Portal de Periódicos da CAPES

Development of Activity-Based Probes for Cathepsin X

2011; American Chemical Society; Volume: 6; Issue: 6 Linguagem: Inglês

10.1021/cb100392r

1554-8937

Margot G. Paulick, Matthew Bogyo,

Blood Coagulation and Thrombosis Mechanisms

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.