[Role of GTP-binding proteins in phospholipid metabolism in human platelets].
Phosphoinositide-specific phospholipase C (PLC) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate (PIP2) to inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DG), which act as second messengers. Substantial evidence has strongly suggested that a putative G-protein (s), Gp, regulates PLC activity in human platelets. Recently, the molecular mechanism of PLC activity regulation was clarified as to two types of enzymes, PLC-gamma and PLC-beta. In this chapter, the regulatory mechanisms of the PLCs via a Gp or tyrosine kinase is summarized, and the involvement of some G-protein in the regulation of other phospholipases, phosphatidylcholine-specific PLC, phospholipase A2 and phospholipase D, is also discussed.
Nagata
K
K
Department of Biochemistry, Gifu University School of Medicine.
Nozawa
Y
Y
D001792:Blood Platelets / Q000201:enzymology / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000502:physiology*; D006801:Humans; D010739:Phospholipase D / Q000378:metabolism; D010741:Phospholipases A / Q000378:metabolism; D054467:Phospholipases A2; D010743:Phospholipids / Q000378:metabolism*; D015290:Second Messenger Systems; D013379:Substrate Specificity; D010738:Type C Phospholipases / Q000378:metabolism* / Q000502:physiology
D010743:Phospholipids; D010741:Phospholipases A; D054467:Phospholipases A2; D010738:Type C Phospholipases; D010739:Phospholipase D; D019204:GTP-Binding Proteins