Development of activity-based probes for cathepsin X

Area of Science:

• Biochemistry
• Molecular Biology
• Protease research

Background:

• Cathepsin X is a recently discovered lysosomal cysteine protease with carboxypeptidase activity.
• Its precise physiological roles remain largely unknown, but it is implicated in cancer, neurodegeneration, inflammation, and cell signaling.
• Understanding Cathepsin X function is crucial for investigating these diverse biological processes.

Purpose of the Study:

• To synthesize and characterize novel activity-based probes (ABPs) specifically targeting active Cathepsin X.
• To utilize these ABPs for labeling and visualizing Cathepsin X in various biological contexts.
• To provide essential tools for advancing the study of Cathepsin X's biological functions.

Main Methods:

• Synthesis and characterization of multiple activity-based probes (ABPs).
• Application of ABPs to label Cathepsin X in complex biological lysates.
• Utilized ABPs for labeling and visualization in whole cells and in vivo models.

Main Results:

• Successfully synthesized and validated several ABPs targeting active Cathepsin X.
• Demonstrated the ability of ABPs to label Cathepsin X in vitro, in whole cells, and in vivo.
• Developed a method for selective labeling and visualization of active Cathepsin X.

Conclusions:

• The developed ABPs are effective tools for studying Cathepsin X.
• These probes facilitate the investigation of Cathepsin X's role in various physiological and pathological processes.
• The study provides valuable reagents for future research on Cathepsin X function.