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Article: Caerulein causes translocation of protein kinase C in rat acini without increasing cytosolic free Ca2+

TitleCaerulein causes translocation of protein kinase C in rat acini without increasing cytosolic free Ca2+
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1988
PublisherAmerican Physiological Society. The Journal's web site is located at http://ajpcon.physiology.org/
Citation
American Journal Of Physiology - Gastrointestinal And Liver Physiology, 1988, v. 255 n. 1, p. 18/1 How to Cite?
AbstractWe investigated the relationships between changes in cytosolic free Ca2+ ([Ca2+](i)) and amylase secretion in dispersed rat pancreatic acini. Although 10 pM caerulein did not raise [Ca2+](i), higher concentrations (1 nM) of the peptide elicited a prompt, marked, but transient (2-3 min) elevation of [Ca2+](i). Both concentrations of caerulein caused an almost identical release of amylase over a 30-min period. To investigate the mechanism(s) underlying Ca2+-independent secretion, we measured the effect of the secretagogue on protein kinase C activity and found that both caerulein concentrations caused a significant translocation of protein kinase C from the cytosolic to the microsomal fraction. Because 1 nM caerulein induced a greater enzyme secretion than 10 pM caerulein during the first 2-5 min of stimulation, we explored further the role of [Ca2+](i) transients during the first minutes of secretion. Addition of ionomycin in the presence of 10 pM caerulein resulted in a rise in [Ca2+](i) and enhanced secretion as a result of caerulein in a near additive fashion during the first 2 min of stimulation. Second, we pretreated acini for 5 min with 1 μM 12-O-tetradecanoylphorbol-13-acetate. This maneuver inhibited both caerulein-induced inositol trisphosphate formation and [Ca2+](i) elevation. These findings were paralleled by a similar inhibition of caerulein-stimulated amylase release only during the first 5 min of secretion. These results indicate that 1) caerulein can stimulate amylase secretion independently of a concomitant [Ca2+](i) rise, possibly by activation of protein kinase C, and 2) an elevation of [Ca2+](i) serves as a trigger to enhance amylase release only during the initial phase of secretion.
Persistent Identifierhttp://hdl.handle.net/10722/132781
ISSN
1998 Impact Factor: 3.077
2004 SCImago Journal Rankings: 1.102
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBruzzone, Ren_HK
dc.contributor.authorRegazzi, Ren_HK
dc.contributor.authorWollheim, CBen_HK
dc.date.accessioned2011-03-28T09:28:56Z-
dc.date.available2011-03-28T09:28:56Z-
dc.date.issued1988en_HK
dc.identifier.citationAmerican Journal Of Physiology - Gastrointestinal And Liver Physiology, 1988, v. 255 n. 1, p. 18/1en_HK
dc.identifier.issn0002-9513en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132781-
dc.description.abstractWe investigated the relationships between changes in cytosolic free Ca2+ ([Ca2+](i)) and amylase secretion in dispersed rat pancreatic acini. Although 10 pM caerulein did not raise [Ca2+](i), higher concentrations (1 nM) of the peptide elicited a prompt, marked, but transient (2-3 min) elevation of [Ca2+](i). Both concentrations of caerulein caused an almost identical release of amylase over a 30-min period. To investigate the mechanism(s) underlying Ca2+-independent secretion, we measured the effect of the secretagogue on protein kinase C activity and found that both caerulein concentrations caused a significant translocation of protein kinase C from the cytosolic to the microsomal fraction. Because 1 nM caerulein induced a greater enzyme secretion than 10 pM caerulein during the first 2-5 min of stimulation, we explored further the role of [Ca2+](i) transients during the first minutes of secretion. Addition of ionomycin in the presence of 10 pM caerulein resulted in a rise in [Ca2+](i) and enhanced secretion as a result of caerulein in a near additive fashion during the first 2 min of stimulation. Second, we pretreated acini for 5 min with 1 μM 12-O-tetradecanoylphorbol-13-acetate. This maneuver inhibited both caerulein-induced inositol trisphosphate formation and [Ca2+](i) elevation. These findings were paralleled by a similar inhibition of caerulein-stimulated amylase release only during the first 5 min of secretion. These results indicate that 1) caerulein can stimulate amylase secretion independently of a concomitant [Ca2+](i) rise, possibly by activation of protein kinase C, and 2) an elevation of [Ca2+](i) serves as a trigger to enhance amylase release only during the initial phase of secretion.en_HK
dc.languageengen_US
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://ajpcon.physiology.org/en_HK
dc.relation.ispartofAmerican Journal of Physiology - Gastrointestinal and Liver Physiologyen_HK
dc.subjectChemicals And Cas Registry Numbersen_US
dc.titleCaerulein causes translocation of protein kinase C in rat acini without increasing cytosolic free Ca2+en_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.pmid2455450-
dc.identifier.scopuseid_2-s2.0-0023779836en_HK
dc.identifier.volume255en_HK
dc.identifier.issue1en_HK
dc.identifier.spage18/1en_HK
dc.identifier.epage18/1en_HK
dc.identifier.isiWOS:A1988P300000036-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK
dc.identifier.scopusauthoridRegazzi, R=7004590576en_HK
dc.identifier.scopusauthoridWollheim, CB=7103171309en_HK

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