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Once secreted, GLP-1 is extremely susceptible to the catalytic activity of the proteolytic enzyme [[dipeptidyl peptidase-4]] ([[DPP-4]]). Specifically, [[DPP-4]] cleaves the [[peptide bond]] between [[alanine|Ala]]<sup>8</sup>-[[glutamic acid|Glu]]<sup>9</sup> resulting in the abundant GLP-1 (9–36) amide constituting 60–80 % of total GLP-1 in circulation. [[DPP-4]] is widely expressed in multiple tissues and cell types and exists in both a membrane-anchored and soluble circulating form. Notably, [[DPP-4]] is expressed on the surface of [[endothelial cells]], including those located directly adjacent to GLP-1 secretion sites. Consequently, less than 25% of secreted GLP-1 is estimated to leave the gut intact. Additionally, presumably due to the high concentration of [[DPP-4]] found on [[hepatocytes]], 40–50% of the remaining active GLP-1 is degraded across the [[liver]]. Thus, due to the activity of [[DPP-4]] only 10–15 % of secreted GLP-1 reaches circulation intact.

Translations:Glucagon-like peptide-1/15/en - Revision history

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