[HTML][HTML] Collagen XVII is destabilized by a glycine substitution mutation in the cell adhesion domain Col15
K Tasanen, JA Eble, M Aumailley, H Schumann… - Journal of Biological …, 2000 - ASBMB
Collagen XVII is a hemidesmosomal transmembrane molecule important for epithelial
adhesion in the skin. It exists in two forms, as a full-length protein and as a soluble
ectodomain that is shed from the keratinocyte surface by furin-mediated proteolysis. To
obtain information on the conformation and the functions of this unusual collagen, its largest
collagenous domain, Col15, was expressed in a eukaryotic episomal expression system
and purified by DEAE and fast protein liquid-Mono S chromatography. The protein was triple …
adhesion in the skin. It exists in two forms, as a full-length protein and as a soluble
ectodomain that is shed from the keratinocyte surface by furin-mediated proteolysis. To
obtain information on the conformation and the functions of this unusual collagen, its largest
collagenous domain, Col15, was expressed in a eukaryotic episomal expression system
and purified by DEAE and fast protein liquid-Mono S chromatography. The protein was triple …