期刊
FEBS LETTERS
卷 534, 期 1-3, 页码 175-179出版社
WILEY
DOI: 10.1016/S0014-5793(02)03834-6
关键词
aldose reductase; protein kinase C; smooth muscle cell; HL60; REH; phorbol ester; bryostatin-1
资金
- NCI NIH HHS [CA44649] Funding Source: Medline
- NHLBI NIH HHS [HL59378, HL54083, HL55477] Funding Source: Medline
Although aldose reductase (AR) is a critical participant in osmoregulation, and the metabolism of glucose and aldehydes derived from lipid peroxidation, post-translational mechanisms regulating its activity have not been identified. In this paper, we report that stimulation of protein kinase C (PKC) in several cell types induces phosphorylation of AR and translocation of the phosphorylated protein to the mitochondria. In vitro, recombinant AR was directly phosphorylated by activated PKC, suggesting that AR may be an in vivo PKC substrate. Together, these observations reveal a novel link between PKC activation and the regulation of glucose and aldehyde metabolism. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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