Protease-activated form of protein kinase C with Mr 80,000 generated from rat liver plasma membrane by trypsin-like protease.
New type of protease-activated form of protein kinase C was generated from rat liver plasma membrane by action of endogenous trypsin-like protease. The molecular mass was estimated to be about 80,000 by immunoblot analysis which was slightly smaller (approximately 2,000) than that of native protein kinase C. The protein kinase activity was 2-times stimulated by Ca2+ and phospholipid and inhibited by the synthetic peptide derived from the pseudosubstrate region of protein kinase C. This type of activated kinase was produced in purified enzyme system in the absence of either Ca2+ or phospholipid or both. These results suggest that limited proteolysis generating the active form of Mr 80,000 may occur on the inactive form of protein kinase C.
Hashimoto
E
E
Department of Biochemistry, Fukui Medical School, Japan.
Takeuchi
F
F
Yamamura
H
H
D000595:Amino Acid Sequence; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002417:Cattle; D002462:Cell Membrane / Q000201:enzymology*; D002850:Chromatography, Gel; D010450:Endopeptidases / Q000378:metabolism*; D004789:Enzyme Activation; D015151:Immunoblotting; D008099:Liver / Q000201:enzymology* / Q000648:ultrastructure; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D051381:Rats; D014357:Trypsin / Q000378:metabolism*
D011493:Protein Kinase C; D010450:Endopeptidases; D014357:Trypsin; D002118:Calcium