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J Biol Chem, Vol. 275, Issue 5, 3093-3099, February 4, 2000
From the Departments of 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-helical (Tm of 26.5 °C) when produced
in cultures containing ascorbic acid. When the vitamin supply was
limited, the 4-hydroxyproline content was reduced from 74 to 9%,
which, in turn, resulted in a drastic reduction of the stability of the
triple helix. The glycine substitution mutation G627V associated with
junctional epidermolysis bullosa, a human blistering skin disease, also
had a striking effect on thermal stability of rCol15 causing partial unfolding already at 4 °C. Col15 promoted cell adhesion of
epithelial and fibroblastic cell lines with a
Collagen XVII Is Destabilized by a Glycine Substitution Mutation
in the Cell Adhesion Domain Col15*
§,
**,,,,§§
Dermatology and
¶ Physiological Chemistry, University of Münster, 48149 Münster, Germany, the Departments of § Dermatology and
Medical Biochemistry, University of Oulu,
90220 Oulu, Finland, and the Department of Biochemistry,
University of Cologne, 50931 Cologne, Germany
1 integrin-mediated
mechanism. In concert with this, in acquired autoimmune blistering skin
diseases, circulating IgG and IgA autoantibodies were found to target rCol15r.
*
This work was supported in part by grants from the Academy
of Finland, the Alexander von Humboldt Foundation, and the Oulu University Hospital (to K. T.), by Grants Br 1475/1-2 and SFB 293/B3
(to L. B.-T.) and Br 1497/1-2 (to P. B.) from the Deutsche Forschungsgemeinschaft as well as by EU Contract BM4CT-97-2062.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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