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Effects of peroxynitrite-induced protein modifications on tyrosine phosphorylation and degradation.
- Source :
-
FEBS letters [FEBS Lett] 1996 Apr 29; Vol. 385 (1-2), pp. 63-6. - Publication Year :
- 1996
-
Abstract
- The ability of protein tyrosine kinases to phosphorylate a synthetic peptide was inhibited 51% by peroxynitrite-mediated nitration of tyrosine. Exposure of endothelial cells to peroxynitrite decreased the intensity of tyrosine phosphorylated proteins and increased the intensity of nitrotyrosine-containing proteins. Peroxynitrite-modified BSA was degraded by human red blood cell lysates. However, human plasma in a concentration-, time-, and temperature-dependent manner, removed the protein nitrotyrosine epitope. These results suggest that tyrosine nitration interferes with phosphorylation and targets proteins for degradation. Specific enzymatic process(es) for removing nitrotyrosine may be present in vivo.
- Subjects :
- Animals
Cattle
Endothelium, Vascular drug effects
Endothelium, Vascular metabolism
Erythrocytes metabolism
Gastrins metabolism
Humans
Peptides chemical synthesis
Peptides metabolism
Phosphorylation drug effects
Plasma
Protein-Tyrosine Kinases antagonists & inhibitors
Serum Albumin, Bovine metabolism
Nitrates pharmacology
Proteins metabolism
Tyrosine metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0014-5793
- Volume :
- 385
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 8641468
- Full Text :
- https://doi.org/10.1016/0014-5793(96)00347-x