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Article: Mechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathway

TitleMechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathway
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1989
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB
Citation
European Journal Of Biochemistry, 1989, v. 179 n. 2, p. 323-331 How to Cite?
AbstractThe mode of action of bombesin on amylase secretion was investigated in rat pancreatic acini. Bombesin induced a dose-dependent increase in inositol 1,4,5-trisphosphate and cytosolic free Ca2+. The threshold concentration capable of inducing both effects was 0.1 nM and the half-maximal dose of the peptide for Ca2+ mobilization was approximately 0.6 nM. By contrast, amylase release was approximately 30 times more sensitive than inositol 1,4,5-trisphosphate production and Ca2+ mobilization to bombesin action, with 1 pM being the first stimulatory concentration and a half-maximal effect at approximately 20 pM. The ability of low bombesin doses to trigger enzyme secretion was unaffected by chelation of extracellular Ca2+ with EGTA. In order to test whether the stimulation of amylase release was truly a Ca2+-independent response, the intracellular Ca2+ stores were depleted by pretreating acini with EGTA plus ionomycin, the Ca2+ ionophore. Under these conditions bombesin was still capable of eliciting a significant twofold enhancement of the secretory activity. These results indicate that bombesin, an agonist thought to activate secretion mainly through mobilization of Ca2+ from intracellular stores, elicits amylase release at low concentrations, independently of a concomitant rise in cytosolic free Ca2+. The relevance of these findings to the physiological regulation of pancreatic exocrine secretion is discussed.
Persistent Identifierhttp://hdl.handle.net/10722/132776
ISSN
2006 Impact Factor: 3.579
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBruzzone, Ren_HK
dc.date.accessioned2011-03-28T09:28:54Z-
dc.date.available2011-03-28T09:28:54Z-
dc.date.issued1989en_HK
dc.identifier.citationEuropean Journal Of Biochemistry, 1989, v. 179 n. 2, p. 323-331en_HK
dc.identifier.issn0014-2956en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132776-
dc.description.abstractThe mode of action of bombesin on amylase secretion was investigated in rat pancreatic acini. Bombesin induced a dose-dependent increase in inositol 1,4,5-trisphosphate and cytosolic free Ca2+. The threshold concentration capable of inducing both effects was 0.1 nM and the half-maximal dose of the peptide for Ca2+ mobilization was approximately 0.6 nM. By contrast, amylase release was approximately 30 times more sensitive than inositol 1,4,5-trisphosphate production and Ca2+ mobilization to bombesin action, with 1 pM being the first stimulatory concentration and a half-maximal effect at approximately 20 pM. The ability of low bombesin doses to trigger enzyme secretion was unaffected by chelation of extracellular Ca2+ with EGTA. In order to test whether the stimulation of amylase release was truly a Ca2+-independent response, the intracellular Ca2+ stores were depleted by pretreating acini with EGTA plus ionomycin, the Ca2+ ionophore. Under these conditions bombesin was still capable of eliciting a significant twofold enhancement of the secretory activity. These results indicate that bombesin, an agonist thought to activate secretion mainly through mobilization of Ca2+ from intracellular stores, elicits amylase release at low concentrations, independently of a concomitant rise in cytosolic free Ca2+. The relevance of these findings to the physiological regulation of pancreatic exocrine secretion is discussed.en_HK
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJBen_HK
dc.relation.ispartofEuropean Journal of Biochemistryen_HK
dc.subjectChemicals And Cas Registry Numbersen_US
dc.titleMechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathwayen_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.pmid2465152-
dc.identifier.scopuseid_2-s2.0-0024576781en_HK
dc.identifier.volume179en_HK
dc.identifier.issue2en_HK
dc.identifier.spage323en_HK
dc.identifier.epage331en_HK
dc.identifier.isiWOS:A1989T174100010-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK

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