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- Publisher Website: 10.1111/j.1432-1033.1989.tb14558.x
- Scopus: eid_2-s2.0-0024576781
- PMID: 2465152
- WOS: WOS:A1989T174100010
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Article: Mechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathway
Title | Mechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathway |
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Authors | |
Keywords | Chemicals And Cas Registry Numbers |
Issue Date | 1989 |
Publisher | Blackwell 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/132776 |
ISSN | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Bruzzone, R | en_HK |
dc.date.accessioned | 2011-03-28T09:28:54Z | - |
dc.date.available | 2011-03-28T09:28:54Z | - |
dc.date.issued | 1989 | en_HK |
dc.identifier.citation | European Journal Of Biochemistry, 1989, v. 179 n. 2, p. 323-331 | en_HK |
dc.identifier.issn | 0014-2956 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/132776 | - |
dc.description.abstract | The 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.language | eng | en_US |
dc.publisher | Blackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/EJB | en_HK |
dc.relation.ispartof | European Journal of Biochemistry | en_HK |
dc.subject | Chemicals And Cas Registry Numbers | en_US |
dc.title | Mechanism of action of bombesin on amylase secretion. Evidence for a Ca2+-independent pathway | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Bruzzone, R: bruzzone@hkucc.hku.hk | en_HK |
dc.identifier.authority | Bruzzone, R=rp01442 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1111/j.1432-1033.1989.tb14558.x | - |
dc.identifier.pmid | 2465152 | - |
dc.identifier.scopus | eid_2-s2.0-0024576781 | en_HK |
dc.identifier.volume | 179 | en_HK |
dc.identifier.issue | 2 | en_HK |
dc.identifier.spage | 323 | en_HK |
dc.identifier.epage | 331 | en_HK |
dc.identifier.isi | WOS:A1989T174100010 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Bruzzone, R=7006793327 | en_HK |
dc.identifier.issnl | 0014-2956 | - |