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Article: Molecular evolution of vertebrate VIP receptors and functional characterization of a VIP receptor from goldfish Carassius auratus

TitleMolecular evolution of vertebrate VIP receptors and functional characterization of a VIP receptor from goldfish Carassius auratus
Authors
Issue Date1997
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygcen
Citation
General And Comparative Endocrinology, 1997, v. 105 n. 2, p. 176-185 How to Cite?
AbstractVasoactive intestinal polypeptide (VIP) is a neuropeptide that has numerous physiological actions and is widely distributed in the body. However, as yet, there is no sequence information about VIP receptors in lower vertebrates. Partial cDNA fragments spanning transmembrane domains 2 to 6 of VIP receptors were isolated from six nonmammalian vertebrate species, including chicken, pigeon, frog, lizard, salmon, and goldfish. Sequence comparison of these receptors revealed essential structural motifs responsible for receptor function. In addition, the first nonmammalian full- length VIP receptor cDNA was obtained by screening a goldfish brain and pituitary cDNA library. Functional expression of this receptor in mammalian COS-7 cells showed that it is coupled to cAMP production in a VIP and PACAP concentration-dependent manner; the EC 50 of VIP was determined to be 1 nM. At 100 nM peptide, the relative potency of various peptides in stimulating cAMP in the transfected cells was VIP > PACAP > GHRH = secretin > PHM > PTH > glucagon > GLP-1 > GIP. Characterization of the VIP receptors in lower vertebrates should enhance our understanding of the molecular evolution and physiology of VIP in vertebrates.
Persistent Identifierhttp://hdl.handle.net/10722/84895
ISSN
2015 Impact Factor: 2.667
2015 SCImago Journal Rankings: 1.245
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChow, BKCen_HK
dc.contributor.authorYuen, TTHen_HK
dc.contributor.authorChan, KWen_HK
dc.date.accessioned2010-09-06T08:58:22Z-
dc.date.available2010-09-06T08:58:22Z-
dc.date.issued1997en_HK
dc.identifier.citationGeneral And Comparative Endocrinology, 1997, v. 105 n. 2, p. 176-185en_HK
dc.identifier.issn0016-6480en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84895-
dc.description.abstractVasoactive intestinal polypeptide (VIP) is a neuropeptide that has numerous physiological actions and is widely distributed in the body. However, as yet, there is no sequence information about VIP receptors in lower vertebrates. Partial cDNA fragments spanning transmembrane domains 2 to 6 of VIP receptors were isolated from six nonmammalian vertebrate species, including chicken, pigeon, frog, lizard, salmon, and goldfish. Sequence comparison of these receptors revealed essential structural motifs responsible for receptor function. In addition, the first nonmammalian full- length VIP receptor cDNA was obtained by screening a goldfish brain and pituitary cDNA library. Functional expression of this receptor in mammalian COS-7 cells showed that it is coupled to cAMP production in a VIP and PACAP concentration-dependent manner; the EC 50 of VIP was determined to be 1 nM. At 100 nM peptide, the relative potency of various peptides in stimulating cAMP in the transfected cells was VIP > PACAP > GHRH = secretin > PHM > PTH > glucagon > GLP-1 > GIP. Characterization of the VIP receptors in lower vertebrates should enhance our understanding of the molecular evolution and physiology of VIP in vertebrates.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/ygcenen_HK
dc.relation.ispartofGeneral and Comparative Endocrinologyen_HK
dc.titleMolecular evolution of vertebrate VIP receptors and functional characterization of a VIP receptor from goldfish Carassius auratusen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0016-6480&volume=105&spage=176&epage=185&date=1997&atitle=Molecular+evolution+of+vertebrate+VIP+receptors+and+functional+characterization+of+a+VIP+receptor+from+goldfish,+Carassius+auratusen_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1006/gcen.1996.6818en_HK
dc.identifier.pmid9038250-
dc.identifier.scopuseid_2-s2.0-0031081172en_HK
dc.identifier.hkuros24436en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031081172&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume105en_HK
dc.identifier.issue2en_HK
dc.identifier.spage176en_HK
dc.identifier.epage185en_HK
dc.identifier.isiWOS:A1997WK78300005-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK
dc.identifier.scopusauthoridYuen, TTH=36957362600en_HK
dc.identifier.scopusauthoridChan, KW=8587755300en_HK

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