Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs

Collagen XVII, a type II transmembrane protein and epithelial adhesion molecule, can be proteolytically shed from the cell surface to generate a soluble collagen. Here we investigated the release of the ectodomain and identified the enzymes involved. After surface biotinylation of keratinocytes, the...

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Veröffentlicht in:	The EMBO journal 2002-10, Vol.21 (19), p.5026-5035
Hauptverfasser:	Franzke, Claus-Werner, Tasanen, Kaisa, Schäcke, Heike, Zhou, Zhongjun, Tryggvason, Karl, Mauch, Cornelia, Zigrino, Paola, Sunnarborg, Susan, Lee, David C., Fahrenholz, Falk, Bruckner-Tuderman, Leena
Format:	Artikel
Sprache:	eng
Schlagworte:	Adhesion Antibody Specificity Autoantigens - chemistry Autoantigens - immunology Autoantigens - physiology Base Sequence basement membrane Biotinylation Carrier Proteins Cell Adhesion Molecules - physiology Cell Membrane - physiology Cells, Cultured Collagen - chemistry Collagen - immunology Collagen - physiology Collagen Type XVII Cytoskeletal Proteins DNA Primers Dystonin EMBO05 Endopeptidases - metabolism Esters hemidesmosome Humans Keratinocytes - physiology Matrix Metalloproteinase Inhibitors Matrix Metalloproteinases - metabolism metalloprotease Nerve Tissue Proteins Non-Fibrillar Collagens Protease Inhibitors - pharmacology Recombinant Proteins - metabolism secretase skin Tissue Inhibitor of Metalloproteinase-2 - pharmacology Tissue Inhibitor of Metalloproteinase-3 - pharmacology Transfection
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