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胃抑制多肽(GIP)受体结合及刺激胰岛素释放的结构要求。

Structural requirements for gastric inhibitory polypeptide (GIP) receptor binding and stimulation of insulin release.

作者信息

Maletti M, Carlquist M, Portha B, Kergoat M, Mutt V, Rosselin G

出版信息

Peptides. 1986;7 Suppl 1:75-8. doi: 10.1016/0196-9781(86)90167-1.

DOI:10.1016/0196-9781(86)90167-1
PMID:3018705
Abstract

The effect of bovine GIP 1-42 and several of its fragments in competing with the binding of 125I-GIP to beta-cell plasma membranes from transplantable hamster insulinoma, and in stimulating insulin release from the isolated perfused rat pancreas, was investigated. Our results, in association with the results of previous studies, indicate that the sequence 17-38 is necessary for receptor binding and biological activity of GIP. By contrast, the N-terminal portion of GIP can be removed without seriously impairing the activity of the molecule.

摘要

研究了牛GIP 1-42及其几个片段与125I-GIP竞争性结合可移植仓鼠胰岛素瘤β细胞膜以及刺激离体灌注大鼠胰腺释放胰岛素的作用。我们的结果与先前研究结果表明,17-38序列对于GIP的受体结合和生物活性是必需的。相比之下,GIP的N端部分可以去除而不会严重损害该分子的活性。

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Structural requirements for gastric inhibitory polypeptide (GIP) receptor binding and stimulation of insulin release.胃抑制多肽(GIP)受体结合及刺激胰岛素释放的结构要求。
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N-terminally and C-terminally truncated forms of glucose-dependent insulinotropic polypeptide are high-affinity competitive antagonists of the human GIP receptor.葡萄糖依赖性促胰岛素多肽的N端和C端截短形式是人GIP受体的高亲和力竞争性拮抗剂。
Br J Pharmacol. 2016 Mar;173(5):826-38. doi: 10.1111/bph.13384. Epub 2016 Jan 30.