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.

Alexandre, D ; Anouar, Y ; et al.

In: Endocrinology, Jg. 140 (1999-03-01), Heft 3, S. 1285-93

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Three receptor subtypes for the neuropeptides vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) have been identified in mammals: the PAC1 receptor (PAC1-R) which is selectively activated by PACAP, and two VPAC receptors (VPAC1-R and VPAC2-R), which are equally stimulated by PACAP and VIP. The structures of PACAP and VIP have been well conserved during evolution, but little is known about VIP/PACAP receptors in nonmammalian species. An amphibian VIP/PACAP receptor complementary DNA (cDNA) has been cloned and characterized from a frog (Rana ridibunda) pituitary cDNA library. The predicted protein contains seven putative transmembrane domains and exhibits the highest sequence identity (65%) with the human VPAC1-R. The cloned cDNA was transiently expressed in LLC-PK1 cells, and its pharmacological profile was determined in comparison with the human VPAC1-R. Both PACAP and VIP stimulated cAMP accumulation through the cloned receptor with an EC50 of about 30 nM. In contrast, secretin, at concentrations that stimulate the human VPAC1-R, had no effect on cAMP production. RT-PCR analysis revealed the widespread distribution of this frog VIP/PACAP receptor in peripheral tissues. In situ hybridization histochemistry using a complementary RNA probe showed that the receptor gene is highly expressed in several hypothalamic and thalamic nuclei and to a lesser extent in the pallium and striatum. In the pituitary, the highest messenger RNA levels were detected in the distal lobe. Taken together, these data show that the cloned frog receptor shares several common features with both the VPAC1-R and VPAC2-R of mammals; the frog receptor exhibits the highest sequence identity with mammalian VPAC1-R, but the lack of effect of secretin and the brain distribution of the receptor are reminiscent of the characteristics of the mammalian VPAC2-R. The sequence of the frog receptor should thus prove useful to decipher the structure-activity relationships of the VIP/PACAP receptor family.

Titel:	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.
Autor/in / Beteiligte Person:	Alexandre, D ; Anouar, Y ; Jegou, S ; Fournier, A ; Vaudry, H
Link:	Zum Volltext
Zeitschrift:	Endocrinology, Jg. 140 (1999-03-01), Heft 3, S. 1285-93
Veröffentlichung:	2017- : New York : Oxford University Press ; <i>Original Publication</i>: Los Angeles, Calif. : Association for the Study of Internal Secretions,, 1999
Medientyp:	academicJournal
ISSN:	0013-7227 (print)
DOI:	10.1210/endo.140.3.6576
Schlagwort:	Adenylyl Cyclases drug effects Amino Acid Sequence Animals Brain Chemistry physiology Cloning, Molecular Humans Molecular Sequence Data Neuropeptides pharmacology Organ Specificity Pituitary Adenylate Cyclase-Activating Polypeptide Pituitary Gland chemistry Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I Receptors, Vasoactive Intestinal Peptide analysis Receptors, Vasoactive Intestinal Peptide, Type II Receptors, Vasoactive Intestinal Polypeptide, Type I Sequence Homology, Amino Acid Species Specificity Vasoactive Intestinal Peptide pharmacology Mammals physiology Rana ridibunda physiology Receptors, Pituitary Hormone genetics Receptors, Vasoactive Intestinal Peptide drug effects Receptors, Vasoactive Intestinal Peptide genetics
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [Endocrinology] 1999 Mar; Vol. 140 (3), pp. 1285-93. MeSH Terms: Mammals / physiology ; Rana ridibunda / physiology ; Receptors, Pituitary Hormone / genetics ; Receptors, Vasoactive Intestinal Peptide / drug effects ; Receptors, Vasoactive Intestinal Peptide / *genetics ; Adenylyl Cyclases / drug effects ; Amino Acid Sequence ; Animals ; Brain Chemistry / physiology ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; Neuropeptides / pharmacology ; Organ Specificity ; Pituitary Adenylate Cyclase-Activating Polypeptide ; Pituitary Gland / chemistry ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide ; Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I ; Receptors, Vasoactive Intestinal Peptide / analysis ; Receptors, Vasoactive Intestinal Peptide, Type II ; Receptors, Vasoactive Intestinal Polypeptide, Type I ; Sequence Homology, Amino Acid ; Species Specificity ; Vasoactive Intestinal Peptide / pharmacology Molecular Sequence: GENBANK AF100642; AF100643; AF100644 Substance Nomenclature: 0 (ADCYAP1 protein, human) ; 0 (ADCYAP1R1 protein, human) ; 0 (Neuropeptides) ; 0 (Pituitary Adenylate Cyclase-Activating Polypeptide) ; 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide) ; 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I) ; 0 (Receptors, Pituitary Hormone) ; 0 (Receptors, Vasoactive Intestinal Peptide) ; 0 (Receptors, Vasoactive Intestinal Peptide, Type II) ; 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I) ; 0 (VIPR1 protein, human) ; 0 (VIPR2 protein, human) ; 37221-79-7 (Vasoactive Intestinal Peptide) ; EC 4.6.1.1 (Adenylyl Cyclases) Entry Date(s): Date Created: 19990306 Date Completed: 19990323 Latest Revision: 20151119 Update Code: 20231215

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