Protein N -homocysteinylation: implications for atherosclerosis
Biomedicine & Pharmacotherapy, ISSN: 0753-3322, Vol: 55, Issue: 8, Page: 443-447
2001
- 72Citations
- 26Captures
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Metrics Details
- Citations72
- Citation Indexes72
- 72
- CrossRef52
- Captures26
- Readers26
- 26
Article Description
Elevated levels of homocysteine (Hcy) are associated with various human pathologies, including cardiovascular disease. However, it is not exactly known why Hcy is harmful. A plausible hypothesis is that the indirect incorporation of Hcy into protein, referred to as protein N -homocysteinylation, leads to cell damage. A translational pathway involves: 1) reversible S -nitrosylation of Hcy with nitric oxide produced by nitric oxide synthase; 2) aminoacylation of tRNA Met with S -nitroso-Hcy catalyzed by MetRS; and 3) transfer of S -nitroso-Hcy from S -nitroso-Hcy-tRNA Met into growing polypeptide chains at positions normally occupied by methionine. Subsequent trans-nitrosylation leaves Hcy in the protein chain. A post-translational pathway involves: 1) metabolic conversion of Hcy to thiolactone by methionyl-tRNA synthetase (MetRS), and 2) acylation of protein lysine residues by Hcy thiolactone. The levels of Hcy thiolactone and N -homocysteinylated protein in human vascular endothelial cells depend on the ratio of Hcy/Met, levels of folic acid, and HDL, factors linked to cardiovascular disease. HDL-associated human serum Hcy thiolactonase/paraoxonase hydrolyzes thiolactone to Hcy, thereby minimizing protein N -homocysteinylation. Variations in Hcy thiolactonase may play an important role in Hcy-associated human cardiovascular disease.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0753332201000853; http://dx.doi.org/10.1016/s0753-3322(01)00085-3; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0034802174&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/11686577; http://linkinghub.elsevier.com/retrieve/pii/S0753332201000853; http://api.elsevier.com/content/article/PII:S0753332201000853?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0753332201000853?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0753332201000853; http://dx.doi.org/10.1016/s0753-3322%2801%2900085-3; https://dx.doi.org/10.1016/s0753-3322%2801%2900085-3
Elsevier BV
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