Recombinant Human CTRL protein

Supplementary info

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

Activity summary

The CTRL protein also known as chymotrypsin-like protease CTRL-1 functions primarily as a serine protease. It exhibits a catalytic domain typical of the Chymotrypsin family of serine proteases. With a mass of approximately 29 kDa CTRL is expressed prominently in pancreatic tissue but can also be found in other tissues at lower levels. It plays a role in protein degradation by cleaving at specific amino acid sites.

Biological function summary

The serine protease activity of CTRL contributes to the digestion process by breaking down protein chains into smaller peptides. It does not work alone but rather as part of a larger complex. This involvement makes it integral to maintaining protein homeostasis in the body. It's expressed in various cellular processes that require the precise breakdown of polypeptides emphasizing its importance in tissue maintenance and repair.

Pathways

CTRL is involved in the proteolytic pathway facilitating the breakdown of dietary proteins into absorbable units. It collaborates closely with other proteases such as trypsin that complement its function by targeting different peptide bonds. Additionally CTRL takes part in cellular metabolism pathways where it assists in processing proteins needed for cellular activities.

Associated diseases and disorders

Dysfunctional CTRL activity associates with digestive disorders such as pancreatitis. An imbalance in its activity can also contribute to the development of pancreatic insufficiencies. In these contexts CTRL interacts with proteins like elastase where altered activity levels can exacerbate tissue damage during inflammatory conditions. Understanding CTRL's precise role provides insights into potential therapeutic targets for managing certain pathologies.