Activation of TIMP-2/progelatinase A complex by stromelysin. |
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Authors: | K Miyazaki F Umenishi K Funahashi N Koshikawa H Yasumitsu M Umeda |
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Institution: | Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan. |
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Abstract: | Progelatinase A was purified as a complex with TIMP-2 from the conditioned medium of a human glioblastoma cell line. The TIMP-2/progelatinase complex was resistant to the activation by p-aminophenylmercuric acetic acid (APMA), and showed less than 10% of the activity of the TIMP-2-free active enzyme. When the complex was incubated with stromelysin in the presence of APMA, the 64-kDa progelatinase was effectively converted to the 57-kDa mature enzyme, increasing its gelatinolytic activity about 8-fold. These results suggest that stromelysin is a natural activator of TIMP-2-bound progelatinase A. |
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