&lt;b&gt;GLP-1(&lt;i&gt;7—36&lt;/i&gt;)AMIDE: CHARACTERIZATION OF ITS BINDING TO SPECIFIC RECEPTORS IN NORMAL AND TUIVIORAL RAT ISLET CELLS &lt;/b&gt;

Valverde, Isabel; García, S. Ovejero; Ruiz-Grande, Carmen; Furundarena, Eunate; Trapote, M. A.; Villanueva-Peñacarrillo, María Luisa

doi:10.2220/biomedres.12.263

Cited by 4 publications

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“…[125I]GLP-l(7-36)amide binding (Göke & Conlon 1988), or not to compete at all in a pancreatic B-cell line (Valverde et al 1991) and, also, not to be insulinotropic at the lower doses at which the short GLP-1 forms exert this effect (Orskov et al 1986, Kawai et al 1989). …”

Section: Discussionmentioning

confidence: 99%

Glucagon-like peptide-1 binding to rat hepatic membranes

Villanueva-Peñacarrillo¹,

Delgado²,

Trapote³

et al. 1995

Journal of Endocrinology

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We have found [125I]glucagon-like peptide (GLP)-1(7-36)amide specific binding activity in rat liver and isolated hepatocyte plasma membranes, with an M(r) of approximately 63,000, estimated by cross-linking and SDS-PAGE. The specific binding was time- and membrane protein concentration-dependent, and equally displaced by unlabelled GLP-1(7-36)amide and by GLP-1(1-36)amide, achieving its ID50 at 3 x 10(-9) M of the peptides. GLP-1(7-36)amide did not modify the basal or the glucagon (10(-8) M)-stimulated adenylate cyclase in the hepatocyte plasma membranes. These data, together with our previous findings of a potent glycogenic effect of GLP-1(7-36)amide in isolated rat hepatocytes, led us to postulate that the insulin-like effects of this peptide on glucose liver metabolism could be mediated by a type of receptor probably different from that described for GLP-1 in pancreatic B-cells or, alternatively, by the same receptor which, in this tissue as well as in muscle, uses a different transduction system.

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Section: Discussionmentioning

confidence: 99%

Glucagon-like peptide-1 binding to rat hepatic membranes

Villanueva-Peñacarrillo¹,

Delgado²,

Trapote³

et al. 1995

Journal of Endocrinology

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Inositolphosphoglycans possibly mediate the effects of glucagon-like peptide-1(7-36)amide on rat liver and adipose tissue

Márquez

Trapote

Luque

et al. 1998

Cell Biochem. Funct.

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Insulin-like effects of glucagon-like peptide-1(7-36)amide (GLP-1) in rat liver, skeletal muscle and fat, and also the presence of GLP-1 receptors in these extrapancreatic tissues, have been documented. In skeletal muscle and liver, the action of GLP-1 is not associated with an activation of adenylate cyclase, and in cultured murine myocytes and hepatoma cell lines, it was found that GLP-1 provokes the generation of inositolphosphoglycan molecules (IPGs), which are considered second messengers of insulin action. In the present work, we document in isolated normal rat adipocytes and hepatocytes that GLP-1 exerts a rapid decrease of the radiolabelled glycosylphosphatidylinositols (GPIs)--precursors of IPGs--in the same manner as insulin, indicating their hydrolysis and the immediate short-lived generation of IPGs. Thus, IPGs could be mediators in the GLP-1 actions in adipose tissue and liver, as well as in skeletal muscle, through GLP-1 receptors which are, at least functionally, different from that of the pancreatic B-cell.

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