Domain interactions in the gelatinase A.TIMP-2.MT1-MMP activation complex. The ectodomain of the 44-kDa form of membrane type-1 matrix metalloproteinase does not modulate gelatinase A activation

On the cell surface, the 59-kDa membrane type 1-matrix metalloproteinase (MT1-MMP) activates the 72-kDa progelatinase A (MMP-2) after binding the tissue inhibitor of metalloproteinases (TIMP)-2. A 44-kDa remnant of MT1-MMP, with an N terminus at Gly(285), is also present on the cell after autolytic...

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Veröffentlicht in:	The Journal of biological chemistry 2000-12, Vol.275 (50), p.39497
Hauptverfasser:	Overall, C M, Tam, E, McQuibban, G A, Morrison, C, Wallon, U M, Bigg, H F, King, A E, Roberts, C R
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Cell Membrane - metabolism Cells, Cultured Chromatography Concanavalin A - pharmacology Dose-Response Relationship, Drug Electrophoresis, Polyacrylamide Gel Enzyme Activation Epitopes Glycine - chemistry Immunohistochemistry Kinetics Matrix Metalloproteinase 2 - chemistry Matrix Metalloproteinase 2 - metabolism Matrix Metalloproteinases, Membrane-Associated Metalloendopeptidases - chemistry Metalloendopeptidases - metabolism Metalloendopeptidases - physiology Protein Binding Protein Isoforms Protein Structure, Tertiary Rats Receptors, Peptide - chemistry Recombinant Proteins - metabolism Reverse Transcriptase Polymerase Chain Reaction Tissue Inhibitor of Metalloproteinase-2 - chemistry Tumor Cells, Cultured Two-Hybrid System Techniques
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