PHOSPHOINOSITIDE HYDROLYSIS BY PHOSPHOLIPASE-C MODULATED BY MULTIVALENT CATIONS LA3+, AL3+, NEOMYCIN, POLYAMINES, AND MELITTIN

被引：36

作者：

MCDONALD, LJ

MAMRACK, MD

机构：

[1] WRIGHT STATE UNIV,DEPT BIOL SCI,DAYTON,OH 45435

[2] WRIGHT STATE UNIV,PROGRAM BIOMED SCI,DAYTON,OH 45435

来源：

JOURNAL OF LIPID MEDIATORS AND CELL SIGNALLING | 1995年 / 11卷 / 01期

关键词：

PHOSPHOLIPASE C; PHOSPHOINOSITIDES; ALUMINUM; LANTHANUM; MELITTIN; NEOMYCIN; POLYAMINES;

D O I：

10.1016/0929-7855(94)00029-C

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：

Second messenger production from phosphoinositide hydrolysis is regulated by different pathways, such as G-proteins or tyrosine phosphorylation of phosphoinositide phospholipase C (PI-PLC). Another means of altering the activity of PI-PLC is through cation interaction with the phosphoinositide substrate. A variety of organic and inorganic multi-valent cations were examined for their effects on the activity of purified PI-PLC delta. Surprisingly, the cations produced both stimulation and inhibition of PI-PLC catalyzed phosphoinositide hydrolysis, depending on the substrate and the ion to phosphoinositide stoichiometry. These data support the hypothesis that ionic complexes with phosphoinositides may alter their hydrolysis by PI-PLC.

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页码：81 / 91

页数：11

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