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Article: Goldfish calmodulin: Molecular cloning, tissue distribution, and regulation of transcript expression in goldfish pituitary cells

TitleGoldfish calmodulin: Molecular cloning, tissue distribution, and regulation of transcript expression in goldfish pituitary cells
Authors
Issue Date2004
PublisherThe Endocrine Society. The Journal's web site is located at http://endo.endojournals.org
Citation
Endocrinology, 2004, v. 145 n. 11, p. 5056-5067 How to Cite?
AbstractCalmodulin (CaM) is a Ca2+-binding protein essential for biological functions mediated through Ca2+-dependent mechanisms. In the goldfish, CaM is involved in the signaling events mediating pituitary hormone secretion induced by hypothalamic factors. However, the structural identity of goldfish CaM has not been established, and the neuroendocrine mechanisms regulating CaM gene expression at the pituitary level are still unknown. Here we cloned the goldfish CaM and tested the hypothesis that pituitary expression of CaM transcripts can be the target of modulation by hypothalamic factors. Three goldfish CaM cDNAs, namely CaM-a, CaM-bS, and CaM-bL, were isolated by library screening. These cDNAs carry a 450-bp open reading frame encoding the same 149-amino acid CaM protein, the amino acid sequence of which is identical with that of mammals, birds, and amphibians and is highly homologous (≥90%) to that in invertebrates. In goldfish pituitary cells, activation of cAMP- or PKC-dependent pathways increased CaM mRNA levels, whereas the opposite was true for induction of Ca2+ entry. Basal levels of CaM mRNA was accentuated by GnRH and pituitary adenylate cyclase-activating polypeptide but suppressed by dopaminergic stimulation. Pharmacological studies using D1 and D2 analogs revealed that dopaminergic inhibition of CaM mRNA expression was mediated through pituitary D2 receptors. At the pituitary level, D2 activation was also effective in blocking GnRH- and pituitary adenylate cyclase-activating polypeptide-stimulated CaM mRNA expression. As a whole, the present study has confirmed that the molecular structure of CaM is highly conserved, and its mRNA expression at the pituitary level can be regulated by interactions among hypothalamic factors.
Persistent Identifierhttp://hdl.handle.net/10722/84715
ISSN
2015 Impact Factor: 4.159
2015 SCImago Journal Rankings: 2.363
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorHuo, Len_HK
dc.contributor.authorLee, EKYen_HK
dc.contributor.authorLeung, PCen_HK
dc.contributor.authorWong, AOLen_HK
dc.date.accessioned2010-09-06T08:56:17Z-
dc.date.available2010-09-06T08:56:17Z-
dc.date.issued2004en_HK
dc.identifier.citationEndocrinology, 2004, v. 145 n. 11, p. 5056-5067en_HK
dc.identifier.issn0013-7227en_HK
dc.identifier.urihttp://hdl.handle.net/10722/84715-
dc.description.abstractCalmodulin (CaM) is a Ca2+-binding protein essential for biological functions mediated through Ca2+-dependent mechanisms. In the goldfish, CaM is involved in the signaling events mediating pituitary hormone secretion induced by hypothalamic factors. However, the structural identity of goldfish CaM has not been established, and the neuroendocrine mechanisms regulating CaM gene expression at the pituitary level are still unknown. Here we cloned the goldfish CaM and tested the hypothesis that pituitary expression of CaM transcripts can be the target of modulation by hypothalamic factors. Three goldfish CaM cDNAs, namely CaM-a, CaM-bS, and CaM-bL, were isolated by library screening. These cDNAs carry a 450-bp open reading frame encoding the same 149-amino acid CaM protein, the amino acid sequence of which is identical with that of mammals, birds, and amphibians and is highly homologous (≥90%) to that in invertebrates. In goldfish pituitary cells, activation of cAMP- or PKC-dependent pathways increased CaM mRNA levels, whereas the opposite was true for induction of Ca2+ entry. Basal levels of CaM mRNA was accentuated by GnRH and pituitary adenylate cyclase-activating polypeptide but suppressed by dopaminergic stimulation. Pharmacological studies using D1 and D2 analogs revealed that dopaminergic inhibition of CaM mRNA expression was mediated through pituitary D2 receptors. At the pituitary level, D2 activation was also effective in blocking GnRH- and pituitary adenylate cyclase-activating polypeptide-stimulated CaM mRNA expression. As a whole, the present study has confirmed that the molecular structure of CaM is highly conserved, and its mRNA expression at the pituitary level can be regulated by interactions among hypothalamic factors.en_HK
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.rightsEndocrinology. Copyright © The Endocrine Society.en_HK
dc.titleGoldfish calmodulin: Molecular cloning, tissue distribution, and regulation of transcript expression in goldfish pituitary cellsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0013-7227&volume=145&spage=5056&epage=5067&date=2004&atitle=Goldfish+Calmodulin:+Molecular+Cloning,+Tissue+Distribution,+and+Regulation+of+Transcript+Expression+in+Goldfish+Pituitary+Cellsen_HK
dc.identifier.emailLeung, PC: pcleung@hkucc.hku.hken_HK
dc.identifier.emailWong, AOL: olwong@hkucc.hku.hken_HK
dc.identifier.authorityLeung, PC=rp00735en_HK
dc.identifier.authorityWong, AOL=rp00806en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1210/en.2004-0584en_HK
dc.identifier.pmid15297449-
dc.identifier.scopuseid_2-s2.0-9244231118en_HK
dc.identifier.hkuros98357en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-9244231118&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume145en_HK
dc.identifier.issue11en_HK
dc.identifier.spage5056en_HK
dc.identifier.epage5067en_HK
dc.identifier.isiWOS:000224510100035-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridHuo, L=9275343500en_HK
dc.identifier.scopusauthoridLee, EKY=7406968652en_HK
dc.identifier.scopusauthoridLeung, PC=35080988800en_HK
dc.identifier.scopusauthoridWong, AOL=7403147570en_HK

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