Serpins are a superfamily of proteins with similar structures that were first identified for their protease inhibition activity and are found in all kingdoms of life. [1][2] The acronym serpin was originally coined because the first serpins to be identified act on chymotrypsin-like serine proteases (ser ine p rotease in hibitors). [3][4][5] They...

In COPD, the relationship between the neutrophil serine protease, neutrophil elastase, and its endogenous inhibitor, alpha-1-antitrypsin (AAT) is the best characterised. AAT belongs to a superfamily of serine protease inhibitors known as serpins.

2006年7月5日 · Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways.

The serpins are a family of proteins with a shared tertiary structure, whose members largely act as serine protease inhibitors, found in all forms of life, ranging from viruses, bacteria, and archaea to plants and animals. These proteins represent up to 2–10% of proteins in the human blood and are the third most common protein family.

2003年11月1日 · The superfamily of serine proteinase inhibitors (serpins) are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner.

2011年7月22日 · In this short review, I introduce the serpin structure and general mechanism of protease inhibition, and illustrate, using recent crystallographic and biochemical data on antithrombin (AT), how serpin activity can be modulated by cofactors.

any of a superfamily of inhibitors of serine endopeptidase (serine proteinase), found in plasma and tissues; all are similarly structured single-chain glycoproteins although each one acts specifically on particular endopeptidases.

2006年5月30日 · Serpins are a broadly distributed family of protease inhibitors that use a conformational change to inhibit target enzymes. They are central in controlling many important proteolytic cascades, including the mammalian coagulation pathways.

The serpins represent an ancient pathway now known to be present in all kingdoms and often regulating central pathways for clotting, immunity, and even cancer in man. Serpins have been present from the time of the dinosaurs and can represent a …

Serine proteases drive important physiological processes such as coagulation, fibrinolysis, inflammation and angiogenesis. These proteases are controlled by serine protease inhibitors (SERPINs) that neutralize their activity. Currently, over 1,500 SERPINs are known in nature, but only 37 SERPINs are found in humans.