Regulation of Proteolysis at the Neutrophil-Substrate Interface by Secretory Leukoprotease Inhibitor

作者：William Gorham Rice, Stephen J. Weiss · 发表于：Science · 年份：1990 · DOI：10.1126/science.2371565 · 被引用次数：165 · 研究领域：Protease and Inhibitor Mechanisms、Cell Adhesion Molecules Research、Blood Coagulation and Thrombosis Mechanisms

Human neutrophils can initiate the rapid degradation of extracellular matrix macromolecules by localizing the destructive process to sites of cell-substrate contact. Although plasma and its filtrates contain multiple proteinase inhibitors, these inhibitors did not prevent neutrophils from attacking either underlying fibronectin or elastin. However, subjacent substrates could be protected from neutrophils by recombinant secretory leukoprotease inhibitor, a structurally unique serine proteinase inhibitor whose natural counterpart is normally confined to human mucous secretions. The identification of this extravascular proteinase inhibitor as a potent regulator of subjacent proteolysis could lead to the development of a new class of anti-inflammatory therapeutics.