Molecular cloning and functional characterization ...[Biochem Biophys Res Commun. 1994]

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1: Biochem Biophys Res Commun. 1994 Dec 30;205(3):1617-24. Links

Molecular cloning and functional characterization of a human VIP receptor from SUP-T1 lymphoblasts.

Svoboda M, Tastenoy M, Van Rampelbergh J, Goossens JF, De Neef P, Waelbroeck M, Robberecht P.

Department of Biochemistry and Nutrition, Medical School, Université Libre de Bruxelles, Belgium.

We have cloned and sequenced a cDNA isolated from a human SUP-T1 lymphoblast cell line library. It encoded a 457 amino acids protein having 87% identity with the rat PACAP type II, VIP2 receptor. Chinese hamster ovary (CHO) cells stably transfected with cloned cDNA expressed a specific binding of 125I[Acetyl-His1]PACAP-27. This binding was inhibited by GTP, and by the peptides helodermin, VIP, PACAP-27 and PACAP-38 that also stimulated adenylate cyclase activity. The order of potency was PACAP-38 > VIP > or = helodermin > or = PACAP-27. Comparison of the results in two cell lines expressing different receptor densities suggested that helodermin and PACAP-38 had a higher intrinsic activity than VIP and PACAP-27.

PMID: 7811244 [PubMed - indexed for MEDLINE]

Analogues of VIP, helodermin, and PACAP discriminate between rat and human VIP1 and VIP2 receptors.
Ann N Y Acad Sci. 1998 Dec 11; 865:247-52.

[Ann N Y Acad Sci. 1998]
A cloned frog vasoactive intestinal polypeptide/pituitary adenylate cyclase-activating polypeptide receptor exhibits pharmacological and tissue distribution characteristics of both VPAC1 and VPAC2 receptors in mammals.
Endocrinology. 1999 Mar; 140(3):1285-93.

[Endocrinology. 1999]
Properties of the pituitary adenylate cyclase-activating polypeptide I and II receptors, vasoactive intestinal peptide1, and chimeric amino-terminal pituitary adenylate cyclase-activating polypeptide/vasoactive intestinal peptide1 receptors: evidence for multiple receptor states.
Mol Pharmacol. 1996 Dec; 50(6):1596-604.

[Mol Pharmacol. 1996]
ReviewPACAP/VIP receptors in pancreatic beta-cells: their roles in insulin secretion.
Ann N Y Acad Sci. 1996 Dec 26; 805:44-51; discussion 52-3.

[Ann N Y Acad Sci. 1996]
ReviewCharacterization of the VIP receptor from SUP T1 lymphoblasts.
Adv Neuroimmunol. 1996; 6(1):49-57.

[Adv Neuroimmunol. 1996]
» See reviews... | » See all...

Cited by 8 PubMed Central articles

Inhibition of intestinal dipeptide transport by the neuropeptide VIP is an anti-absorptive effect via the VPAC1 receptor in a human enterocyte-like cell line (Caco-2).
Anderson CM, Mendoza ME, Kennedy DJ, Raldua D, Thwaites DT. Br J Pharmacol. 2003 Feb; 138(4):564-73.

[Br J Pharmacol. 2003]
Evidence for a direct interaction between the Thr11 residue of vasoactive intestinal polypeptide and Tyr184 located in the first extracellular loop of the VPAC2 receptor.
Nachtergael I, Vertongen P, Langer I, Perret J, Robberecht P, Waelbroeck M. Biochem J. 2003 Mar 15; 370(Pt 3):1003-9.

[Biochem J. 2003]
Two tyrosine residues in the first transmembrane helix of the human vasoactive intestinal peptide receptors play a role in supporting the active conformation.
Perret J, Vertongen P, Solano RM, Langer I, Cnudde J, Robberecht P, Waelbroeck M. Br J Pharmacol. 2002 Aug; 136(7):1042-8.

[Br J Pharmacol. 2002]
» See all...

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