The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs

The ADAM family of proteases are type I transmembrane proteins with both metalloproteinase and disintegrin containing extracellular domains. ADAMs are implicated in the proteolytic processing of membrane-bound precursors and involved in modulating cell–cell and cell–matrix interactions. ADAM8 (MS2,...

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Veröffentlicht in:	FEBS letters 2002-07, Vol.524 (1), p.154-158
Hauptverfasser:	Amour, Augustin, Knight, C.Graham, English, William R, Webster, Ailsa, Slocombe, Patrick M, Knäuper, Vera, Docherty, Andrew J.P, Becherer, J.David, Blobel, Carl P, Murphy, Gillian
Format:	Artikel
Sprache:	eng
Schlagworte:	ADAM ADAM Proteins Amino Acid Sequence Antigens, CD Antigens, Surface - genetics Antigens, Surface - isolation & purification Antigens, Surface - metabolism Catalysis Chromatography, Affinity Disintegrin metalloproteinase Disintegrins - metabolism Electrophoresis, Polyacrylamide Gel HB-EGF, heparin binding epidermal growth factor HPLC, high performance liquid chromatography K i, inhibition constant MBP, myelin basic protein Membrane Proteins Membrane-type metalloproteinase Metalloendopeptidases - antagonists & inhibitors Metalloendopeptidases - genetics Metalloendopeptidases - isolation & purification Metalloendopeptidases - metabolism Metalloproteinase MMP, matrix metalloproteinase Molecular Sequence Data NS0, non-secreter zero Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism SDS–PAGE, sodium dodecyl sulphate–polyacrylamide gel electrophoresis TACE, tumour necrosis factor-α converting enzyme TFA, trifluoroacetic acid TIMP, tissue inhibitor of metalloproteinases Tissue inhibitor of metalloproteinases Tissue Inhibitor of Metalloproteinases - metabolism
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