EFFECT OF MONOLAYER SURFACE PRESSURE ON THE ACTIVITIES OF PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE-C-BETA-1, PHOSPHOLIPASE-C-GAMMA-1, AND PHOSPHOLIPASE-C-DELTA-1

被引:132
作者
BOGUSLAVSKY, V
REBECCHI, M
MORRIS, AJ
JHON, DY
RHEE, SG
MCLAUGHLIN, S
机构
[1] SUNY STONY BROOK,HLTH SCI CTR,STONY BROOK,NY 11794
[2] NHLBI,BIOCHEM LAB,BETHESDA,MD 20892
关键词
D O I
10.1021/bi00176a036
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Three isoforms of phospholipase C, either PLC-beta(1), PLC-gamma(1), or PLC-delta(1), were added to the aqueous subphase beneath phospholipid monolayers formed at an air-solution interface, and the initial rate of hydrolysis of phosphatidylinositol 4,5-bisphosphate was measured after addition of 10 mu M free Ca2+. The monolayers were formed from mixtures of phosphatidylcholine (65% PC), phosphatidylserine (33% PS), and phosphatidylinositol 4,5-bisphosphate (2% PIP2). Increasing the surface pressure of the monolayer, pi, from 15 to 25 mN/m decreases the rate of hydrolysis 16-, 13-, and 5-fold for PLC-beta(1), PLC-gamma(1), and PLC-delta(1), respectively. The simplest interpretation of these results is that a portion of each of the enzymes of area A(p) must insert into the monolayer, doing work pi A(p), prior to hydrolysis of PIP2; binding studies with simple model compounds of known cross-sectional area are consistent with this interpretation. Removing the monovalent acidic lipid PS from the monolayer decreases the initial rates of hydrolysis of PIP2 about 3-fold for each PLC isoform, which suggests that negative electrostatic surface potentials increase the PLC activity.
引用
收藏
页码:3032 / 3037
页数:6
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