INTERACTIONS BETWEEN NPY AND ITS RECEPTOR - ASSESSMENT USING ANTI-NPY ANTIBODIES

被引：14

作者：

GROUZMANN, E

CRESSIER, F

WALKER, P

HOFBAUER, K

WAEBER, B

BRUNNER, HR

机构：

[1] UNIV LAUSANNE HOSP,CARDIOVASC RES GRP,CH-1011 LAUSANNE,SWITZERLAND

[2] CIBA GEIGY LTD,BASEL,SWITZERLAND

来源：

REGULATORY PEPTIDES | 1994年 / 54卷 / 2-3期

关键词：

NEUROPEPTIDE Y; Y1; RECEPTOR; ANTI-NPY ANTIBODY;

D O I：

10.1016/0167-0115(94)90541-X

中图分类号：

R5 [内科学];

学科分类号：

1002 ; 100201 ;

摘要：

The present data show that monoclonal antibodies (NPY02, NPY03, NPY04, NPY05) directed against 4 distinct epitopes on NPY may have different actions on NPY binding and NPY induced cellular responses. NPY02 and NPY05 recognize the 11-24 and 32-36 amidated form of NPY, respectively. These 2 antibodies block the binding of NPY to its receptor as well as the NPY-induced inhibition of cAMP accumulation caused in SK-N-MC cells by forskolin. NPY02 and NPY05 have also an inhibitory action on NPY-induced contraction of rabbit femoral arteries. NPY03 and NPY04 are directed against the 27-34 and 1-12 part of NPY, respectively. NPY03 and NPY04 inhibit the binding of NPY only at very high concentrations and have a weak effect on cAMP response to NPY. NPY02 and NPY05 might provide useful tools to study the effect of NPY in cellular systems and organ preparations.

引用

页码：439 / 444

页数：6

共 14 条

[1] MOLECULAR-STRUCTURE OF MAMMALIAN NEUROPEPTIDE-Y - ANALYSIS BY MOLECULAR-CLONING AND COMPUTER-AIDED COMPARISON WITH CRYSTAL-STRUCTURE OF AVIAN HOMOLOG [J].