N-terminomics/proteomics investigation of Calpain-2 substrates

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dc.contributor.advisorDufour, Antoine
dc.contributor.authorAnowai, Anthonia
dc.contributor.committeememberHollenberg, Morley
dc.contributor.committeememberRobbins, Stephen
dc.date2022-06
dc.date.accessioned2022-04-26T20:32:20Z
dc.date.available2022-04-26T20:32:20Z
dc.date.issued2022-04-21
dc.description.abstractCalpains are a family of intracellular cysteine proteases that require calcium for activation. Calpain-1 and -2, first described as the classical calpains due to their ubiquitous expression, are part of this larger 15-member family in humans and share similar patterns of expression and structural domains. Despite suggestive indication of a role for calpains in different cell functions in disease and health, it is unclear the repertoire of substrates that are targeted by calpains 1 and 2 in macrophages. To investigate this hypothesis, we focused on calpain-2 and performed N-terminomics/TAILS experiment in calpain-2 knockout human THP-1 monocytic cell lines to identify new substrates. We analyzed the proteomics and Nterminomics data using bioinformatics and pathway enrichment tools (STRING-db (https://string-db.org) and Metascape (https://metascape.org/gp/index.html)). We validated proteolytically processed substrates of calpain-2. We have shown that calpain-2 has novel targets spleen tyrosine kinase (SYK) in THP-1 cells when activated by calcium and may play a role in regulating kinase.en_US
dc.identifier.citationAnowai, A. (2022). N-terminomics/proteomics investigation of Calpain-2 substrates (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca.en_US
dc.identifier.doihttp://dx.doi.org/10.11575/PRISM/39702
dc.identifier.urihttp://hdl.handle.net/1880/114581
dc.language.isoengen_US
dc.publisher.facultyScienceen_US
dc.publisher.institutionUniversity of Calgaryen
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.en_US
dc.subjectproteases proteomicsen_US
dc.subject.classificationBiologyen_US
dc.subject.classificationBiology--Molecularen_US
dc.subject.classificationBiochemistryen_US
dc.titleN-terminomics/proteomics investigation of Calpain-2 substratesen_US
dc.typemaster thesisen_US
thesis.degree.disciplineMedicine – Biochemistry and Molecular Biologyen_US
thesis.degree.grantorUniversity of Calgaryen_US
thesis.degree.nameMaster of Science (MSc)en_US
ucalgary.item.requestcopytrueen_US
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