Activation of TIMP-2/progelatinase a complex by stromelysin

doi:10.1016/0006-291X(92)91705-U

Biochemical and Biophysical Research Communications

Volume 185, Issue 3, 30 June 1992, Pages 852-859

https://doi.org/10.1016/0006-291X(92)91705-U Get rights and content

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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^☆: This work was supported by the Special Coordination Funds of the Science and Technology Agency of Japan.

³: Present address: Department of Human Genetics and Legal Medicine, Jichi Medical School, Kawachi, Tochigi 329-04, Japan.

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Activation of TIMP-2/progelatinase a complex by stromelysin☆

Abstract

Trend Genet

Biochem. Biophys. Res. Commun

Methods Enzymol

J. Biol. Chem

J. Biol. Chem

J. Biol. Chem

J. Biol. Chem

FASEB J

Cancer Res