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Protein kinase C‐dependent phosphorylation and mitochondrial translocation of aldose reductase
Author(s) -
Varma Tushar,
Liu Si-Qi,
West Matthew,
Thongboonkerd Visith,
Ruvolo Peter P.,
May W.Stratford,
Bhatnagar Aruni
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03834-6
Subject(s) - aldose reductase , protein kinase c , phosphorylation , biochemistry , protein kinase a , microbiology and biotechnology , substrate level phosphorylation , kinase , aldehyde reductase , chromosomal translocation , chemistry , mitochondrion , oxidative phosphorylation , biology , enzyme , gene
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.