GTP[S]对酶原颗粒膜中磷脂酶A2活性的调节；GTP结合蛋白调节的证据。
Modulation of phospholipase A2 activity in zymogen granule membranes by GTP[S]; evidence for GTP-binding protein regulation.
作者信息
Rubin R P, Withiam-Leitch M, Laychock S G
机构信息
Department of Pharmacology & Therapeutics, State University of New York, Buffalo 14214.
出版信息
Biochem Biophys Res Commun. 1991 May 31;177(1):22-6. doi: 10.1016/0006-291x(91)91942-6.
In membranes associated with purified pancreatic zymogen granules, GTP[S] elicited a concentration-dependent activation of phospholipase A2 (PLA2), which was converted to inhibition in the presence of added Ca2+. The GTP-binding protein inhibitor GDP[S] blocked both the stimulatory and inhibitory actions of GTP[S]. We conclude that in zymogen granule membranes GTP-binding proteins exert a dual regulation of PLA2 activity.
在与纯化的胰腺酶原颗粒相关的膜中，鸟苷-5'-O-(3-硫代)三磷酸（GTP[S]）引发了磷脂酶A2（PLA2）浓度依赖性的激活，而在添加钙离子（Ca2+）的情况下这种激活转变为抑制作用。GTP结合蛋白抑制剂鸟苷-5'-O-(2-硫代)二磷酸（GDP[S]）阻断了GTP[S]的刺激和抑制作用。我们得出结论，在酶原颗粒膜中，GTP结合蛋白对PLA2活性发挥双重调节作用。
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