TY - JOUR
T1 - Activation of the inhibitory GTP-binding protein of adenylate cyclase, G(i), by β-adrenergic receptors in reconstituted phospholipid vesicles
AU - Asano, T.
AU - Katada, T.
AU - Gilman, A. G.
AU - Ross, E. M.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1984
Y1 - 1984
N2 - β-Adrenergic receptors and the inhibitory GTP-binding protein, G(i) of the adenylate cyclase system were reconstituted into phospholipid vesicles by the method described previously for reconstituting receptors and the stimulatory GTP-binding protein G(s) (Brandt, D.R., Asano, T., Pedersen, S.E., and Ross, E.M. (1983) Biochemistry 22, 4357-4362). In the receptor-G(i) vesicles, β-adrenergic agonists stimulated both the high-affinity binding of guanosine 5'-O-(3-thiotriphosphate) (GTPγS) to G(i) and GTPase activity to an extent similar to that observed in vesicles containing β-adrenergic receptors and G(s). Stimulation required receptors and displayed appropriate β-adrenergic specificity. The prior treatment of receptor-G(i) vesicles with islet-activating protein (pertussis toxin) plus NAD markedly inhibited both the isoproterenol-stimulated binding of GTPγS and the isoproterenol-stimulated GTPase activity. No contamination of G(i) by G(s) was apparent. These data suggest that receptors that typically stimulate adenylate cyclase activity may also activate the inhibitory system, perhaps as one mechanism of desensitization.
AB - β-Adrenergic receptors and the inhibitory GTP-binding protein, G(i) of the adenylate cyclase system were reconstituted into phospholipid vesicles by the method described previously for reconstituting receptors and the stimulatory GTP-binding protein G(s) (Brandt, D.R., Asano, T., Pedersen, S.E., and Ross, E.M. (1983) Biochemistry 22, 4357-4362). In the receptor-G(i) vesicles, β-adrenergic agonists stimulated both the high-affinity binding of guanosine 5'-O-(3-thiotriphosphate) (GTPγS) to G(i) and GTPase activity to an extent similar to that observed in vesicles containing β-adrenergic receptors and G(s). Stimulation required receptors and displayed appropriate β-adrenergic specificity. The prior treatment of receptor-G(i) vesicles with islet-activating protein (pertussis toxin) plus NAD markedly inhibited both the isoproterenol-stimulated binding of GTPγS and the isoproterenol-stimulated GTPase activity. No contamination of G(i) by G(s) was apparent. These data suggest that receptors that typically stimulate adenylate cyclase activity may also activate the inhibitory system, perhaps as one mechanism of desensitization.
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M3 - Article
C2 - 6146612
AN - SCOPUS:0021194782
SN - 0021-9258
VL - 259
SP - 9351
EP - 9354
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 15
ER -