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Article: Hypophysiotropic action of pituitary adenylate cyclase-activating polypeptide (PACAP) in the goldfish: Immunohistochemical demonstration of PACAP in the pituitary, PACAP stimulation of growth hormone release from pituitary cells, and molecular cloning of pituitary type I PACAP receptor

TitleHypophysiotropic action of pituitary adenylate cyclase-activating polypeptide (PACAP) in the goldfish: Immunohistochemical demonstration of PACAP in the pituitary, PACAP stimulation of growth hormone release from pituitary cells, and molecular cloning of pituitary type I PACAP receptor
Authors
Issue Date1998
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 1998, v. 139 n. 8, p. 3465-3479 How to Cite?
AbstractPituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the glucagon/secretin peptide family, and its molecular structure is highly conserved in vertebrates. In this study, the functional role of PACAP in regulating GH release in the goldfish was investigated. Using immunohistochemical staining, nerve fibers with PACAP immunoreactivity were identified in the vicinity of goldfish somatotrophs, suggesting that this neuropeptide may influence GH release in the goldfish. The direct regulatory action of PACAP on GH secretion was demonstrated in vitro in perifused goldfish pituitary cells. PACAPs (0.01 nM to 1 μM) from different species, including ovine PACAP 27, ovine PACAP 38, frog PACAP 38, zebra fish PACAP 27, and zebra fish PACAP 38, were all effective in stimulating GH release with ED 50 values of 8.9 ± 3.5, 3.3 ± 1.6, 14.4 ± 3.5, 15.4 ± 4.1, and 1.4 ± 0.2 nM, respectively. Similar concentrations of vasoactive intestinal polypeptide (VIP), a peptide related to PACAP, was not effective in this respect. In addition, the GH-releasing action of ovine PACAP 38 (10 nM) was inhibited by the PACAP antagonist PACAP 6-38 (10 μM), but not by the VIP antagonist [4-Cl-D-Phe 6, Leu 17]VIP (10 μM). The pharmacology of these GH responses is consistent with the mammalian type I PACAP receptors, suggesting that a similar receptor sub- type is present in the goldfish pituitary and mediates the GH-releasing action of PACAP. To establish the structural identity of this goldfish PACAP receptor, a complementary DNA (cDNA) clone sharing a high degree of sequence homology with mammalian type I PACAP receptors was isolated from a goldfish pituitary cDNA library. This cDNA was 5.2 kb in size with a 1.4-kb open reading frame and encoded a 465- amino acid protein with the typical structure of a 7-transmembrane domain- containing, G protein-coupled receptor. Functional expression of this cDNA in COS-7 cells revealed that this fish type I PACAP receptor could be activated by ovine PACAP 27 and PACAP 38 to increase cAMP synthesis with ED 50 values of 2.4 ± 0.8 and 4.2 ± 1.2 nM, respectively. Other structurally related peptides, including VIP (100 nM), GH-releasing hormone (100 nM), glucagon (100 nM), secretin (100 nM), gastric inhibitory polypeptide (100 nM), and PTH (100 nM), were not effective in altering cAMP production. Using Northern blot and RT-PCR, messenger RNA transcripts of this PACAP receptor were identified in the brain, heart, and pituitary of the goldfish. These results, taken together, support the hypothesis that PACAP functions as a novel GH-releasing factor in the goldfish through activation of type I PACAP receptors.
