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Updated: Aug 8, 2026

Assessment of Mitochondrial Functions and Cell Viability in Renal Cells Overexpressing Protein Kinase C Isozymes
Published on: January 7, 2013
Altered protein kinase C activity and its endogenous protein phosphorylation in rat liver after administration of
1Hokkaido Branch Laboratory, National Institute of Animal Health, Sapporo, Japan.
Abstract:
Ethionine, an ethyl analogue of methionine, induces fatty liver in rats. The effects of ethionine administration on protein kinase C (PKC) in rat liver was examined. By a single administration at a dose of 0.5 mg/g body wt., liver PKC activity was increased in both cytosolic and total particulate fractions. The increase in cytosol was significant, even at 4 h after administration, when compared with control rat liver cytosol. On the other hand, a 4-day consecutive administration (0.5 mg/g per day) resulted in decreased PKC activity, particularly in cytosol, when compared with the control. Protein phosphorylation in liver catalyzed by PKC was found to be enhanced by ethionine, irrespective of the mode of administration. The enhanced phosphorylation was observed in both cytosolic and total particulate fractions. The change of PKC activity, and the phosphorylation of its endogenous substrates, are postulated to be involved in the pathogenesis of ethionine-induced fatty liver of rats.
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