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A possible role of protein kinase C in signal-induced lysosomal enzyme release.

作者信息

Kajikawa N, Kaibuchi K, Matsubara T, Kikkawa U, Takai Y, Nishizuka Y, Itoh K, Tomioka C

出版信息

Biochem Biophys Res Commun. 1983 Oct 31;116(2):743-50. doi: 10.1016/0006-291x(83)90587-9.

Abstract

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.

摘要

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