6．リン脂質代謝と三量体Gタンパク質 : 三量体Gタンパク質研究の現状
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Phosphoinositide-specific phospholipase C (PI-PLC) catalyzes the hydrolysis of phosphatidylinositol 4, 5-bisphosphate to inositol 1, 4, 5-trisphosphate (IP<SUB>3</SUB>) and diacylglycerol. IP<SUB>3</SUB> induces the release of Ca<SUP>2+</SUP> from intracellular stores, and diacylglycerol acts as the physiological activator of protein kinase C. Several distinct PI-PLC enzymes have been identified from various cells. Based on the primary sequences, PI-PLC isozymes are divided into three families: PLC-β, PLC-γ, and PLC-δ. Substantial evidence has strongly suggested that G proteins regulate PI-PLC in various cell-stimulation systems and that there might be two distinct pathways (pertussis toxin-sensitive and pertussis toxin-insensitive). Recently, it has become apparent that β-type PLC isoforms are activated by the heterotrimeric G protein subfamily G<SUB>q</SUB>. Careful studies using in vitro and in vivo reconstitution systems have further suggested that the α-subunits of G<SUB>q/11/16</SUB> specifically regulate PLC-β<SUB>1</SUB> and PLC-β<SUB>3</SUB> and that the βγ-subunits of the G<SUB>i</SUB> subfamily interact with PLC-β<SUB>2</SUB>, which are considered to be responsible for the pertussis toxin-insensitive and the pertussis toxin-sensitive pathways, respectively. In this paper, involvement of G proteins in the regulation of phospholipase A<SUB>2</SUB> and phosphatidylcholine-specific PLC and PLD is also discussed.
- 社団法人 日本薬理学会の論文
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