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The extracellular matrix produced by bovine corneal endothelial cells contains progelatinase A
Author(s) -
Menashi Suzanne,
Vlodavsky Israel,
Ishai-Michaeli Rivka,
Legrand Yves,
Fridman Rafael
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00125-s
Subject(s) - extracellular matrix , matrix metalloproteinase , chemistry , gelatinase , angiogenesis , microbiology and biotechnology , matrix (chemical analysis) , wound healing , biochemistry , biology , cancer research , immunology , chromatography
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.