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Functional characterization of the putative orphan neuropeptide G‐protein coupled receptor C26F1.6 in Caenorhabditis elegans
Author(s) -
Mertens Inge,
Vandingenen Anick,
Meeusen Tom,
Janssen Tom,
Luyten Walter,
Nachman Ronald J.,
De Loof Arnold,
Schoofs Liliane
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.058
Subject(s) - caenorhabditis elegans , peptide , biology , receptor , neuropeptide , orphan receptor , biochemistry , microbiology and biotechnology , chemistry , gene , transcription factor
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.