Gastric inhibitory polypeptide receptor

Gastric inhibitory polypeptide receptor

Gastric inhibitory polypeptide receptor
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; PGQTL2
External IDs IUPHAR: ChEMBL: GeneCards:
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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] The GIP-R is seven-transmembrane proteins found on beta-cells in the pancreas.[3][4]


  • Function 1
  • References 2
  • Further reading 3
  • External links 4


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]


  1. ^ a b "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.  
  3. ^ "Gastrointestinal Hormones and Peptides". Retrieved 2007-08-24. 
  4. ^ 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.  

Further reading

  • Yamada Y, Seino Y (2005). "Physiology of GIP--a lesson from GIP receptor knockout mice". Horm. Metab. Res. 36 (11–12): 771–774.  
  • Gremlich S, Porret A, Hani EH, et al. (1995). "Cloning, functional expression, and chromosomal localization of the human pancreatic islet glucose-dependent insulinotropic polypeptide receptor". Diabetes 44 (10): 1202–1208.  
  • Volz A, Göke R, Lankat-Buttgereit B, et al. (1995). "Molecular cloning, functional expression, and signal transduction of the GIP-receptor cloned from a human insulinoma". FEBS Lett. 373 (1): 23–29.  
  • Usdin TB, Mezey E, Button DC, et al. (1994). "Gastric inhibitory polypeptide receptor, a member of the secretin-vasoactive intestinal peptide receptor family, is widely distributed in peripheral organs and the brain". Endocrinology 133 (6): 2861–2870.  
  • Yamada Y, Hayami T, Nakamura K, et al. (1996). "Human gastric inhibitory polypeptide receptor: cloning of the gene (GIPR) and cDNA". Genomics 29 (3): 773–776.  
  • Gallwitz B, Witt M, Morys-Wortmann C, et al. (1997). "GLP-1/GIP chimeric peptides define the structural requirements for specific ligand-receptor interaction of GLP-1". Regul. Pept. 63 (1): 17–22.  
  • N'Diaye N, Tremblay J, Hamet P, et al. (1998). "Adrenocortical overexpression of gastric inhibitory polypeptide receptor underlies food-dependent Cushing's syndrome". J. Clin. Endocrinol. Metab. 83 (8): 2781–2785.  
  • Tseng CC, Zhang XY (2000). "Role of G protein-coupled receptor kinases in glucose-dependent insulinotropic polypeptide receptor signaling". Endocrinology 141 (3): 947–952.  
  • Bollag RJ, Zhong Q, Phillips P, et al. (2000). "Osteoblast-derived cells express functional glucose-dependent insulinotropic peptide receptors". Endocrinology 141 (3): 1228–1235.  
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903.  
  • Baldacchino V, Oble S, Hamet P, et al. (2003). "Partial characterisation of the 5' flanking region of the human GIP receptor (GIPR) gene". Endocr. Res. 28 (4): 577–577.  
  • Antonini SR, N'Diaye N, Hamet P, et al. (2003). "Analysis of the putative promoter region of the GIP receptor gene (GIPR) in GIP-dependent Cushing's syndrome (CS)". Endocr. Res. 28 (4): 755–756.  
  • Manhart S, Hinke SA, McIntosh CH, et al. (2003). "Structure-function analysis of a series of novel GIP analogues containing different helical length linkers". Biochemistry 42 (10): 3081–3088.  
  • Ding KH, Zhong Q, Isales CM (2003). "Glucose-dependent insulinotropic peptide stimulates thymidine incorporation in endothelial cells: role of endothelin-1". Am. J. Physiol. Endocrinol. Metab. 285 (2): E390–6.  
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature 428 (6982): 529–535.  
  • Hansotia T, Baggio LL, Delmeire D, et al. (2004). "Double incretin receptor knockout (DIRKO) mice reveal an essential role for the enteroinsular axis in transducing the glucoregulatory actions of DPP-IV inhibitors". Diabetes 53 (5): 1326–1335.  
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127.  
  • Baldacchino V, Oble S, Hamet P, et al. (2005). "The Sp transcription factor family is involved in the cellular expression of the human GIP-R gene promoter". Endocr. Res. 30 (4): 805–806.  

External links

  • "Glucagon Receptor Family: GIP". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. 
  • gastric inhibitory polypeptide receptor at the US National Library of Medicine Medical Subject Headings (MeSH)

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