A receptor for VIP-related peptides with an unusual selectivity profile on the melanoma cell line IGR37.
A receptor capable of recognizing VIP-related peptides with unusual functional characteristics and selectivity profile was characterized on human IGR37 melanoma cells. When using either [125I]VIP or [125I]N-AcPACAP27 as a tracer, PACAP38 had the highest affinity, while PACAP27, VIP, helodermin, GRF and the VIP fragment VIP10-28 showed the same low affinity. Moreover, this receptor did not recognize PHM, PHV, helospectin, secretin, GIP, glucagon and glucagon-like peptide-1(7-36). Surprisingly, none of the peptides significantly stimulated the cAMP production. By covalent crosslinking, the receptor was shown to have a M(r) = 60,500.
Fabre
C
C
Institut de Chimie Biologique, Université de Provence, Marseille, France.
Bellan
C
C
Marvaldi
J
J
Luis
J
J
D001667:Binding, Competitive; D000242:Cyclic AMP / Q000096:biosynthesis; D006801:Humans; D007457:Iodine Radioisotopes; D008545:Melanoma / Q000378:metabolism* / Q000648:ultrastructure*; D009479:Neuropeptides / Q000378:metabolism / Q000494:pharmacology; D018005:Receptors, Vasoactive Intestinal Peptide / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D014660:Vasoactive Intestinal Peptide / Q000378:metabolism / Q000494:pharmacology
D007457:Iodine Radioisotopes; C092889:N-acetyl-pituitary adenylate cyclase activity peptide 27; D009479:Neuropeptides; D018005:Receptors, Vasoactive Intestinal Peptide; D014660:Vasoactive Intestinal Peptide; D000242:Cyclic AMP