DIRECT INTERACTIONS OF MASTOPARAN AND COMPOUND 48/80 WITH GTP-BINDING PROTEINS

被引:54
作者
TOMITA, U
INANOBE, A
KOBAYASHI, I
TAKAHASHI, K
UI, M
KATADA, T
机构
[1] TOKYO INST TECHNOL,DEPT LIFE SCI,4259 NAGATSUTA,MIDORI KU,YOKOHAMA,KANAGAWA 227,JAPAN
[2] UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,BUNKYO KU,TOKYO 113,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123342
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
The effects of mastoparan and compound 48/80 on the activities of alpha-beta-gamma-trimeric GTP-binding proteins (G proteins) were studied with purified G(o) and G(i-1) which had been reconstituted into phospholipid vesicles. Pertussis toxin-catalyzed ADP-ribosylation of G(0) or G(i-1) was inhibited by mastoparan or compound 48/80, suggesting that the G proteins were dissociated into their constituent-alpha- and beta-gamma-subunits in the presence of these compounds. The steady-state rate of GTP hydrolysis catalyzed by G(0) or G(i-1) was stimulated by the two compounds. Both the stimulations were due to increases in the rate of the GDP-GTP exchange reaction occurring on the G proteins. However, the modes stimulation of the GTPase activity depended on the type of G protein used, and the stimulations caused by the two compounds were differently affected by pertussis toxin-catalyzed ADP-ribosylation of G proteins. Moreover, the mastoparan-induced stimulation of the GTPase activity was partially inhibited by compound 48/80. Thus, the two histamine secretagogues mastoparan and compound 48/80 appear to activate G proteins differently, though they interact with the signal-transducing proteins, at least partly, at a common binding site.
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页码:184 / 189
页数:6
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