Alternative splicing of NCX1 affects the sensitivity of its Ca2+ sensors
atmire.migration.oldid | 423 | |
dc.contributor.advisor | Lytton, Jonathan | |
dc.contributor.author | Torry, Lisa | |
dc.date.accessioned | 2012-10-01T18:41:52Z | |
dc.date.available | 2012-11-13T08:01:44Z | |
dc.date.issued | 2012-10-01 | |
dc.date.submitted | 2012 | en |
dc.description.abstract | The 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.identifier.citation | Torry, L. (2012). Alternative splicing of NCX1 affects the sensitivity of its Ca2+ sensors (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca. doi:10.11575/PRISM/24780 | en_US |
dc.identifier.doi | http://dx.doi.org/10.11575/PRISM/24780 | |
dc.identifier.uri | http://hdl.handle.net/11023/254 | |
dc.language.iso | eng | |
dc.publisher.faculty | Graduate Studies | |
dc.publisher.institution | University of Calgary | en |
dc.publisher.place | Calgary | en |
dc.rights | University 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.subject | Biology--Molecular | |
dc.subject | Chemistry--Analytical | |
dc.subject | Biochemistry | |
dc.subject.classification | NCX1 | en_US |
dc.subject.classification | alternative splicing | en_US |
dc.subject.classification | Ca2+ binding domains | en_US |
dc.title | Alternative splicing of NCX1 affects the sensitivity of its Ca2+ sensors | |
dc.type | master thesis | |
thesis.degree.discipline | Biochemistry and Molecular Biology | |
thesis.degree.grantor | University of Calgary | |
thesis.degree.name | Master of Science (MSc) | |
ucalgary.item.requestcopy | true |