Anti-Cathepsin C antibody

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Cathepsin C also known as dipeptidyl peptidase I is a lysosomal cysteine protease with a molecular mass of approximately 51 kDa. It functions mechanically by cleaving off dipeptides from the N-terminal end of proteins and peptides. Cathepsin C is widely expressed in various tissues with higher levels in immune cells like neutrophils and macrophages. This enzyme activates serine proteases from their inactive zymogen forms which is important for immune responses.

Biological function summary

The enzyme contributes significantly to the immune system. It forms part of a multi-enzyme complex that processes proenzymes such as granzymes and cathepsin G into their active forms. Through these actions Cathepsin C regulates cellular activities linked to inflammation and apoptosis. The proteolytic activity it provides is critical for the functioning of immune-related cells facilitating defense mechanisms against pathogens.

Pathways

Cathepsin C plays roles in the inflammatory and immune response pathways. It connects to the granzyme and lysosomal pathways important in processing and regulating granzyme activities critical for cytotoxic T lymphocyte functions. Cathepsin C maintains connections with proteins like granzymes and cathepsin G each involved in mediating immune responses and cellular death.

Associated diseases and disorders

Cathepsin C is associated with conditions such as Papillon-Lefèvre Syndrome and aggressive periodontitis. These disorders arise due to disruptions in immune protection resulting from mutations in the Cathepsin C gene. The enzyme's abnormal activity in these diseases highlights its connection with proteins such as neutrophil elastase which play critical roles in tissue degradation processes leading to periodontal disease.