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Article: Caerulein and carbamoylcholine stimulate pancreatic amylase release at resting cytosolic free Ca2+

TitleCaerulein and carbamoylcholine stimulate pancreatic amylase release at resting cytosolic free Ca2+
Authors
KeywordsChemicals And Cas Registry Numbers
Issue Date1986
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1986, v. 235 n. 1, p. 139-143 How to Cite?
AbstractCytosolic free calcium concentrations ([Ca2+](i)) and amylase secretion were measured in isolated rat pancreatic acini loaded with the intracellularly trapped fluorescent indicator quin2. Both caerulein and carbamoylcholine caused a rapid increase in [Ca2+](i), with a maximal 3-fold increase at 10-9 M-caerulein and 10-4 M-carbamoylcholine. However, caerulein (10-12 M and 10-11 M) as well as carbamoylcholine (10-7 M) caused a significant stimulation of amylase release, while not inducing any detectable rise in [Ca2+](i). Changes in [Ca2+](i) after addition of either secretagogue were transient and did not last more than 2-3 min. By contrast, when amylase secretion was monitored as a function of time, two distinct secretory phases could be observed upon addition of either carbamoylcholine (10-5 M) or caerulein (10-10 M). An initial, rapid phase (0-5 min) which caused a 6-7-fold increase above basal, followed by a sustained (5-30 min), but less marked, secretory rate (2-3-fold above basal). Addition of atropine (10-4 M) 5 min after carbamoylcholine (10-5 M) (i.e. after termination of the rise in [Ca2+](i) and of the first secretory phase) did not cause any significant change in [Ca2+](i), while significantly inhibiting amylase secretion from 5 to 30 min to the same rate observed in the absence of the secretagogue. These results show that caerulein and carbamoylcholine, two agents thought to activate secretion mainly through mobilization of Ca2+ from intracellular stores, are capable of eliciting amylase secretion independently of a concomitant rise in [Ca2+](i). Furthermore, with both secretagogues the rise in [Ca2+](i), when observed, was only transient, while the stimulation of amylase release was sustained.
Persistent Identifierhttp://hdl.handle.net/10722/132679
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorBruzzone, Ren_HK
dc.contributor.authorPozzan, Ten_HK
dc.contributor.authorWollheim, CBen_HK
dc.date.accessioned2011-03-28T09:28:11Z-
dc.date.available2011-03-28T09:28:11Z-
dc.date.issued1986en_HK
dc.identifier.citationBiochemical Journal, 1986, v. 235 n. 1, p. 139-143en_HK
dc.identifier.issn0264-6021en_HK
dc.identifier.urihttp://hdl.handle.net/10722/132679-
dc.description.abstractCytosolic free calcium concentrations ([Ca2+](i)) and amylase secretion were measured in isolated rat pancreatic acini loaded with the intracellularly trapped fluorescent indicator quin2. Both caerulein and carbamoylcholine caused a rapid increase in [Ca2+](i), with a maximal 3-fold increase at 10-9 M-caerulein and 10-4 M-carbamoylcholine. However, caerulein (10-12 M and 10-11 M) as well as carbamoylcholine (10-7 M) caused a significant stimulation of amylase release, while not inducing any detectable rise in [Ca2+](i). Changes in [Ca2+](i) after addition of either secretagogue were transient and did not last more than 2-3 min. By contrast, when amylase secretion was monitored as a function of time, two distinct secretory phases could be observed upon addition of either carbamoylcholine (10-5 M) or caerulein (10-10 M). An initial, rapid phase (0-5 min) which caused a 6-7-fold increase above basal, followed by a sustained (5-30 min), but less marked, secretory rate (2-3-fold above basal). Addition of atropine (10-4 M) 5 min after carbamoylcholine (10-5 M) (i.e. after termination of the rise in [Ca2+](i) and of the first secretory phase) did not cause any significant change in [Ca2+](i), while significantly inhibiting amylase secretion from 5 to 30 min to the same rate observed in the absence of the secretagogue. These results show that caerulein and carbamoylcholine, two agents thought to activate secretion mainly through mobilization of Ca2+ from intracellular stores, are capable of eliciting amylase secretion independently of a concomitant rise in [Ca2+](i). Furthermore, with both secretagogues the rise in [Ca2+](i), when observed, was only transient, while the stimulation of amylase release was sustained.en_HK
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_HK
dc.relation.ispartofBiochemical Journalen_HK
dc.subjectChemicals And Cas Registry Numbersen_US
dc.titleCaerulein and carbamoylcholine stimulate pancreatic amylase release at resting 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.pmid2427070-
dc.identifier.scopuseid_2-s2.0-0022470430en_HK
dc.identifier.volume235en_HK
dc.identifier.issue1en_HK
dc.identifier.spage139en_HK
dc.identifier.epage143en_HK
dc.identifier.isiWOS:A1986A690100021-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridBruzzone, R=7006793327en_HK
dc.identifier.scopusauthoridPozzan, T=7102571129en_HK
dc.identifier.scopusauthoridWollheim, CB=7103171309en_HK

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