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G Proteins Coupled to Phospholipase C: Molecular Targets of Long‐Term Ethanol Exposure
Author(s) -
Simonsson Per,
Rodriguez F. David,
Loman Niklas,
Alling Christer
Publication year - 1991
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1991.tb03461.x
Subject(s) - phospholipase c , bradykinin , gtp' , g protein , chemistry , phosphatidylinositol , biochemistry , pertussis toxin , guanosine , inositol , inositol trisphosphate , phosphoinositide phospholipase c , bradykinin receptor , phospholipase , ethanol , inositol phosphate , signal transduction , receptor , enzyme
Long‐term ethanol exposure is known to inhibit bradykinin‐stimulated phosphoinositide hydrolysis in cultures of neuroblastoma × glioma 108–15 cells. In the present study, [ 3 H]bradykinin binding, GTP‐binding protein function, and phospholipase C activity were assayed in cells grown for 4 days in 100 m M ethanol with the aim of elucidating the molecular target of ethanol on signal transduction coupled to inositol trisphosphate and diacylglycerol formation. Ethanol exposure reduced guanosine 5′‐ O ‐(3‐thiotriphosphate) [GTP(S)]‐ and, to a lesser extent, NaF/AlCl 3 ‐stimulated phosphoinositide hydrolysis, whereas it had no effect on the enzymatic activity of a phosphatidylinositol 4,5‐bisphosphate‐specific phospholipase C. [ 3 H]Bradykinin binding in the absence of GTP(S) was not influenced by ethanol exposure. However, the reduction in [ 3 H]bradykinin binding seen in control cells after addition of GTP analogue was inhibited in cells grown in ethanol‐containing medium. The results indicate that long‐term ethanol exposure exerts its effects on receptor‐stimulated phosphoinositide hydrolysis primarily at the level of the GTP‐binding protein.