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INHIBITION OF ADENYLYL-CYCLASE BY G(I-ALPHA)
Author(s): TAUSSIG R, INIGUEZLLUHI JA, GILMAN AG
Source: SCIENCE    Volume: 261    Issue: 5118    Pages: 218-221    Published: JUL 9 1993  
Times Cited: 244     References: 31     
Abstract: Evidence suggests that both alpha and betagamma subunits of heterotrimeric guanine nucleotide-binding regulatory proteins (G proteins) inhibit adenylyl cyclase. Although type I adenylyl cyclase is inhibited directly by exogenous betagamma, inhibition of adenylyl cyclase by G(ialpha) has not been convincingly demonstrated in vitro. Concentration-dependent inhibition of adenylyl cyclases by purified G(ialpha) subunits is described. Activated G(ialpha) but not G(oalpha) was effective, and myristoylation of G(ialpha) was required. The characteristics of the inhibitory effect were dependent on the type of adenylyl cyclase and the nature of the activator of the enzyme. The concentrations of G(ialpha) required to inhibit adenylyl cyclase were substantially higher than those normally thought to be relevant physiologically. However, analysis indicates that these concentrations may be relevant and reasonable.
Document Type: Article
Language: English
Reprint Address: TAUSSIG, R (reprint author), UNIV TEXAS, SW MED CTR, DEPT PHARMACOL, 5323 HARRY HINES BLVD, DALLAS, TX 75235 USA
Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005
Subject Category: Multidisciplinary Sciences
IDS Number: LL596
ISSN: 0036-8075
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