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GLP-1 stimulates pancreatic β cells to secrete insulin as an incretin hormone. GLP-1 also has additional actions, including suppression of glucagon secretion, inhibition of gastric motility, and promotion of satiety.
GLP-1 was first identified in the early 1980s, following the cloning of the proglucagon gene. The biological activity of GLP-1 was investigated initially by using the N-terminal extended forms of GLP-1(1–37 and 1–36 amide). However, these forms were devoid of biological activity. In the late 1980s, bioactive GLP-1 peptides were purified from gut extracts and were identified to be GLP1(7–37) and GLP-1(7–36)-amide. In the current literature, the unqualified designation of GLP-1 corresponds to the truncated peptides.
Glucagon-Like Peptide I (GLP1) is an incretin hormone, which functions as ligand for GLP1 receptors (GLP1R). These receptors are expressed in renal and cardiovascular system, such as smooth muscle and endothelial cells.
Glucagon Like Peptide-1 is a single, non-glycosylated, polypeptide chain containing 30 amino acids and having a molecular mass of 3297.7 Dalton.The GLP-1 is purified by proprietary chromatographic techniques.