MATRILYSIN IS MUCH MORE EFFICIENT THAN OTHER MATRIX METALLOPROTEINASES IN THE PROTEOLYTIC INACTIVATION OF ALPHA(1)-ANTITRYPSIN
MATRILYSIN IS MUCH MORE EFFICIENT THAN OTHER MATRIX METALLOPROTEINASES IN THE PROTEOLYTIC INACTIVATION OF ALPHA(1)-ANTITRYPSIN
复制标题
DOI：
10.1006/bbrc.1994.2503
复制
发表时间：
1994-10-28
影响因子：
3.1
通讯作者：
SENIOR, RM
中科院分区：
文献类型：
--
作者：
SIRES, UI;MURPHY, G;SENIOR, RM
α（1）-抗胰蛋白酶是人白细胞弹性蛋白酶的主要生理抑制剂，它被几种基质金属蛋白酶（包括间质胶原酶、基质溶解素和92 kDa明胶酶）蛋白水解灭活。在这份报告中，我们描述了催化作用的基质溶解素，最近发现的金属蛋白酶，α（1）-抗胰蛋白酶。发现基质溶素比92 kDa明胶酶有效约30倍，比胶原酶有效约70倍，比基质溶素有效约180倍。基质溶解素切割α（1）-抗胰蛋白酶产生两个约50 kDa和4 kDa的片段。在α（1）-抗胰蛋白酶活性位点环上的Phe（352）·Leu（353）肽键处发生单断裂。这些结果表明，除了其对细胞外基质的活性外，基质溶解素通过其降解α（1）-AT的能力提供了调节白细胞弹性蛋白酶活性的机制。(C)1994年出版社出版。
alpha(1)-antitrypsin, the primary physiologic inhibitor of human leukocyte elastase, is proteolytically inactivated by several matrix metalloproteinases including interstitial collagenase, stromelysin and 92 kDa gelatinase. In this report, we describe the catalytic effects of matrilysin, a recently identified metalloproteinase, upon alpha(1)-antitrypsin. Matrilysin was found to be approximately 30-fold more effective than 92 kDa gelatinase, 70-fold more effective than collagenase, and 180-fold more effective than stromelysin. Cleavage of alpha(1)-antitrypsin by matrilysin produced two fragments of approximately 50 kDa and 4 kDa. The single cleavage occurred at the Phe(352).Leu(353) peptide bond, a locus within alpha(1)-antitrypsin's active-site loop. These results suggest that apart from its activity against extracellular matrix, matrilysin provides a mechanism for the regulation of leukocyte elastase activity through its capacity to degrade alpha(1)-AT. (C) 1994 Academic Press, Inc.