600539.
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