Gastric inhibitory polypeptide

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Gastric inhibitory polypeptide
Identifiers
Symbol GIP
Entrez 2695
HUGO 4270
OMIM 137240
RefSeq NM_004123
UniProt P09681
Other data
Locus Chr. 17 q21.3-q22

Gastric inhibitory polypeptide (GIP), also known as the glucose-dependent insulinotropic peptide is a member of the secretin family of hormones.[1]

GIP, along with glucagon-like peptide-1 (GLP-1), belongs to a class of molecules referred to as incretins.[2]

Synthesis and transport

GIP is derived from a 153-amino acid proprotein encoded by the GIP gene and circulates as a biologically active 42-amino acid peptide. It is synthesized by K cells, which are found in the mucosa of the duodenum and the jejunum of the gastrointestinal tract.

Like all endocrine hormones, it is transported by blood.

Gastric inhibitory polypeptide receptors are seven-transmembrane proteins found on beta-cells in the pancreas.

Functions

It has traditionally been named gastrointestinal inhibitory peptide or gastric inhibitory peptide and was found to decrease the secretion of stomach acid[3] to protect the small intestine from acid damage, reduce the rate at which food is transferred through the stomach, and inhibit the GI motility and secretion of acid. However, this is incorrect, as it was discovered that these effects are achieved only with higher-than-normal physiological level, and that these results naturally occur in the body through a similar hormone, secretin.

It is now believed that the function of GIP is to induce insulin secretion, which is stimulated primarily by hyperosmolarity of glucose in the duodenum.[4] After this discovery, some researchers prefer the new name of glucose-dependent insulinotropic peptide, while retaining the acronym "GIP." The amount of insulin secreted is greater when glucose is administered orally than intravenously.[5]

GIP is also thought to have significant effects on fatty acid metabolism through stimulation of lipoprotein lipase activity in adipocytes. GIP release has been demonstrated in the ruminant animal and may play a role in nutrient partitioning in milk production (lipid metabolism). GIP is secreted in response to the first maternal feed (colostrum) in goat kids—GIP being measured via umbilical vein before its closure. For ethical reasons, GIP secretion has been demonstrated in humans only at approx 10 days of age. With respect to the role of GIP in lipid metabolism, supraphysiological levels have shown a lipogenic action, however the action of collagenase in experimental protocols is known to degrade GIP/ GIP receptors. GIP is part of the diffuse endocrine system and, as a consequence, difficult to demonstrate physiological or clinical effects. In comparison to insulin its effects are very subtle.

GIP recently appeared as a major player in bone remodelling. Researchers at Universities of Angers and Ulster evidenced that genetic ablation of the GIP receptor in mice resulted in profound alterations of bone microarchitecture through modification of the adipokine network.[6] Furthermore, the deficiency in GIP receptors has also been associated in mice with a dramatic decrease in bone quality and a subsequent increase in fracture risk.[7]

Pathology

It has been found that Type 2 diabetics are not responsive to GIP and have lower levels of GIP secretion after a meal when compared to non-diabetics.[8] In research involving knockout mice, it was found that absence of the GIP receptors correlates with resistance to obesity.[9]

References

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External links