THE EXTRACELLULAR-MATRIX PRODUCED BY BOVINE CORNEAL ENDOTHELIAL-CELLSCONTAINS PROGELATINASE-A

Progelatinase A is a matrix metalloproteinase involved in the turnover of extracellular matrix (ECM). We report that the ECM produced by bov ine corneal endothelial (BCE) cells contains progelatinase A free of t issue inhibitor of metalloproteinase (TIMP2). The matrix-bound progela tinase A can be activated by APMA to generate a 62 kDa and a 45 kDa sp ecies with enzymatic activity and is inhibited by TIMP2. The bound pro gelatinase 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.