Matrix Metalloproteinase 8, Human (MMP8, MMP-8, CLG1, HNC, Neutrophil Collagenase, PMNL Collagenase, PMNL-CL)

The progelatinase A, a member of the matrix metalloproteinase (MMP) family, has been isolated from macrophages and fibroblasts. Gelatinase A hydrolyses several components of the extracellular matrix, e.g. the collagen types IV, V and XI and gelatin. Progelatinase A complexed via their C-terminal domain with TIMP-2 was isolated from culture media of different cell types. This complex shows both properties of its constituents: Like TIMP-2 it inhibits active matrix metalloproteinases and like gelatinase it shows proteolytic activity after activation with APMA (4-aminophenylmercury acetate). However, its proteolytic activity is less than 10% of that of gelatinase A not complexed with TIMP-2. In contrast to the other MMPs the progelatinase A cannot be activated by the serine proteinase trypsin. Until quite recently a potential natural activator that can transform latent progelatinase A into the active form was unknown. It was shown that the catalytic domain of the membrane type 2-matrix metalloproteinase activates progelatinase A as well as the progelatinase A / TIMP-2 complex, by cleaving the 72kD progelatinase A to yield 67kD gelatinase A, which is than transformed into 62kD gelatinase A. The 62kD form is about twice as active as the 67kD form towards the Dnp-pepitde (Masui et al.). No significant difference in activity was found between free and complexed gelatinase A forms\n\nSource: \nMatrix Metalloproteinase 8, purified from human neutrophil granulocytes.\n\nMolecular Weight: \n~40/42kD\n\nConcentration:\n>100mUnits/mg\n\nActivation:\nThe latent 58kD form can be activated by both p-chloromercuribenzoate PCMB (0.1mM) and trypsin (10ug/ml) at 25 degrees C for 20 min, but PCMB is substantially more effective. The latent 58kD form can also be activated using 2mM (final concentration) aminophenylmercuric acetate (APMA) or 1mM mersalylic acid for 60min. at 37 degrees C. Either activation method will result in the preparation having a comparable catalytic efficiency against a peptide or\ngelatin substrate.\n\nInhibitors:\nThe activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-1 (TIMP-1) and by chelators of divalent cations like EDTA or o-phenanthroline.\n\nStorage and Stability:\nAliquot to avoid repeated freezing and thawing and store at -70 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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