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Article: Secretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms

TitleSecretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanisms
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1987
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 1987, v. 84 n. 10, p. 3146-3150 How to Cite?
AbstractIn rat pancreatic acinar tissue adenylate cyclase is stimulated by low concentrations of secretin, while higher concentrations also activate phosphatidylinositol bisphosphate hydrolysis. By the use of the secretin analogues [Tyr 10,13]secretin and [Tyr 10,13,Phe 22,Trp 25]secretin, we have shown that substitution of tyrosine for leucine at positions 10 and 13 was sufficient to reduce the ability of the peptide to stimulate the production of inositol trisphosphate and the increases in cytosolic free calcium, while the ability to stimulate cAMP is little affected and the peptide remained a full agonist. Incubation with cholera toxin caused increases in cAMP, which were maximal after 30 min. Cholera toxin treatment also resulted in a marked reduction of secretin-stimulated inositol trisphosphate production, but this required a much more prolonged treatment (150-240 min), suggesting that different cholera toxin substrates were involved. Activation of protein kinase C with the phorbol ester phorbol 12-myristate 13-acetate had no effect on secretin-induced cAMP formation, nor was secretin-stimulated inositol trisphosphate formation altered by further increases in cAMP. These results indicate that the mechanisms by which secretin stimulates adenylate cyclase and activates phospholipase C in acinar tissue are completely independent.
Persistent Identifierhttp://hdl.handle.net/10722/132672
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTrimble, ERen_HK
dc.contributor.authorBruzzone, Ren_HK
dc.contributor.authorBiden, TJen_HK
dc.date.accessioned2011-03-28T09:28:07Z-
dc.date.available2011-03-28T09:28:07Z-
dc.date.issued1987en_HK
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 1987, v. 84 n. 10, p. 3146-3150en_HK
dc.identifier.issn0027-8424en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132672-
dc.description.abstractIn rat pancreatic acinar tissue adenylate cyclase is stimulated by low concentrations of secretin, while higher concentrations also activate phosphatidylinositol bisphosphate hydrolysis. By the use of the secretin analogues [Tyr 10,13]secretin and [Tyr 10,13,Phe 22,Trp 25]secretin, we have shown that substitution of tyrosine for leucine at positions 10 and 13 was sufficient to reduce the ability of the peptide to stimulate the production of inositol trisphosphate and the increases in cytosolic free calcium, while the ability to stimulate cAMP is little affected and the peptide remained a full agonist. Incubation with cholera toxin caused increases in cAMP, which were maximal after 30 min. Cholera toxin treatment also resulted in a marked reduction of secretin-stimulated inositol trisphosphate production, but this required a much more prolonged treatment (150-240 min), suggesting that different cholera toxin substrates were involved. Activation of protein kinase C with the phorbol ester phorbol 12-myristate 13-acetate had no effect on secretin-induced cAMP formation, nor was secretin-stimulated inositol trisphosphate formation altered by further increases in cAMP. These results indicate that the mechanisms by which secretin stimulates adenylate cyclase and activates phospholipase C in acinar tissue are completely independent.en_HK
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_HK
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_HK
dc.subjectChemicals And Cas Registry Numbersen_US
dc.titleSecretin stimulates cyclic AMP and inositol trisphosphate production in rat pancreatic acinar tissue by two fully independent mechanismsen_HK
dc.typeArticleen_HK
dc.identifier.emailBruzzone, R: bruzzone@hkucc.hku.hken_HK
dc.identifier.authorityBruzzone, R=rp01442en_HK
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1073/pnas.84.10.3146-
dc.identifier.pmid2437575-
dc.identifier.scopuseid_2-s2.0-0023193492en_HK
dc.identifier.volume84en_HK
dc.identifier.issue10en_HK
dc.identifier.spage3146en_HK
dc.identifier.epage3150en_HK
dc.identifier.isiWOS:A1987H388200015-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTrimble, ER=7005267920en_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK
dc.identifier.scopusauthoridBiden, TJ=7004993479en_HK

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