期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
卷 1546, 期 1, 页码 79-86出版社
ELSEVIER
DOI: 10.1016/S0167-4838(00)00270-3
关键词
G-protein; G-protein coupled receptor; GLP-1 glucagon like peptide-1; GLP-1 glucagon like peptide-1 receptor; pertussis toxin; cholera toxin; third intracellular loop; synthetic peptide; receptor domain; GTPase; GTP gamma S; cAMP
It has previously been shown that the GLP-1 receptor is primarily coupled to the adenylate cyclase pathway via activation of G alpha (s) proteins. Recent studies have shown that the third intracellular loop of the receptor is important in the stimulation of cAMP production. We have studied the effect of three synthetic peptide sequences derived from the third intracellular loop of the GLP-1 receptor on signal transduction in Rin m5F cell membranes. The whole third intracellular loop strongly stimulates both pertussis toxin and cholera toxin-sensitive G proteins, while the N-terminal half exclusively stimulates cholera toxin-sensitive G proteins and the C-terminal half only stimulates pertussis toxin-sensitive G-proteins as demonstrated by measurements of GTPase activity. These data confirm that the principal stimulatory G-protein interaction site resides in the third intracellular loop, but also suggest that the GLP-1 receptor is not only coupled to the G alpha (s) but also to the G alpha (i)/G alpha (o), type of G proteins and that distinct domains within the third intracellular loop are responsible for the activation of the different G-protein subfamilies. (C) 2001 Elsevier Science B.V. All rights reserved.
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