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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, Q1
He, M1
Wang, X1
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
2013 Impact Factor: 4.088
 
DOIhttp://dx.doi.org/10.1152/ajpendo.90386.2008
 
ISI Accession Number IDWOS:000258133200031
 
ReferencesReferences in Scopus
 
DC FieldValue
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.eissn1522-1555
 
dc.identifier.epageE490
 
dc.identifier.hkuros151032
 
dc.identifier.isiWOS:000258133200031
 
dc.identifier.issn0193-1849
2013 Impact Factor: 4.088
 
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
 
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<description.abstract>Somatolactin (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, SL&#945; and SL&#948; 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 SL&#945; 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 SL&#946; 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 SL&#945; and SL&#948; gene expression in fish model via PAC-I receptors through differential coupling to overlapping and yet distinct signaling pathways. Copyright &#169; 2008 the American Physiological Society.</description.abstract>
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Author Affiliations
  1. The University of Hong Kong