Journal article
N-Terminomics/TAILS Profiling of Macrophages after Chemical Inhibition of Legumain
BM Anderson, LGN De Almeida, H Sekhon, D Young, A Dufour, LE Edgington-Mitchell
Biochemistry | AMER CHEMICAL SOC | Published : 2020
Abstract
Legumain (asparaginyl endopeptidase) is the only protease with a preference for cleavage after asparagine residues. Increased legumain activity is a hallmark of inflammation, neurodegenerative diseases, and cancer, and legumain inhibitors have exhibited therapeutic effects in mouse models of these pathologies. Improved knowledge of its substrates and cellular functions is a requisite to further validation of legumain as a drug target. We, therefore, aimed to investigate the effects of legumain inhibition in macrophages using an unbiased and systematic approach. By shotgun proteomics, we identified 16 »094 unique peptides in RAW264.7 cells. Among these, 326 unique peptides were upregulated in..
View full abstractGrants
Awarded by University of Melbourne
Funding Acknowledgements
L.E.M. was supported by an Early Career Fellowship from the National Health and Medical Research Council of Australia (NHMRC, GNT1091636), a Grimwade Fellowship funded by the Russell and Mab Grimwade Miegunyah Fund at the University of Melbourne, a DECRA Fellowship from the Australian Research Council (ARC, DE180100418), and a Priority-Driven Collaborative Cancer Research Young Investigator Award from Cure Cancer and Cancer Australia (GNT1157171). A.D. was supported by an NSERC Discovery Grant (DGECR-2019-00112).