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Glucose-dependent insulinotropic polypeptide: difference between revisions

Diff·revision 6 → 7·11:21, 5 Jul 2024

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Revision 6 — 05:32, 4 Jul 2024
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Revision 7 — 11:21, 5 Jul 2024
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10GIP is processed post-translationally from pro-GIP and circulates in two forms: the active GIP (1–42) and an N-terminally cleaved GIP (3–42) produced by dipeptidyl peptidase-4 cleavage. Both forms retain insulin-secretory activity, which is unusual among incretin peptides and is the basis for the ''glucose-dependent'' descriptor — GIP potentiates insulin secretion only when glucose is elevated.{{r|deacon1995}}10GIP is processed post-translationally from pro-GIP and circulates in two forms: the active GIP (1–42) and an N-terminally cleaved GIP (3–42) produced by dipeptidyl peptidase-4 cleavage. Both forms retain insulin-secretory activity, which is unusual among incretin peptides and is the basis for the ''glucose-dependent'' descriptor — GIP potentiates insulin secretion only when glucose is elevated.{{r|deacon1995}}
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+12== Biosynthesis and secretion ==
+13GIP is encoded by the ''GIP'' gene and is processed from a 153-residue pro-GIP. Like GLP-1, it is subject to tissue-specific post-translational modification. In K cells, endopeptidases cleave pro-GIP to release the active hormone. The principal stimuli are glucose and long-chain fatty acids; amino acids are a weaker stimulus.{{r|nauck2019}}
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+15K cells are found predominantly in the duodenum and jejunum, extending into the ileum in smaller numbers. They are open-type epithelial cells with an apical surface exposed to the lumen, allowing direct contact with nutrient-induced secretagogues. Secretion is biphasic: an early phase within 15 minutes of ingestion, followed by a later more sustained phase as nutrients pass through the intestine.{{r|nauck2019}}
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12== References ==17== References ==
13{{reflist}}18{{reflist}}