A possible role of protein kinase C in signal-induced lysosomal enzyme release |
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Authors: | N Kajikawa K Kaibuchi T Matsubara U Kikkawa Y Takai Y Nishizuka K Itoh C Tomioka |
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Affiliation: | 1. Department of Biochemistry, Kobe University School of Medicine, Kobe 650, Japan;2. Department of Cell Biology, National Institute for Basic Biology, Okazaki 444, Japan |
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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. |
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Keywords: | To whom correspondence should be addressed at the Department of Biochemistry Kobe University School of Medicine Kobe 650 Japan. |
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