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Functional characterization of the putative orphan neuropeptide G-protein coupled receptor C26F1.6 in Caenorhabditis elegans

被引：37
作者：
Mertens, I
Vandingenen, A
Meeusen, T
Janssen, T
Luyten, W
Nachman, RJ
De Loof, A
Schoofs, L
机构：
[1] Catholic Univ Louvain, Lab Dev Physiol Genomics & Prote, B-3000 Louvain, Belgium
[2] IriDM, B-3000 Louvain, Belgium
[3] USDA ARS, So Plains Agr Res Ctr, College Stn, TX 77845 USA
来源：
FEBS LETTERS | 2004年 / 573卷 / 1-3期
关键词：
Caenorhabditis elegans; VRF-amide receptor 1; reverse pharmacology; FMRFamide related peptide;
D O I：
10.1016/j.febslet.2004.07.058
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：
In this study, we describe the cloning and the characterization of the third FMRFamide-related peptide (FaRP) receptor in Caenorhabditis elegans, the VRFa receptor 1. Numerous structurally different FaRPs were synthesized and used to screen the orphan C26F1.6 receptor for activation. Two peptides ending in M(orL)VRFamide elicited a calcium response in receptor expressing mammalian cells. The response is dose-dependent and appeared to be very specific, since very closely related FaRPs were less active, even the other peptides ending in M(orL)VRFamide. Pharmacological profiling of the most active peptide suggests that SMVRFa is the most active binding core. N-terminal extension decreases peptide activity. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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页码：55 / 60
页数：6
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