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dc.contributor.advisorLytton, Jonathan
dc.contributor.authorTorry, Lisa
dc.date.accessioned2012-10-01T18:41:52Z
dc.date.available2012-11-13T08:01:44Z
dc.date.issued2012-10-01
dc.date.submitted2012en
dc.identifier.citationTorry, L. (2012). Alternative splicing of NCX1 affects the sensitivity of its Ca2+ sensors (Unpublished master's thesis). University of Calgary, Calgary, AB. doi:10.11575/PRISM/24780en_US
dc.identifier.urihttp://hdl.handle.net/11023/254
dc.description.abstractThe Na+/Ca2+ exchanger, NCX1, is important for Ca2+ homeostasis in many different tissues. Exchange function is regulated by Ca2+ binding to two cytoplasmic domains, CBD1 and CBD2, that are subject to tissue-specific alternative splicing. To test if alternative splicing modulates Ca2+ binding to the CBDs, the isolated domains CBD1, CBD2, and the tandem construct CBD12 from different NCX1 spliced isoforms were produced, purified and analyzed for Ca2+ binding in a competition binding assay using fluorescent Ca2+ indicators. NCX1.4-CBD2 bound two Ca2+ ions while NCX1.3-CBD2 did not bind Ca2+. CBD1 bound four Ca2+ ions, and some of the CBD1 Ca2+ binding sites in the CBD12 tandem construct had isoform-specific affinities significantly higher than CBD1 alone. My results confirm that alternative splicing of NCX1 affects regulatory Ca2+ binding in both CBDs, and thus tailors NCX1 function to suit tissue-specific requirements for Ca2+ homeostasis.en_US
dc.language.isoeng
dc.rightsUniversity of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.
dc.subjectBiology--Molecular
dc.subjectChemistry--Analytical
dc.subjectBiochemistry
dc.subject.classificationNCX1en_US
dc.subject.classificationalternative splicingen_US
dc.subject.classificationCa2+ binding domainsen_US
dc.titleAlternative splicing of NCX1 affects the sensitivity of its Ca2+ sensors
dc.typemaster thesis
dc.publisher.facultyGraduate Studies
dc.publisher.institutionUniversity of Calgaryen
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/24780
thesis.degree.nameMaster of Science
thesis.degree.nameMS
thesis.degree.nameMSc
thesis.degree.disciplineBiochemistry and Molecular Biology
thesis.degree.grantorUniversity of Calgary
atmire.migration.oldid423
dc.publisher.placeCalgaryen


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