Activation of TIMP-2/progelatinase A complex by stromelysin.
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.
Miyazaki
K
K
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Japan.
Umenishi
F
F
Funahashi
K
K
Koshikawa
N
N
Yasumitsu
H
H
Umeda
M
M
D002460:Cell Line; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000302:isolation & purification / Q000378:metabolism*; D018093:Gelatinases; D005910:Glioma; D006801:Humans; D007700:Kinetics; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000494:pharmacology*; D009363:Neoplasm Proteins / Q000302:isolation & purification / Q000378:metabolism*; D010434:Pepsin A / Q000302:isolation & purification / Q000378:metabolism*; D010662:Phenylmercuric Acetate / Q000031:analogs & derivatives / Q000494:pharmacology; D011485:Protein Binding; D019716:Tissue Inhibitor of Metalloproteinase-2
D004792:Enzyme Precursors; D009363:Neoplasm Proteins; D019716:Tissue Inhibitor of Metalloproteinase-2; C010024:4-aminophenylmercuriacetate; D010434:Pepsin A; D018093:Gelatinases; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D010662:Phenylmercuric Acetate