title: [Activation mechanisms, biological role and inhibitors of metalloproteases in the extracellular matrix].
abstract: 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.
authors.affiliation: Klinika Chirurgii Naczyń i Transplantacji Akademii Medycznej w Białymstoku.
authors.forename: M
authors.initials: M
authors.lastname: Gacko
mesh_terms: 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
chemical_list: D019715:Tissue Inhibitor of Metalloproteinase-1; D012697:Serine Endopeptidases; D013381:Subtilisins; D019272:Leukocyte Elastase; D045683:Furin; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3