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Article: Pituitary adenylate cyclase-activating polypeptide and its receptors: 20 Years after the discovery

TitlePituitary adenylate cyclase-activating polypeptide and its receptors: 20 Years after the discovery
Authors
Issue Date2009
PublisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.pharmrev.org/
Citation
Pharmacological Reviews, 2009, v. 61 n. 3, p. 283-357 How to Cite?
AbstractPituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior pituitary cells (Miyata et al., 1989). PACAP belongs to the vasoactive intestinal polypeptide (VIP)-secretingrowth hormone-releasing hormone-glucagon superfamily. The sequence of PACAP has been remarkably well conserved during evolution from protochordates to mammals, suggesting that PACAP is involved in the regulation of important biological functions. PACAP is widely distributed in the brain and peripheral organs, notably in the endocrine pancreas, gonads, respiratory and urogenital tracts. Characterization of the PACAP precursor has revealed the existence of a PACAP-related peptide, the activity of which remains unknown. Two types of PACAP binding sites have been characterized: type I binding sites exhibit a high affinity for PACAP and a much lower affinity for VIP, whereas type II binding sites have similar affinity for PACAP and VIP. Molecular cloning of PACAP receptors has shown the existence of three distinct receptor subtypes: the PACAP-specific PAC1-R, which is coupled to several transduction systems, and the PACAP/VIP-indifferent VPAC1-R and VPAC2-R, which are primarily coupled to adenylyl cyclase. PAC1-Rs are particularly abundant in the brain, the pituitary and the adrenal gland, whereas VPAC receptors are expressed mainly in lung, liver, and testis. The development of transgenic animal models and specific PACAP receptor ligands has strongly contributed to deciphering the various actions of PACAP. Consistent with the wide distribution of PACAP and its receptors, the peptide has now been shown to exert a large array of pharmacological effects and biological functions. The present report reviews the current knowledge concerning the pleiotropic actions of PACAP and discusses its possible use for future therapeutic applications. Copyright © 2009 by The American Society for Pharmacology and Experimental Therapeutics.
Persistent Identifierhttp://hdl.handle.net/10722/127421
ISSN
2015 Impact Factor: 18.393
2015 SCImago Journal Rankings: 8.937
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorVaudry, Den_HK
dc.contributor.authorFalluelMorel, Aen_HK
dc.contributor.authorBourgault, Sen_HK
dc.contributor.authorBasille, Men_HK
dc.contributor.authorBurel, Den_HK
dc.contributor.authorWurtz, Oen_HK
dc.contributor.authorFournier, Aen_HK
dc.contributor.authorChow, BKCen_HK
dc.contributor.authorHashimoto, Hen_HK
dc.contributor.authorGalas, Len_HK
dc.contributor.authorVaudry, Hen_HK
dc.date.accessioned2010-10-31T13:24:39Z-
dc.date.available2010-10-31T13:24:39Z-
dc.date.issued2009en_HK
dc.identifier.citationPharmacological Reviews, 2009, v. 61 n. 3, p. 283-357en_HK
dc.identifier.issn0031-6997en_HK
dc.identifier.urihttp://hdl.handle.net/10722/127421-
dc.description.abstractPituitary adenylate cyclase-activating polypeptide (PACAP) is a 38-amino acid C-terminally α-amidated peptide that was first isolated 20 years ago from an ovine hypothalamic extract on the basis of its ability to stimulate cAMP formation in anterior pituitary cells (Miyata et al., 1989). PACAP belongs to the vasoactive intestinal polypeptide (VIP)-secretingrowth hormone-releasing hormone-glucagon superfamily. The sequence of PACAP has been remarkably well conserved during evolution from protochordates to mammals, suggesting that PACAP is involved in the regulation of important biological functions. PACAP is widely distributed in the brain and peripheral organs, notably in the endocrine pancreas, gonads, respiratory and urogenital tracts. Characterization of the PACAP precursor has revealed the existence of a PACAP-related peptide, the activity of which remains unknown. Two types of PACAP binding sites have been characterized: type I binding sites exhibit a high affinity for PACAP and a much lower affinity for VIP, whereas type II binding sites have similar affinity for PACAP and VIP. Molecular cloning of PACAP receptors has shown the existence of three distinct receptor subtypes: the PACAP-specific PAC1-R, which is coupled to several transduction systems, and the PACAP/VIP-indifferent VPAC1-R and VPAC2-R, which are primarily coupled to adenylyl cyclase. PAC1-Rs are particularly abundant in the brain, the pituitary and the adrenal gland, whereas VPAC receptors are expressed mainly in lung, liver, and testis. The development of transgenic animal models and specific PACAP receptor ligands has strongly contributed to deciphering the various actions of PACAP. Consistent with the wide distribution of PACAP and its receptors, the peptide has now been shown to exert a large array of pharmacological effects and biological functions. The present report reviews the current knowledge concerning the pleiotropic actions of PACAP and discusses its possible use for future therapeutic applications. Copyright © 2009 by The American Society for Pharmacology and Experimental Therapeutics.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Pharmacology and Experimental Therapeutics. The Journal's web site is located at http://www.pharmrev.org/en_HK
dc.relation.ispartofPharmacological Reviewsen_HK
dc.titlePituitary adenylate cyclase-activating polypeptide and its receptors: 20 Years after the discoveryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0031-6997&volume=61&spage=283&epage=357&date=2009&atitle=Pituitary+Adenylate+Cyclase-Activating+Polypeptide+and+Its+Receptors:+20+Years+after+the+Discovery.en_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1124/pr.109.001370en_HK
dc.identifier.pmid19805477-
dc.identifier.scopuseid_2-s2.0-70349922918en_HK
dc.identifier.hkuros175851en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70349922918&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue3en_HK
dc.identifier.spage283en_HK
dc.identifier.epage357en_HK
dc.identifier.isiWOS:000270453000004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridVaudry, D=6603869843en_HK
dc.identifier.scopusauthoridFalluelMorel, A=6507803477en_HK
dc.identifier.scopusauthoridBourgault, S=8606232800en_HK
dc.identifier.scopusauthoridBasille, M=6603609688en_HK
dc.identifier.scopusauthoridBurel, D=16444324700en_HK
dc.identifier.scopusauthoridWurtz, O=6506682396en_HK
dc.identifier.scopusauthoridFournier, A=7401993674en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK
dc.identifier.scopusauthoridHashimoto, H=35352982100en_HK
dc.identifier.scopusauthoridGalas, L=6602711708en_HK
dc.identifier.scopusauthoridVaudry, H=35446602600en_HK

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