SELECTIVE EXPRESSION OF VASOACTIVE-INTESTINAL-PEPTIDE (VIP)(2) PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE (PACAP)(3) RECEPTORS IN RABBIT AND GUINEA-PIG GASTRIC AND TENIA COLI SMOOTH-MUSCLE CELLS/
Bq. Teng et al., SELECTIVE EXPRESSION OF VASOACTIVE-INTESTINAL-PEPTIDE (VIP)(2) PITUITARY ADENYLATE CYCLASE-ACTIVATING POLYPEPTIDE (PACAP)(3) RECEPTORS IN RABBIT AND GUINEA-PIG GASTRIC AND TENIA COLI SMOOTH-MUSCLE CELLS/, Regulatory peptides, 77(1-3), 1998, pp. 127-134
In both functional and radioligand binding studies of gastric smooth m
uscle from rabbit and guinea pig, vasoactive intestinal peptide (VIP)
and pituitary adenylate cyclase-activating polypeptide (PACAP) show eq
ual potency indicating that the receptor type is either a VIP1 /PACAP(
2) or a VIP2/PACAP(3) receptor. We have characterized the VIP/PACAP re
ceptor expressed in freshly dispersed and cultured gastric and tenia c
oli smooth muscle cells of rabbit and guinea pig by reverse transcript
ase-polymerase chain reaction (RT-PCR), Northern analysis, and cloning
of the first extracellular domain. Specific primers based on cDNA seq
uences for rat VIP1/PACAP(2), VIP2/PACAP(3) and PACAP(1) receptors wer
e designed spanning the first extracellular domain. A 275 base pair pr
oduct corresponding to VIP2/PACAP(3) receptor was amplified by RT-PCR
in muscle cells from both species. No RT-PCR product was obtained with
primers for VIP2/PACAP(3) and PACAP(1) receptors. The deduced amino a
cid sequences showed 90% similarity in rabbit and 77% in guinea pig to
the sequence in rat. The location of the aspartate, tryptophan and gl
ycine residues and all six N-terminal cysteines required for VIP bindi
ng were conserved. The sequence in guinea pig tenia coli differed from
that in guinea pig stomach by two amino acid residues, Phe(40) and Ph
e(41). Northern analysis revealed a single 3.9 kilobase (kb) mRNA corr
esponding to VIP2/PACAP(3) receptors in rabbit and a 2.1 kb mRNA in gu
ineapig gastric and tenia coli muscle cells. We conclude that only VIP
2/PACAP(3) receptors are expressed in smooth muscle cells of rabbit an
d guinea pig. The two amino acid difference in the sequence obtained f
rom guinea pig tenia coli may reflect the distinct binding and functio
nal properties of this tissue. (C) 1998 Elsevier Science B.V All right
s reserved.