Bkc. Chow, THE GOLDFISH VASOACTIVE INTESTINAL POLYPEPTIDE RECEPTOR - FUNCTIONAL-STUDIES AND TISSUE DISTRIBUTION, Fish physiology and biochemistry, 17(1-6), 1997, pp. 213-222
Vasoactive intestinal polypeptide (VIP)(1) is a neuropeptide that has
numerous physiological actions and is widely distibuted in the body of
most vertebrate species yet studied. A full-length VIP receptor cDNA
was obtained by screening a goldfish brain and pituitary cDNA library.
Functional expression of this receptor in mammalian COS-7 cells showe
d that it is coupled to cAMP production in a VIP (Atlantic cod, Gadus
morhua) concentration-dependent manner; the EC50 of the VIP receptor i
n response to cod VIP stimulation was determined to be at 1.0 nM. At 1
00 nM of peptide, the relative potency of various peptides in stimulat
ing cAMP in the transfected cells was cod VIP>human VIP>human PACAP-38
>human PACAP-27>human secretin>dogfish glucagon>carp GHRH. The recepto
r was able to bind specifically to VIP and PACAP as indicated by compe
titive displacement assays. By reverse-transcriptase polymerase chain
reaction, the transcripts of this receptor were detected in goldfish b
rain, pituitary gland, gall bladder, kidney, gill, small and large int
estine, heart, muscle and spleen. The expression pattern of goldfish V
IP receptor is similar to that of mammals and thus further evidence of
the conservation of VIP function in vertebrates. Characterization of
the VIP1 receptor from goldfish is the first step in understanding 2 o
f the most important neuropeptides, VIP and PACAP, and their interacti
on with multiple receptor system in lower vertebrates.