Tahiri-Jouti N, Dufresne M, Viguerie N, Fourmy D, Estève J P, Rivier J, Moroder L, Susini C, Vaysse N
Inserm U151, CHU Rangueil, Toulouse, France.
Neuropeptides. 1991 Jun;19(2):65-71. doi: 10.1016/0143-4179(91)90134-5.
The ability of somatostatin analogs to interact with the binding of cholecystokinin has been studied in pancreatic and brain cortical membranes. Only the 28 amino-acid forms of somatostatin (S28), [Nle8]S28 and [Des Lys14,DTrp22]S28 were found to inhibit the binding of cholecystokinin to rat pancreatic plasma membranes and to increase the amylase release from pancreatic acini. This effect was independent of somatostatin receptor and resulted from an interaction between S28 and CCK receptor. This interaction was not observed with [Leu8, DTrp22, Tyr25]S28, indicating that this analog does not possess the biological activity of the native peptide and that the iodinated peptide could not label specific S28 receptors. S28 interacted also with CCK receptors in cortical brain membranes. Our results support the concept that S28, but not S14, may function as a regulatory molecule at CCK receptors and emphasize that S28 and S14 may be distinct neuromodulators.
已在胰腺和脑皮质膜中研究了生长抑素类似物与胆囊收缩素结合相互作用的能力。仅发现28个氨基酸形式的生长抑素（S28）、[Nle8]S28和[去赖氨酸14，D-色氨酸22]S28可抑制胆囊收缩素与大鼠胰腺质膜的结合，并增加胰腺腺泡淀粉酶的释放。这种作用与生长抑素受体无关，而是由S28与CCK受体之间的相互作用引起的。未观察到[亮氨酸8，D-色氨酸22，酪氨酸25]S28有这种相互作用，这表明该类似物不具有天然肽的生物活性，且碘化肽不能标记特定的S28受体。S28也与脑皮质膜中的CCK受体相互作用。我们的结果支持S28而非S14可能作为CCK受体的调节分子发挥作用这一概念，并强调S28和S14可能是不同的神经调节剂。
