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   <subfield code="a">Effects of the C-terminal Peptide of the αs subunit of the G protein on the regulation of Adenylyl Cyclase and Protein Kinase A activities by Biogenic Amines and Glucagon in Mollusk and Rat Muscles</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[A. Shpakov, V. Korol'kov, S. Plesneva, L. Kuznetsova, M. Pertseva]</subfield>
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   <subfield code="a">The C-terminal parts of the α subunits of heteromeric G proteins play an important role in the functional linkage of G proteins with receptors of the serpentine type. The present report describes studies of the effects of the C-terminal octapeptide 387-394 of the αs subunit of the mammalian G protein on the transmission of the hormonal signal via the hormone-sensitive adenylyl cyclase signal system, whose major components are receptors of the serpentine type, G proteins, and the enzymes adenylyl cyclase and protein kinase A. The peptide synthesized here, 387-394 amide (10-7 - 10-4 M), dose-dependently decreased adenylyl cyclase and protein kinase A activities stimulated by serotonin and glucagon in smooth muscle from the freshwater bivalve mollusk Anodonta cygnea and by the β agonist isoproterenol in rat skeletal muscle. At a concentration as low as 10-7 M, the peptide released potentiation of the stimulatory effects of hormones on adenylyl cyclase activity due to the non-hydrolyzable guanine nucleotide analog Gpp[NH]p. At the same time, it had almost no effect on the stimulation of adenylyl cyclase activity by non-hormonal agents (NaF, Gpp[NH]p, and forskolin). The inhibitory effects of hormones on adenylyl cyclase and protein kinase A activities persisted in the presence of the peptide. Our data demonstrate the importance of the C-terminal part of the αs subunit of the stimulatory G protein for its functional linkage with receptors of the serpentine type and throw light on the molecular mechanisms of the interactions between G proteins and receptors.</subfield>
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