Anti-SLPI antibody [31]

Supplementary info

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

Activity summary

Secretory leukocyte protease inhibitor (SLPI) also known as antileukoproteinase and neutrophil elastase inhibitor is a protein with a molecular mass of approximately 12 kDa. SLPI is found mainly in epithelial tissues and is expressed in locations such as the respiratory tract skin and cervix. Mechanically SLPI functions as a serine protease inhibitor binding to and neutralizing enzymes like neutrophil elastase cathepsin G and trypsin which helps to limit tissue damage during inflammation.

Biological function summary

SLPI serves as a protector of epithelial surfaces from proteolytic degradation and acts as an anti-inflammatory agent. It displays broad-spectrum antimicrobial properties providing protection against bacterial and viral infections. Although SLPI is not part of a complex itself its interactions with extracellular matrix proteins help modulate wound healing processes and maintain tissue integrity.

Pathways

SLPI participates in the innate immune response and inflammation regulation pathways. It interacts within pathways that involve the complement cascade and kallikrein-kinin system helping to regulate inflammation and modulate immune responses. During these processes SLPI is related to proteins such as alpha-1-antitrypsin in its role as a protease inhibitor contributing to the regulation of protease activity and inflammatory responses.

Associated diseases and disorders

SLPI is implicated in conditions such as chronic obstructive pulmonary disease (COPD) and cystic fibrosis where excessive protease activity leads to tissue damage. In these diseases SLPI shows a protective role against lung tissue degradation. SLPI is also associated with the progression of certain cancers like ovarian cancer where its overexpression may support tumor growth and metastasis. In these contexts SLPI relates to other protease inhibitors such as tissue inhibitors of metalloproteinases (TIMPs) due to their shared function in regulating protease activity and tissue remodeling.