Cathepsin T

Cathepsin T

Crystal structure of Cathepsin T.

Cathepsin T is a member of the cathepsin family of proteases, which are enzymes involved in the degradation of proteins within cells. It is encoded by the CTST gene and is primarily found in lysosomes, the cellular compartments responsible for the breakdown of various biomolecules.

Structure

The crystal structure of Cathepsin T has been determined, revealing its three-dimensional arrangement. It consists of two major domains: the N-terminal propeptide domain and the catalytic domain. The propeptide domain is responsible for the regulation of enzyme activity, while the catalytic domain contains the active site where protein degradation occurs.

Function

Cathepsin T plays a crucial role in the degradation of extracellular matrix proteins, such as collagen and elastin. It is involved in tissue remodeling processes, including bone resorption and wound healing. Additionally, it has been implicated in the regulation of immune responses and antigen presentation.

Clinical Significance

Abnormalities in Cathepsin T expression or activity have been associated with various diseases. For example, increased Cathepsin T levels have been observed in certain types of cancer, suggesting its involvement in tumor progression and metastasis. Inhibition of Cathepsin T activity has also shown potential as a therapeutic strategy for conditions such as osteoporosis and rheumatoid arthritis.

See Also

• Cathepsin
• Protease
• Lysosome
• Extracellular matrix
• Tissue remodeling
• Bone resorption
• Wound healing
• Immune response
• Antigen presentation
• Osteoporosis
• Rheumatoid arthritis