Journal
JOURNAL OF PROTEOMICS
Volume 74, Issue 7, Pages 967-974Publisher
ELSEVIER
DOI: 10.1016/j.jprot.2011.01.021
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Funding
- Ministry of Science and Higher Education, Poland [NN 401 230634, N401 065 32/1504, N401 132 32/2670, N204 053 32/1226, POIG.01.03.01-00-097/08]
- American Heart Association [0855919D]
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Elevated levels of homocysteine (Hcy) are associated with cardiovascular and neurodegenerative diseases in humans. Hcy becomes a component of human proteins as a result of N-homocysteinylation of protein lysine residues by Hcy-thiolactone, which affects the protein's structure and function, and contributes to Hcy-related pathology. Albumin is the major target for N-homocysteinylation in human blood in vivo. Previous work has identified Lys-525 as a predominant site of N-homocysteinylation in vitro and in vivo. Here we show that Lys-4, Lys-12, Lys-137, Lys-159, Lys-205, and Lys-212 of human albumin are susceptible to N-homocysteinylation in vitro and provide evidence that two of those residues, Lys-137 and Lys-212, in addition to Lys-525, are N-homocysteinylated in vivo in human plasma. (C) 2011 Elsevier B.V. All rights reserved.
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