REGULATION OF PROTEOLYSIS AT THE NEUTROPHIL-SUBSTRATE INTERFACE BY SECRETORY LEUKOPROTEASE INHIBITOR
REGULATION OF PROTEOLYSIS AT THE NEUTROPHIL-SUBSTRATE INTERFACE BY SECRETORY LEUKOPROTEASE INHIBITOR
复制标题
DOI：
10.1126/science.2371565
复制
发表时间：
1990-07-13
期刊：
影响因子：
56.9
通讯作者：
WEISS, SJ
中科院分区：
文献类型：
--
作者：
RICE, WG;WEISS, SJ
人中性粒细胞可以通过将破坏性过程定位于细胞-基质接触位点来启动细胞外基质大分子的快速降解。虽然血浆和血浆中含有多种蛋白酶抑制剂，但这些抑制剂并不能阻止中性粒细胞攻击纤维连接蛋白或弹性蛋白。然而，重组分泌性白细胞蛋白酶抑制剂，其结构独特的丝氨酸蛋白酶抑制剂，其天然对应物通常仅限于人类粘液分泌物，可以保护subjectile底物免受中性粒细胞的侵害。这种血管外蛋白酶抑制剂作为皮下蛋白水解的有效调节剂的鉴定可能导致一类新的抗炎治疗剂的开发。
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.