半胱胺选择性增强神经肽Y2受体结合活性。

Cysteamine selectively enhances neuropeptide Y2 receptor binding activity.

作者信息

Li W, Hexum T D

机构信息

Department of Pharmacology, University of Nebraska Medical Center, Omaha 68198-6260.

出版信息

Biochem Biophys Res Commun. 1992 Apr 15;184(1):380-6. doi: 10.1016/0006-291x(92)91204-4.

DOI:10.1016/0006-291x(92)91204-4

PMID:1314592

Abstract

Affinity labeling of [125I]NPY to the bovine hippocampal NPY receptor has revealed a 50 kDa specific binding protein, the Y2 receptor. Cysteamine (10 microM - 10 mM) specifically enhanced NPY specific labeling of the Y2 receptor without affecting cross-linking efficiency. Several structurally related agents, including reduced glutathione, cysteine, beta-mercaptoethanol and ethanolamine, were without effect on receptor binding. The enhancement of binding by cysteamine could be reversed by washing the membranes. These studies suggest that cysteamine may change the conformation of the NPY Y2 receptor and increase its binding activity.

摘要

[125I]神经肽Y（NPY）与牛海马NPY受体的亲和标记显示出一种50 kDa的特异性结合蛋白，即Y2受体。半胱胺（10微摩尔 - 10毫摩尔）特异性增强了Y2受体的NPY特异性标记，而不影响交联效率。几种结构相关的试剂，包括还原型谷胱甘肽、半胱氨酸、β-巯基乙醇和乙醇胺，对受体结合没有影响。通过洗涤膜可以逆转半胱胺对结合的增强作用。这些研究表明，半胱胺可能改变NPY Y2受体的构象并增加其结合活性。