PMID: 8947489Nov 15, 1996Paper

Characterization of two forms of protein kinase C alpha, with different substrate specificities, from skeletal muscle

The Biochemical Journal
C Schmitz-PeifferT J Biden

Abstract

We have investigated protein kinase C (PKC) in skeletal muscle cytosol and demonstrated the presence of two major activities. These did not correspond to different PKC isoenzymes but seemed to represent two species of PKC alpha as deduced by: elution during hydroxyapatite chromatography at KH2PO4 concentrations expected of PKC alpha; detection of the two species by three specific but unrelated anti-(PKC alpha) antibodies; immunodepletion of both activities with anti-(PKC alpha) antibody; and demonstration of identical requirements of both Ca2+ ions and lipid for activation. These species, termed PKC alpha 1 and PKC alpha 2, phosphorylated the modified conventional PKC pseudosubstrate peptide (19-31, Ser-25) equally well. Importantly, however, the activities differed in that PKC alpha 1 phosphorylated histone IIIS, and also peptides derived from the EGF receptor and glycogen synthase, to a much greater extent than did PKC alpha 2. Similarly, incubation of crude muscle extracts with either PKC alpha 1 or alpha 2 gave rise to different protein phosphorylation patterns. The involvement of proteolysis, dephosphorylation or oxidative modification in the interconversion of PKC alpha 1 and PKC alpha 2 during preparation was ruled out. ...Continue Reading

Citations

Feb 18, 2016·Molecular Endocrinology·Bing M LiaoCarsten Schmitz-Peiffer
Feb 14, 2009·Molecular and Cellular Biochemistry·M Gonzalez-RiopedreJ I Ramos-Martínez
May 15, 2002·American Journal of Physiology. Endocrinology and Metabolism·R CazzolliC Schmitz-Peiffer
Jun 8, 2001·The International Journal of Biochemistry & Cell Biology·S PoussardP Cottin

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