[Activation mechanisms, biological role and inhibitors of metalloproteases in the extracellular matrix].
Prometalloproteinases are activated by serine proteases, MMP-3, leucocytic elastase, furin, furin-like proteases and by membrane-type metalloproteinases as well. They form complexes with some proMMPs and thus they modify their activation.
Gacko
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Klinika Chirurgii Naczyń i Transplantacji Akademii Medycznej w Białymstoku.
D000595:Amino Acid Sequence; D000818:Animals; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000378:metabolism*; D045683:Furin; D006801:Humans; D019272:Leukocyte Elastase / Q000378:metabolism; D019278:Matrix Metalloproteinase 3 / Q000378:metabolism; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors* / Q000502:physiology*; D008969:Molecular Sequence Data; D012697:Serine Endopeptidases / Q000378:metabolism; D013381:Subtilisins / Q000378:metabolism; D019715:Tissue Inhibitor of Metalloproteinase-1 / Q000235:genetics / Q000378:metabolism
D019715:Tissue Inhibitor of Metalloproteinase-1; D012697:Serine Endopeptidases; D013381:Subtilisins; D019272:Leukocyte Elastase; D045683:Furin; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3