[I-125]Leu(31), Pro(34)-PYY is a high affinity radioligand for rat PP1/Y4 and Y1 receptors: Evidence for heterogeneity in pancreatic polypeptide receptors

被引：56

作者：

Gehlert, DR ^{[1
]}

Schober, DA ^{[1
]}

Gackenheimer, SL ^{[1
]}

Beavers, L ^{[1
]}

Gadski, R ^{[1
]}

Lundell, I ^{[1
]}

Larhammar, D ^{[1
]}

机构：

[1] UPPSALA UNIV,DEPT MED PHARMACOL,S-75124 UPPSALA,SWEDEN

来源：

PEPTIDES | 1997年 / 18卷 / 03期

关键词：

I-125]Leu(31); Pro(34)-PYY; radioligand; peptides; neuropeptide Y; pancreatic polypeptide;

D O I：

10.1016/S0196-9781(96)00346-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Cloned receptors for the PP-fold peptides are subdivided into Y1, Y2, PP1/Y4, Y5 and Y6. NPY and PYY have similar affinity for Y1, Y2, Y5 and Y6 receptors while PP has highest affinity for PP1. Pro(34)-substituted analogs of NPY and PYY have selectivity for Y1 and Y1-like receptors over Y2 receptors. In the present study, we found the putative Y1-selective radioligand, [I-125]Leu(31), Pro(34)-PYY, also binds with high affinity to the rat PP1 receptor in cell lines expressing the receptor. However, in rat brain sections, [I-125]Leu(31), Pro(34)-PYY does not appear to bind to the interpeduncular nucleus, a brain region containing a high density of [I-125]-bPP binding sites. Therefore, it appears there is additional heterogeneity in receptors recognizing PP. (C) 1997 Elsevier Science Inc.

引用

页码：397 / 401

页数：5

共 18 条

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