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Am J Physiol Cell Physiol 275: C675-C683, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 3, C675-C683, September 1998

GLP-1 action in L6 myotubes is via a receptor different from the pancreatic GLP-1 receptor

H. Yang1, J. M. Egan1, Y. Wang1, C. D. Moyes2, J. Roth3, M. H. Montrose3, and C. Montrose-Rafizadeh1

1 Laboratory of Clinical Physiology, Gerontology Research Center, National Institute on Aging, National Institutes of Health, Baltimore 21224; 3 Department of Medicine, Johns Hopkins University, Baltimore, Maryland 21205; and 2 Department of Biology, Queen's University, Kingston, Ontario, Canada K7L 3N6

The incretin hormone glucagon-like peptide-1 (GLP-1)-(7---36) amide is best known for its antidiabetogenic actions mediated via a GLP-1 receptor present on pancreatic endocrine cells. To investigate the molecular mechanisms of GLP-1 action in muscle, we used cultured L6 myotubes. In L6 myotubes, GLP-1 enhanced insulin-stimulated glycogen synthesis by 140% while stimulating CO2 production and lactate formation by 150%. In the presence of IBMX, GLP-1 diminished cAMP levels to 83% of IBMX alone. In L6 myotubes transfected with pancreatic GLP-1 receptor, GLP-1 increased cAMP levels and inhibited glycogen synthesis by 60%. An antagonist of pancreatic GLP-1 receptor, exendin-4-(9---39), inhibited GLP-1-mediated glycogen synthesis in GLP-1 receptor-transfected L6 myotubes. However, in parental L6 myotubes, exendin-4-(9---39) and GLP-1-(1---36) amide, an inactive peptide on pancreatic GLP-1 receptor, displaced 125I-labeled GLP-1 binding and stimulated glycogen synthesis by 186 and 130%, respectively. These results suggest that the insulinomimetic effects of GLP-1 in L6 cells are likely to be mediated by a receptor that is different from the GLP-1 receptor found in the pancreas.

glycolysis; glycogen synthesis; muscle; transfection; glucagon-like peptide


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