Abstract
Recombinant 72 kDa gelatinase A and a truncated form lacking the C-terminal domain were shown to be activated by organomercurials and to possess similar activities towards a number of substrates. The truncated proenzyme differed from the full-length gelatinase in that it could not be activated by a membrane activator and did not bind tissue inhibitor of metalloproteinase (TIMP)-2. Kinetic studies also showed that the inhibition of the activated truncated enzyme, by both TIMP-1 and TIMP-2, was considerably decreased compared with the full-length enzyme. We conclude that the C-terminal domain plays an important role in the regulation of gelatinase A by a potential physiological activator and inhibitors.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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Catalysis
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Cell Membrane / enzymology
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DNA / chemistry
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Enzyme Activation
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Gelatinases
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Glycoproteins / metabolism
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Glycoproteins / pharmacology
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Humans
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Kinetics
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Molecular Sequence Data
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Molecular Weight
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Mutagenesis
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Neoplasm Proteins / metabolism*
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Neoplasm Proteins / pharmacology
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Pepsin A / chemistry
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Pepsin A / genetics
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Pepsin A / metabolism*
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Peptide Fragments / metabolism*
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Structure-Activity Relationship
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Tissue Inhibitor of Metalloproteinase-2
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Tissue Inhibitor of Metalloproteinases
Substances
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Glycoproteins
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Neoplasm Proteins
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Peptide Fragments
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Tissue Inhibitor of Metalloproteinases
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Tissue Inhibitor of Metalloproteinase-2
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DNA
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Pepsin A
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Gelatinases