Gastric inhibitory polypeptide receptor

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
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RefSeq (mRNA)

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RefSeq (protein)

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The gastric inhibitory polypeptide receptor (GIP-R), also known as the glucose-dependent insulinotropic polypeptide receptor, is a protein that in humans is encoded by the GIPR gene.[1][2] GIP-R is a member of the 7-transmembrane protein family, a class of G protein–coupled receptors.[3] GIP-R is found on beta-cells in the pancreas.[4][5]

Function

Gastric inhibitory polypeptide (GIP), also called glucose-dependent insulinotropic polypeptide, is a 42-amino acid polypeptide synthesized by K cells of the duodenum and small intestine. It was originally identified as an activity in gut extracts that inhibited gastric acid secretion and gastrin release, but subsequently was demonstrated to stimulate insulin release potently in the presence of elevated glucose. The insulinotropic effect on pancreatic islet beta-cells was then recognized to be the principal physiologic action of GIP. Together with glucagon-like peptide-1, GIP is largely responsible for the secretion of insulin after eating. It is involved in several other facets of the anabolic response.[1]

References

  1. 1.0 1.1 "Entrez Gene: gastric inhibitory polypeptide receptor".
  2. Stoffel M, Fernald AA, Le Beau MM, Bell GI (August 1995). "Assignment of the gastric inhibitory polypeptide receptor gene (GIPR) to chromosome bands 19q13.2-q13.3 by fluorescence in situ hybridization". Genomics. 28 (3): 607–609. doi:10.1006/geno.1995.1203. PMID 7490109.
  3. NCBI, NCBI Gene entry 2696 (GIPR), retrieved 2018-12-20.
  4. "Gastrointestinal Hormones and Peptides". Retrieved 2007-08-24.
  5. Brubaker PL, Drucker DJ (2002). "Structure-function of the glucagon receptor family of G protein-coupled receptors: the glucagon, GIP, GLP-1, and GLP-2 receptors". Recept. Channels. 8 (3–4): 179–188. doi:10.1080/10606820213687. PMID 12529935.

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.