The heat-stable protein kinase C (PKC) stimulatory factor in the rat ovary may allow PKC to be active independent of cell membrane lipids.
A protein kinase C (PKC) stimulatory factor in heat-treated ovarian cytosol appears to be protein in nature as it was susceptible to proteinase K digestion and strong acid, and its lipid-substituting properties were retained after extraction of lipids. Phosphorylation of substrate by PKC stimulated by the factor from heat-treated ovarian cytosol in the absence of lipids was subject to dephosphorylation by the ovarian phosphatase. The factor stimulated purified PKC obtained from a commercial source as well as PKC partially purified from rat brain. Heat-treated ovarian cytosol stimulated PKC phosphorylation of myelin basic protein, but not protamine sulphate, in a calcium-dependent manner.
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K M
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Department of Physiology and Pharmacology, University of South Dakota, School of Medicine, Vermillion 57069-2390, USA.
D000818:Animals; D001685:Biological Factors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001921:Brain / Q000187:drug effects / Q000201:enzymology*; D003600:Cytosol / Q000737:chemistry; D019286:Endopeptidase K; D004789:Enzyme Activation / Q000187:drug effects; D005260:Female; D006358:Hot Temperature; D008563:Membrane Lipids / Q000494:pharmacology*; D004676:Myelin Basic Protein / Q000378:metabolism; D010053:Ovary / Q000737:chemistry* / Q000201:enzymology; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism; D010766:Phosphorylation; D011479:Protamines / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D017207:Rats, Sprague-Dawley; D012697:Serine Endopeptidases / Q000494:pharmacology
D001685:Biological Factors; D008563:Membrane Lipids; D004676:Myelin Basic Protein; D011479:Protamines; D011493:Protein Kinase C; D010744:Phosphoric Monoester Hydrolases; D012697:Serine Endopeptidases; D019286:Endopeptidase K