N-terminomics/proteomics investigation of Calpain-2 substrates
Date
2022-04-21
Authors
Journal Title
Journal ISSN
Volume Title
Publisher
Abstract
Calpains 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.
Description
Keywords
proteases proteomics
Citation
Anowai, A. (2022). N-terminomics/proteomics investigation of Calpain-2 substrates (Master's thesis, University of Calgary, Calgary, Canada). Retrieved from https://prism.ucalgary.ca.