In L cells of the intestine the transcription factors TCF-4 (TCF7L2) and Beta-catenin form a heterodimer and bind the G2 enhancer of the Proglucagon gene GCG,activating its transcription to yield Proglucagon mRNA and, following translation, Proglucagon protein. The prohormone convertase PC1 present in the secretory granules of L cells cleaves Proglucagon at two sites to yield mostly Glucagon-like Peptide-1 (7-36) with a small amount of Glucagon-like Peptide-1 (7-37). Glucagon-like Peptide-1 (7-36 and 7-37) (GLP-1) is secreted into the bloodstream in response to glucose, fatty acids, insulin, leptin, gastrin-releasing peptide, cholinergic transmitters, beta-adrenergic transmitters, and peptidergic transmitters. The half-life of GLP-1 in the bloodstream is determined by Dipeptidyl Peptidase IV, which cleaves 2 amino acids at the amino terminus of GLP-1, rendering it biologically inactive.
Holst, JJ
Kim, W, Egan, JM
Todd, JF, Bloom, SR
Gremlich, S, Macé, K, Darimont, C, Nicolas-Métral, V, Rüegg, UT, Reimer, RA
Drucker, DJ, Baggio, LL
Göke, R, Göke, B, Harthus, HP, Eissele, R, Arnold, R, Willemer, S, Vermeer, H
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