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dc.contributor.authorFogarty, Kevin E.
dc.contributor.authorKidd, Jackie F.
dc.contributor.authorTuft, Richard A.
dc.contributor.authorThorn, Peter
dc.date2022-08-11T08:09:44.000
dc.date.accessioned2022-08-23T16:41:30Z
dc.date.available2022-08-23T16:41:30Z
dc.date.issued2000-04-25
dc.date.submitted2008-04-14
dc.identifier.citationBiophys J. 2000 May;78(5):2298-306.
dc.identifier.issn0006-3495 (Print)
dc.identifier.doi10.1016/S0006-3495(00)76776-2
dc.identifier.pmid10777728
dc.identifier.urihttp://hdl.handle.net/20.500.14038/39897
dc.description.abstractInsP(3)-evoked elementary Ca(2+) release events have been postulated to play a role in providing the building blocks of larger Ca(2+) signals. In pancreatic acinar cells, low concentrations of acetylcholine or the injection of low concentrations of InsP(3) elicit a train of spatially localized Ca(2+) spikes. In this study we have quantified these responses and compared the Ca(2+) signals to the elementary events shown in Xenopus oocytes. The results demonstrate, at the same concentrations of InsP(3), Ca(2+) signals consisting of one population of small transient Ca(2+) release events and a second distinct population of larger Ca(2+) spikes. The signal mass amplitudes of both types of events are within the range of amplitudes for the elementary events in Xenopus oocytes. However, the bimodal Ca(2+) distribution of Ca(2+) responses we observe is not consistent with the continuum of event sizes seen in Xenopus. We conclude that the two types of InsP(3)-dependent events in acinar cells are both elementary Ca(2+) signals, which are independent of one another. Our data indicate a complexity to the organization of the Ca(2+) release apparatus in acinar cells, which might result from the presence of multiple InsP(3) receptor isoforms, and is likely to be important in the physiology of these cells.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=10777728&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC1300821/pdf/10777728.pdf
dc.subjectAnimals
dc.subjectBiophysics
dc.subjectCalcium Channels
dc.subjectCalcium Signaling
dc.subjectFemale
dc.subjectInositol 1,4,5-Trisphosphate
dc.subjectInositol 1,4,5-Trisphosphate Receptors
dc.subjectMale
dc.subjectMice
dc.subjectMicroscopy, Fluorescence
dc.subjectOocytes
dc.subjectPancreas
dc.subjectPatch-Clamp Techniques
dc.subjectProtein Isoforms
dc.subjectReceptors, Cytoplasmic and Nuclear
dc.subjectXenopus
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA bimodal pattern of InsP(3)-evoked elementary Ca(2+) signals in pancreatic acinar cells
dc.typeJournal Article
dc.source.journaltitleBiophysical journal
dc.source.volume78
dc.source.issue5
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/270
dc.identifier.contextkey489607
html.description.abstract<p>InsP(3)-evoked elementary Ca(2+) release events have been postulated to play a role in providing the building blocks of larger Ca(2+) signals. In pancreatic acinar cells, low concentrations of acetylcholine or the injection of low concentrations of InsP(3) elicit a train of spatially localized Ca(2+) spikes. In this study we have quantified these responses and compared the Ca(2+) signals to the elementary events shown in Xenopus oocytes. The results demonstrate, at the same concentrations of InsP(3), Ca(2+) signals consisting of one population of small transient Ca(2+) release events and a second distinct population of larger Ca(2+) spikes. The signal mass amplitudes of both types of events are within the range of amplitudes for the elementary events in Xenopus oocytes. However, the bimodal Ca(2+) distribution of Ca(2+) responses we observe is not consistent with the continuum of event sizes seen in Xenopus. We conclude that the two types of InsP(3)-dependent events in acinar cells are both elementary Ca(2+) signals, which are independent of one another. Our data indicate a complexity to the organization of the Ca(2+) release apparatus in acinar cells, which might result from the presence of multiple InsP(3) receptor isoforms, and is likely to be important in the physiology of these cells.</p>
dc.identifier.submissionpathoapubs/270
dc.contributor.departmentBiomedical Imaging Group
dc.source.pages2298-306


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