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Vol. 284, Issue 2, 744-750, February 1998
Unité de Neuroendocrinologie et Biologie Cellulaire
Digestives, Institut National de la Santé et de la Recherche
Médicale, INSERM U410, Faculté de Médecine Xavier
Bichat, 75018 Paris, France
Vasoactive intestinal peptide (VIP1 and VIP2) receptors belong to the
new class II subfamily of G protein-coupled receptors. We investigated
here human VIP1 and VIP2 receptors by mutating in their extracellular
domains all amino acid residues that are conserved in VIP receptors but
are different in other members of their subfamily. They are present in
1) the N-terminal domain, i.e., E36, I43, S64, D132 and F138
in the VIP1 receptor and E24, I31, S53, D116 and F122 in the VIP2
receptor; 2) the second extracellular loop, i.e., T288 and
S292 in the VIP1 receptor and T274 and S278 in the VIP2 receptor. These
residues were changed to alanine (A), and cDNAs were transfected into
Cos cells. For the VIP1 receptor, no specific 125I-VIP
binding could be detected in cells transfected with the E36A mutant,
whereas other mutants exhibited Kd values
similar to that of the wild-type receptor, with the exception of S64A, for which a 3-fold increase of Kd was observed.
For the VIP2 receptor, no specific 125I-VIP binding could
be observed with the E24A mutant, whereas other mutants exhibited
dissociation constants similar to that of the wild-type receptor, with
the exception of I31A and T274A mutants, for which a 11- and 5-fold
increase of Kd was observed, respectively. cAMP
production experiments provided evidence that the E36A VIP1 receptor
and the E24A VIP2 receptor mutants mediated almost no response upon VIP
exposure. For the I31A and T274A mutants of the VIP2 receptor and the
S64A mutant of the VIP1 receptor, the EC50 values of VIP
for stimulating cAMP production were increased 35, 8 and 3 times as
compared with that observed for the wild-type receptor, respectively.
Immunofluorescence studies indicated that all mutants were normally
expressed by Cos cells. These data provide the first evidence for
differences in the structure-function relationship of VIP1 and VIP2
receptors.
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