The Family of Protein Kinase C in Transmembrane Signalling for Cellular Regulation
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概要
- 論文の詳細を見る
Signal-induced hydrolysis of inositol phospholipid produces two second messengers, diacylglycerol and inositol trisphosphate. Diacylglycerol activates protein kinase C, whereas inositol trisphosphate mobilizes Ca<SUP>2+</SUP> from its internal store. Analogously, signal-induced hydrolysis of choline phospholipid generates two second messengers, unsaturated free fatty acid and lysophosphatidylcholine. The free fatty acid synergizes with diacylglycerol to activate protein kinase C and causes full activation of the enzyme even at the basal level of Ca2+. On the other hand, lysophosphatidylcholine dramatically enhances cellular responses such as cell proliferation and differentiation under the conditions where diacylglycerol and Ca<SUP>2+</SUP> are available. It is likely that all of the immediate products of signal-induced degradation of inositol and choline phospholipids are involved directly in concert in the transmembrane control of cellular functions.
- 財団法人 学会誌刊行センターの論文
著者
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Asaoka Y.
Biosignal Research Center Kobe University
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Ogita K.
Department Of Pediatric Surgery Reproductive And Developmental Medicine Graduate School Of Medical S
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KIKKAWA U.
Department of Biochemistry, Kobe University School of Medicine
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KOIDE H.
Biosignal Research Center, Kobe University
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YOSHIDA K.
Biosignal Research Center, Kobe University
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OKA M.
Biosignal Research Center, Kobe University
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SHINOMURA T.
Biosignal Research Center, Kobe University
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NISHIZUKA Y.
Biosignal Research Center, Kobe University
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