Activation of TIMP-2/progelatinase A complex by stromelysin

K Miyazaki; F Umenishi; K Funahashi; N Koshikawa; H Yasumitsu; M Umeda

doi:10.1016/0006-291x(92)91705-u

Activation of TIMP-2/progelatinase A complex by stromelysin

Biochem Biophys Res Commun. 1992 Jun 30;185(3):852-9. doi: 10.1016/0006-291x(92)91705-u.

Authors

K Miyazaki¹, F Umenishi, K Funahashi, N Koshikawa, H Yasumitsu, M Umeda

Affiliation

¹ Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan.

PMID: 1320876
DOI: 10.1016/0006-291x(92)91705-u

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cell Line
Chromatography, Affinity
Chromatography, Gel
Enzyme Activation
Enzyme Precursors / isolation & purification
Enzyme Precursors / metabolism*
Gelatinases
Glioma
Humans
Kinetics
Matrix Metalloproteinase 3
Metalloendopeptidases / pharmacology*
Neoplasm Proteins / isolation & purification
Neoplasm Proteins / metabolism*
Pepsin A / isolation & purification
Pepsin A / metabolism*
Phenylmercuric Acetate / analogs & derivatives
Phenylmercuric Acetate / pharmacology
Protein Binding
Tissue Inhibitor of Metalloproteinase-2

Substances

Enzyme Precursors
Neoplasm Proteins
Tissue Inhibitor of Metalloproteinase-2
4-aminophenylmercuriacetate
Pepsin A
Gelatinases
Metalloendopeptidases
Matrix Metalloproteinase 3
Phenylmercuric Acetate