Protein kinase C from small intestine epithelial cells

Biochemical and Biophysical Research Communications
G VelascoP S Lazo

Abstract

Protein kinase C activity has been identified in cytosolic and membrane fractions from rat and rabbit small intestine epithelial cells. The cytosolic fraction comprised about the 75% of total activity. Protein kinase C activity was resolved from other protein kinase activities by ion exchange chromatography. Phosphatidylserine or phosphatidylinositol were required for protein kinase C to be active. In addition, the activity was enhanced by the presence of a diacylglycerol. Diolein and dimyristin were the most effective (13-14 fold activation). In the presence of phosphatidylserine and diolein, the Ka for activation by Ca2+ was 10(-7)M. The phorbol ester TPA substituted for diacylglycerol in activating protein kinase C. Brush border and basolateral membranes contained protein kinase C activity, although the specific activity of the basal lateral membranes was four-fold higher than the specific activity of the brush border membranes. The presence of PKC in small intestine epithelial cells might have important implications in the Ca2+ mediated control of ionic transport in this tissue.

References

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Citations

Oct 1, 1994·Pflügers Archiv : European journal of physiology·A ItohY Okada
Jan 1, 1996·The International Journal of Biochemistry & Cell Biology·J Usta, I F Durr
Jul 8, 2008·The Journal of Nutritional Biochemistry·Abid Hamid, Jyotdeep Kaur
Dec 1, 1993·Bioscience Reports·P García-ParamioJ C Prieto
Jul 15, 1988·Biochemical and Biophysical Research Communications·B S Baliga, S M Borowitz
Sep 15, 1988·Biochemical and Biophysical Research Communications·S AzharE Reaven

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