Neutrophil elastase

Neutrophil elastase is an enzyme that is part of the serine protease family. It is primarily produced by neutrophils, a type of white blood cell, and plays a crucial role in the immune response.

Function

Neutrophil elastase is involved in the destruction of bacteria and other pathogens. It does this by breaking down the proteins in the cell walls of the pathogens, leading to their destruction. In addition to its role in the immune response, neutrophil elastase is also involved in tissue remodeling and inflammation.

Structure

Neutrophil elastase is a single chain polypeptide composed of 218 amino acids. It has two domains: a small N-terminal domain and a large C-terminal domain. The active site of the enzyme is located in the C-terminal domain.

Clinical significance

Abnormalities in the function or regulation of neutrophil elastase can lead to a variety of diseases. For example, excessive activity of this enzyme can lead to tissue damage and inflammation, as seen in conditions such as chronic obstructive pulmonary disease (COPD) and cystic fibrosis. On the other hand, deficiencies in neutrophil elastase can result in immune deficiencies, making individuals more susceptible to infections.

Inhibitors

Several inhibitors of neutrophil elastase exist, both naturally in the body and as pharmaceutical agents. These inhibitors can help to regulate the activity of the enzyme and prevent tissue damage. Examples of these inhibitors include alpha-1 antitrypsin and elafin.

See also

• Protease
• Serine protease
• Neutrophil
• Alpha-1 antitrypsin
• Elafin

50px

This protease related article is a stub. You can help WikiMD by expanding it.