Article: Grass carp somatolactin: II. Pharmacological study on postreceptor signaling mechanisms for PACAP-induced somatolactin-α and -β gene expression

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TitleGrass carp somatolactin: II. Pharmacological study on postreceptor signaling mechanisms for PACAP-induced somatolactin-α and -β gene expression
AuthorsJiang, Q
He, M
Wang, X
Wong, AOL1
KeywordsGrass carp pituitary cells
Pituitary adenylate cyclase-activating polypeptide
Issue Date2008
PublisherAmerican Physiological Society. The Journal's web site is located at http://ajpendo.physiology.org/
CitationAmerican Journal Of Physiology - Endocrinology And Metabolism, 2008, v. 295 n. 2, p. E477-E490 [How to Cite?]
DOI: http://dx.doi.org/10.1152/ajpendo.90386.2008
AbstractSomatolactin (SL), the latest member of the growth hormone/prolactin family, is a novel pituitary hormone with diverse functions. However, the signal transduction mechanisms responsible for SL expression are still largely unknown. Using grass carp as an animal model, we examined the direct effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on SL gene expression at the pituitary level. In primary cultures of grass carp pituitary cells, SLα and SLδ mRNA levels could be elevated by PACAP via activation of PAC-I receptors. With the use of a pharmacological approach, the AC/cAMP/PKA and PLC/inositol 1,4,5-trisphosphate (IP3)/PKC pathways and subsequent activation of the Ca 2+/calmodulin (CaM)/CaMK-II cascades were shown to be involved in PACAP-induced SLα mRNA expression. Apparently, the downstream Ca 2+/CaM-dependent cascades were triggered by extracellular Ca 2+ ([Ca 2+] e) entry via L-type voltage-sensitive Ca 2+ channels (VSCC) and Ca 2+ release from IP3-sensitive intracellular Ca 2+ stores. In addition, the VSCC component could be activated by cAMP/PKA- and PLC/PKC-dependent mechanisms. Similar postreceptor signaling cascades were also observed for PACAP-induced SLβ mRNA expression, except that [Ca 2+] e entry through VSCC, PKC coupling to PLC, and subsequent activation of CaMK-II were not involved. These findings, taken together, provide evidence for the first time that PACAP can induce SLα and SLδ gene expression in fish model via PAC-I receptors through differential coupling to overlapping and yet distinct signaling pathways. Copyright © 2008 the American Physiological Society.
ISSN0193-1849
2011 Impact Factor: 4.746
2011 SCImago Journal Rankings: 0.542
DOIhttp://dx.doi.org/10.1152/ajpendo.90386.2008
ISI Accession Number IDWOS:000258133200031
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorJiang, Q
dc.contributor.authorHe, M
dc.contributor.authorWang, X
dc.contributor.authorWong, AOL
dc.date.accessioned2010-09-06T09:53:40Z
dc.date.available2010-09-06T09:53:40Z
dc.date.issued2008
dc.description.abstractSomatolactin (SL), the latest member of the growth hormone/prolactin family, is a novel pituitary hormone with diverse functions. However, the signal transduction mechanisms responsible for SL expression are still largely unknown. Using grass carp as an animal model, we examined the direct effects of pituitary adenylate cyclase-activating polypeptide (PACAP) on SL gene expression at the pituitary level. In primary cultures of grass carp pituitary cells, SLα and SLδ mRNA levels could be elevated by PACAP via activation of PAC-I receptors. With the use of a pharmacological approach, the AC/cAMP/PKA and PLC/inositol 1,4,5-trisphosphate (IP3)/PKC pathways and subsequent activation of the Ca 2+/calmodulin (CaM)/CaMK-II cascades were shown to be involved in PACAP-induced SLα mRNA expression. Apparently, the downstream Ca 2+/CaM-dependent cascades were triggered by extracellular Ca 2+ ([Ca 2+] e) entry via L-type voltage-sensitive Ca 2+ channels (VSCC) and Ca 2+ release from IP3-sensitive intracellular Ca 2+ stores. In addition, the VSCC component could be activated by cAMP/PKA- and PLC/PKC-dependent mechanisms. Similar postreceptor signaling cascades were also observed for PACAP-induced SLβ mRNA expression, except that [Ca 2+] e entry through VSCC, PKC coupling to PLC, and subsequent activation of CaMK-II were not involved. These findings, taken together, provide evidence for the first time that PACAP can induce SLα and SLδ gene expression in fish model via PAC-I receptors through differential coupling to overlapping and yet distinct signaling pathways. Copyright © 2008 the American Physiological Society.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationAmerican Journal Of Physiology - Endocrinology And Metabolism, 2008, v. 295 n. 2, p. E477-E490 [How to Cite?]
DOI: http://dx.doi.org/10.1152/ajpendo.90386.2008
dc.identifier.doihttp://dx.doi.org/10.1152/ajpendo.90386.2008
dc.identifier.epageE490
dc.identifier.hkuros151032
dc.identifier.isiWOS:000258133200031
dc.identifier.issn0193-1849
2011 Impact Factor: 4.746
2011 SCImago Journal Rankings: 0.542
dc.identifier.issue2
dc.identifier.openurl
dc.identifier.scopuseid_2-s2.0-52649086807
dc.identifier.spageE477
dc.identifier.urihttp://hdl.handle.net/10722/89191
dc.identifier.volume295
dc.languageeng
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://ajpendo.physiology.org/
dc.publisher.placeUnited States
dc.relation.ispartofAmerican Journal of Physiology - Endocrinology and Metabolism
dc.relation.referencesReferences in Scopus
dc.subjectGrass carp pituitary cells
dc.subjectPituitary adenylate cyclase-activating polypeptide
dc.titleGrass carp somatolactin: II. Pharmacological study on postreceptor signaling mechanisms for PACAP-induced somatolactin-α and -β gene expression
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong