A possible role of protein kinase C in signal-induced lysosomal enzyme release.
In platelets, activation of protein kinase C and mobilization of Ca2+ were selectively induced by the addition of 1-oleoyl-2-acetyl-glycerol and a low concentration of A23187, respectively (Kaibuchi, K., Takai, Y., Sawamura, M., Hoshijima, M., Fujikura, T. and Nishizuka, Y. (1983) J. Biol. Chem. 258, 6701-6704). Using this procedure evidence was obtained suggesting that the protein phosphorylation and Ca2+ mobilization were both essential and synergistically effective to cause release of lysosomal acid hydrolases such as N-acetylglucosaminidase. A similar observation was made for the lysosomal enzyme release from rat neutrophils.
D000818:Animals; D001792:Blood Platelets / Q000201:enzymology; D000001:Calcimycin / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism; D004789:Enzyme Activation; D008247:Lysosomes / Q000201:enzymology*; D008970:Molecular Weight; D009504:Neutrophils / Q000201:enzymology; D011493:Protein Kinase C; D011494:Protein Kinases / Q000097:blood*; D011817:Rabbits; D051381:Rats; D013997:Time Factors
D000001:Calcimycin; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium