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ACS Chem Biol. 2011 Jun 17;6(6):563-72. doi: 10.1021/cb100392r. Epub 2011 Feb 28.

Development of activity-based probes for cathepsin X.

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1
Department of Pathology, Stanford University School of Medicine, 300 Pasteur Dr., Stanford, CA 94305-5324, United States.

Abstract

Cathepsin X is a lysosomal cysteine protease that functions as a carboxypeptidase with broad substrate specificity. Cathepsin X was discovered only recently, and its physiological roles are still not well understood. A number of studies suggest that cathepsin X may be involved in a variety of biological processes, including cancer, aging and degenerative conditions of the brain, inflammation, and cellular communication. Here we present the synthesis and characterization of several activity-based probes (ABPs) that target active cathepsin X. These ABPs were used to label cathepsin X in complex lysates, whole cells, and in vivo. Furthermore, we have developed a method for selectively labeling and visualizing active cathepsin X in vitro and in vivo. Overall, the probes developed in this study are valuable tools for the study of cathepsin X function.

PMID:
21322635
PMCID:
PMC3117957
DOI:
10.1021/cb100392r
[Indexed for MEDLINE]
Free PMC Article
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