Glucagon-like peptide-1: difference between revisions
Diff·revision 12 → 13·00:10, 27 Oct 2024
Difference between revision 12 and revision 13 of Glucagon-like peptide-1. 3 lines changed; the page grew by 487 bytes.
| Revision 12 — 19:37, 13 Oct 2024 COA_Colwyn (talk) add the species in which the knockout work was done 7,399 bytes +178 | Revision 13 — 00:10, 27 Oct 2024 SatietySunniva (talk) add the postprandial time course with its units 7,886 bytes +487 | ||
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| 1 | {{Infobox concept | 1 | {{Infobox concept |
| 2 | | name = Glucagon-like peptide-1 | 2 | | name = Glucagon-like peptide-1 |
| + | 3 | | subtitle = Endogenous incretin hormone | |
| 3 | | image = peptide-chain.svg | 4 | | image = peptide-chain.svg |
| 4 | | caption = Schematic of the GLP-1 (7–36) amide backbone. Residue identities are indicative only. | 5 | | caption = Schematic of the GLP-1 (7–36) amide backbone. Residue identities are indicative only. |
| ⋮ | ⋮ | ||
| 48 | 49 | ||
| 49 | GLP-1 is cleaved between residues 8 and 9 by [[Dipeptidyl peptidase-4|dipeptidyl peptidase-4]], a widely expressed serine exopeptidase present both as a membrane protein on endothelium and as a soluble plasma form. The resulting GLP-1 (9–36) amide is at best weakly active at the [[GLP-1 receptor]] and has historically been regarded as an inactive metabolite, although a degree of independent cardiovascular activity has been proposed.{{r|deacon1995}} | 50 | GLP-1 is cleaved between residues 8 and 9 by [[Dipeptidyl peptidase-4|dipeptidyl peptidase-4]], a widely expressed serine exopeptidase present both as a membrane protein on endothelium and as a soluble plasma form. The resulting GLP-1 (9–36) amide is at best weakly active at the [[GLP-1 receptor]] and has historically been regarded as an inactive metabolite, although a degree of independent cardiovascular activity has been proposed.{{r|deacon1995}} |
| + | 51 | ||
| + | 52 | The consequence is a plasma half-life of approximately 1.5–2 minutes, and an estimated 50–75% of newly secreted GLP-1 is degraded before it leaves the intestinal capillary bed. Two therapeutic strategies follow directly from this: inhibit the enzyme, which is the mechanism of the gliptin class, or engineer the peptide so that it resists the enzyme, which is the mechanism of the [[GLP-1 receptor agonist|agonist class]].{{r|nauck2018}} | |
| 50 | 53 | ||
| 51 | == References == | 54 | == References == |