The extracellular matrix produced by bovine corneal endothelial cells contains progelatinase A

FEBS Letters

Vlodavsky, Israel³  Ishai-Michaeli, Rivka³  Legrand, Yves²  Fridman, Rafael¹  Menashi, Suzanne² 

[1] Department of Pathology, Wayne State University, Detroit, MI 48201, USA;Unité 353 INSERM, Hospital Saint Louis, 1 Ave Claude Vellefaux, 75010 Paris, France;Department of Oncology, Hadassah Hebrew University Hospital, Jerusalem 91120, Israel

关键词: Matrix metalloproteinase;    Extracellular matrix;    Gelatinase;    Corneal endothelial cell;    Protease;   

DOI  :  10.1016/0014-5793(95)00125-S

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Progelatinase A is a matrix metalloproteinase involved in the turnover of extracellular matrix (ECM). We report that the ECM produced by bovine corneal endothelial (BCE) cells contains progelatinase A free of tissue inhibitor of metalloproteinase (TIMP2). The matrix-bound progelatinase A can be activated by APMA to generate a 62 kDa and a 45 kDa species with enzymatic activity and is inhibited by TIMP2. The bound progelatinase can be released after treatment of the ECM with gelatinase B. These studies suggest that the ECM can function as a reservoir for progelatinase A which may be readily available for cells in processes such as metastasis, angiogenesis, inflammation and wound healing.

【 授权许可】

Unknown