4-aminophenylmercuriacetate and Glioma

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.

Topics: Cell Line; Chromatography, Affinity; Chromatography, Gel; Enzyme Activation; Enzyme Precursors; Gelatinases; Glioma; Humans; Kinetics; Matrix Metalloproteinase 3; Metalloendopeptidases; Neoplasm Proteins; Pepsin A; Phenylmercuric Acetate; Protein Binding; Tissue Inhibitor of Metalloproteinase-2