Persistent Identifierhttp://hdl.handle.net/10722/49356
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWong, AOLen_HK
dc.contributor.authorLeung, MYen_HK
dc.contributor.authorShea, WLCen_HK
dc.contributor.authorTse, LYen_HK
dc.contributor.authorChang, JPen_HK
dc.contributor.authorChow, BKCen_HK
dc.date.accessioned2008-06-12T06:40:14Z-
dc.date.available2008-06-12T06:40:14Z-
dc.date.issued1998en_HK
dc.identifier.citationEndocrinology, 1998, v. 139 n. 8, p. 3465-3479en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/49356-
dc.description.abstractPituitary adenylate cyclase-activating polypeptide (PACAP) is a member of the glucagon/secretin peptide family, and its molecular structure is highly conserved in vertebrates. In this study, the functional role of PACAP in regulating GH release in the goldfish was investigated. Using immunohistochemical staining, nerve fibers with PACAP immunoreactivity were identified in the vicinity of goldfish somatotrophs, suggesting that this neuropeptide may influence GH release in the goldfish. The direct regulatory action of PACAP on GH secretion was demonstrated in vitro in perifused goldfish pituitary cells. PACAPs (0.01 nM to 1 μM) from different species, including ovine PACAP 27, ovine PACAP 38, frog PACAP 38, zebra fish PACAP 27, and zebra fish PACAP 38, were all effective in stimulating GH release with ED 50 values of 8.9 ± 3.5, 3.3 ± 1.6, 14.4 ± 3.5, 15.4 ± 4.1, and 1.4 ± 0.2 nM, respectively. Similar concentrations of vasoactive intestinal polypeptide (VIP), a peptide related to PACAP, was not effective in this respect. In addition, the GH-releasing action of ovine PACAP 38 (10 nM) was inhibited by the PACAP antagonist PACAP 6-38 (10 μM), but not by the VIP antagonist [4-Cl-D-Phe 6, Leu 17]VIP (10 μM). The pharmacology of these GH responses is consistent with the mammalian type I PACAP receptors, suggesting that a similar receptor sub- type is present in the goldfish pituitary and mediates the GH-releasing action of PACAP. To establish the structural identity of this goldfish PACAP receptor, a complementary DNA (cDNA) clone sharing a high degree of sequence homology with mammalian type I PACAP receptors was isolated from a goldfish pituitary cDNA library. This cDNA was 5.2 kb in size with a 1.4-kb open reading frame and encoded a 465- amino acid protein with the typical structure of a 7-transmembrane domain- containing, G protein-coupled receptor. Functional expression of this cDNA in COS-7 cells revealed that this fish type I PACAP receptor could be activated by ovine PACAP 27 and PACAP 38 to increase cAMP synthesis with ED 50 values of 2.4 ± 0.8 and 4.2 ± 1.2 nM, respectively. Other structurally related peptides, including VIP (100 nM), GH-releasing hormone (100 nM), glucagon (100 nM), secretin (100 nM), gastric inhibitory polypeptide (100 nM), and PTH (100 nM), were not effective in altering cAMP production. Using Northern blot and RT-PCR, messenger RNA transcripts of this PACAP receptor were identified in the brain, heart, and pituitary of the goldfish. These results, taken together, support the hypothesis that PACAP functions as a novel GH-releasing factor in the goldfish through activation of type I PACAP receptors.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.orgen_HK
dc.relation.ispartofEndocrinologyen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.subject.meshGoldfishen_HK
dc.subject.meshGrowth Hormone - secretionen_HK
dc.subject.meshNeuropeptides - analysis - pharmacologyen_HK
dc.subject.meshPituitary Gland - chemistry - drug effects - physiologyen_HK
dc.subject.meshReceptors, Pituitary Hormone - chemistry - geneticsen_HK
dc.titleHypophysiotropic action of pituitary adenylate cyclase-activating polypeptide (PACAP) in the goldfish: Immunohistochemical demonstration of PACAP in the pituitary, PACAP stimulation of growth hormone release from pituitary cells, and molecular cloning of pituitary type I PACAP receptoren_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=139&issue=8&spage=3465&epage=3479&date=1998&atitle=Hypophysiotropic+action+of+pituitary+adenylate+cyclase+activating+polypeptide+(PACAP)+in+the+goldfish:+Immunohistochemical+demonstration+of+PACAP+in+the+pituitary,+PACAP+stimulation+of+growth+hormone+release,+and+molecular+cloning+of+goldfish+pituitary+tyen_HK
dc.identifier.emailWong, AOL: olwong@hkucc.hku.hken_HK
dc.identifier.emailLeung, MY: kmyleung@hku.hken_HK
dc.identifier.emailChow, BKC: bkcc@hku.hken_HK
dc.identifier.authorityWong, AOL=rp00806en_HK
dc.identifier.authorityLeung, MY=rp00733en_HK
dc.identifier.authorityChow, BKC=rp00681en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1210/en.139.8.3465en_HK
dc.identifier.pmid9681497-
dc.identifier.scopuseid_2-s2.0-0031760755en_HK
dc.identifier.hkuros35060-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031760755&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume139en_HK
dc.identifier.issue8en_HK
dc.identifier.spage3465en_HK
dc.identifier.epage3479en_HK
dc.identifier.isiWOS:000074922600014-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWong, AOL=7403147570en_HK
dc.identifier.scopusauthoridLeung, MY=7401860738en_HK
dc.identifier.scopusauthoridShea, WLC=36854119600en_HK
dc.identifier.scopusauthoridTse, LY=36891045500en_HK
dc.identifier.scopusauthoridChang, JP=7601547649en_HK
dc.identifier.scopusauthoridChow, BKC=7102826193en_HK

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