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Protein kinase C-dependent phosphorylation and mitochondrial translocation of aldose reductase
Authors:Varma Tushar  Liu Si Qi  West Matthew  Thongboonkerd Visith  Ruvolo Peter P  May W Stratford  Bhatnagar Aruni
Institution:Division of Anesthesiology, Department of Internal Medicine, University of Texas Medical Branch, Galveston, TX 77550, USA.
Abstract: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.
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