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Article: Structural and functional identification of the pituitary adenylate cyclase-activating polypeptide receptor VPAC2 from the frog Rana tigrina rugulosa

TitleStructural and functional identification of the pituitary adenylate cyclase-activating polypeptide receptor VPAC2 from the frog Rana tigrina rugulosa
Authors
Issue Date2001
PublisherSociety for Endocrinology. The Journal's web site is located at http://jme.endocrinology-journals.org/
Citation
Journal Of Molecular Endocrinology, 2001, v. 27 n. 2, p. 229-238 How to Cite?
AbstractRecently, a frog pituitary adenylate cyclase-activating polypeptide (PACAP)/vasoactive intestinal peptide (VIP) receptor (fPVR) has been characterized, and interestingly, this receptor exhibits characteristics of both mammalian PACAP type II receptors VPAC1R and VPAC2R. In order to investigate the receptors responsible for mediating the actions of VIP and PACAP in amphibians, in this report, a frog VPAC2 receptor (fVPAC2R) cDNA was isolated. fVPAC2R shares 47.7, 46.9 and 62.5% amino acid sequence identify with fPVR, human VPAC1R and human VPAC2R respectively. Functionally, fVPAC2R, when expressed in CHO cells, was responsive to both frog peptides including VIP, PACAP38 and PACAP27 where the EC50 values of these peptides in intracellular cAMP production were 0.15, 0.18 and 0.16 μM respectively. The pharmacological profiles of human peptides (VIP, PACAP38 and peptide histidine methionine) to stimulate frog and human VPAC2Rs were compared, and it was found that these peptides could only activate the frog receptor at micromolar concentrations. fVPAC2R was found to be widely distributed in various peripheral tissues as well as several regions of the brain. The presence of the receptor transcripts suggests the functional roles of the receptor in mediating the actions of PACAP and/or VIP in these tissues. As VIP and particularly PACAP27 are highly conserved peptides in vertebrate evolution, comparative studies of these peptides and their receptors in non-mammalian vertebrates should provide clues to better understand the physiology of these important peptides in human and other vertebrates.
Persistent Identifierhttp://hdl.handle.net/10722/84792
ISSN
2015 Impact Factor: 2.947
2015 SCImago Journal Rankings: 1.674
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHoo, RLCen_HK
dc.contributor.authorAlexandre, Den_HK
dc.contributor.authorChan, SMen_HK
dc.contributor.authorAnouar, Yen_HK
dc.contributor.authorPang, RTKen_HK
dc.contributor.authorVaudry, Hen_HK
dc.contributor.authorChow, BKCen_HK
dc.date.accessioned2010-09-06T08:57:10Z-
dc.date.available2010-09-06T08:57:10Z-
dc.date.issued2001en_HK
dc.identifier.citationJournal Of Molecular Endocrinology, 2001, v. 27 n. 2, p. 229-238en_HK
dc.identifier.issn0952-5041en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84792-
dc.description.abstractRecently, a frog pituitary adenylate cyclase-activating polypeptide (PACAP)/vasoactive intestinal peptide (VIP) receptor (fPVR) has been characterized, and interestingly, this receptor exhibits characteristics of both mammalian PACAP type II receptors VPAC1R and VPAC2R. In order to investigate the receptors responsible for mediating the actions of VIP and PACAP in amphibians, in this report, a frog VPAC2 receptor (fVPAC2R) cDNA was isolated. fVPAC2R shares 47.7, 46.9 and 62.5% amino acid sequence identify with fPVR, human VPAC1R and human VPAC2R respectively. Functionally, fVPAC2R, when expressed in CHO cells, was responsive to both frog peptides including VIP, PACAP38 and PACAP27 where the EC50 values of these peptides in intracellular cAMP production were 0.15, 0.18 and 0.16 μM respectively. The pharmacological profiles of human peptides (VIP, PACAP38 and peptide histidine methionine) to stimulate frog and human VPAC2Rs were compared, and it was found that these peptides could only activate the frog receptor at micromolar concentrations. fVPAC2R was found to be widely distributed in various peripheral tissues as well as several regions of the brain. The presence of the receptor transcripts suggests the functional roles of the receptor in mediating the actions of PACAP and/or VIP in these tissues. As VIP and particularly PACAP27 are highly conserved peptides in vertebrate evolution, comparative studies of these peptides and their receptors in non-mammalian vertebrates should provide clues to better understand the physiology of these important peptides in human and other vertebrates.en_HK
dc.languageengen_HK
dc.publisherSociety for Endocrinology. The Journal's web site is located at http://jme.endocrinology-journals.org/en_HK
dc.relation.ispartofJournal of Molecular Endocrinologyen_HK
dc.rightsJournal of Molecular Endocrinology. Copyright © Society for Endocrinology.en_HK
dc.subject.meshAmino Acid Sequence-
dc.subject.meshAnimals-
dc.subject.meshPituitary Gland - metabolism-
dc.subject.meshRanidae - genetics - metabolism-
dc.subject.meshReceptors, Vasoactive Intestinal Peptide - chemistry - genetics - metabolism-
dc.titleStructural and functional identification of the pituitary adenylate cyclase-activating polypeptide receptor VPAC2 from the frog Rana tigrina rugulosaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0952-5041&volume=27&issue=2&spage=229&epage=238&date=2001&atitle=Structural+and+functional+identification+of+the+pituitary+adenylate+cyclase-activating+polypeptide+receptor+VPAC2+from+the+frog+Rana+tigrina+rugulosa+en_HK
dc.identifier.emailHoo, RLC: rubyhoo@hkucc.hku.hken_HK
dc.identifier.emailPang, RTK: rtkpang@hku.hken_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityHoo, RLC=rp01334en_HK
dc.identifier.authorityPang, RTK=rp01761en_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1677/jme.0.0270229en_HK
dc.identifier.pmid11564605-
dc.identifier.scopuseid_2-s2.0-0034786385en_HK
dc.identifier.hkuros65788en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034786385&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume27en_HK
dc.identifier.issue2en_HK
dc.identifier.spage229en_HK
dc.identifier.epage238en_HK
dc.identifier.isiWOS:000171523100008-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridHoo, RLC=6602369766en_HK
dc.identifier.scopusauthoridAlexandre, D=7004013112en_HK
dc.identifier.scopusauthoridChan, SM=7404255669en_HK
dc.identifier.scopusauthoridAnouar, Y=7003561768en_HK
dc.identifier.scopusauthoridPang, RTK=7004376636en_HK
dc.identifier.scopusauthoridVaudry, H=35446602600en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK

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