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J. Biol. Chem., Vol. 277, Issue 29, 26372-26378, July 19, 2002
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From the Collagen VII is the major structural component of
the anchoring fibrils at the dermal-epidermal junction in the skin. It
is secreted by keratinocytes as a precursor, procollagen VII, and processed into mature collagen during polymerization of the anchoring fibrils. We show that bone morphogenetic protein-1 (BMP-1), which exhibits procollagen C-proteinase activity, cleaves the C-terminal propeptide from human procollagen VII. The cleavage occurs at the BMP-1
consensus cleavage site SYAA
Proteinases of the Bone Morphogenetic Protein-1 Family Convert
Procollagen VII to Mature Anchoring Fibril Collagen*
,
,,,§§
Department of Dermatology, University of
Münster, 48149 Münster, Germany, the
§ Departments of Pathology and Laboratory Medicine and
Biomolecular Chemistry, University of Wisconsin,
Madison, Wisconsin 53706, ¶ Cutaneous Biology Research Center,
Massachusetts General Hospital/Harvard Medical School,
Charlestown, Massachusetts 02129, Shriners Hospital for
Children, Portland, Oregon 97201, ** Wellcome Trust
Centre for Cell-Matrix Research, School of Biological Sciences,
University of Manchester, Manchester M139PT, United Kingdom, and
Max-Planck-Institute for Biochemistry,
82152 Martinsried, Germany
DTAG within the NC-2 domain. Mammalian tolloid-like (mTLL)-1 and -2, two other proteases of the
astacin enzyme family, were able to process procollagen VII at the same
site in vitro. Immunohistochemical and genetic evidence supported the involvement of these enzymes in cleaving type VII procollagen in vivo. Both BMP-1 and mTLL-1 are expressed in
the skin and in cultured cutaneous cells. A naturally occurring
deletion in the human COL7A1 gene, 8523del14, which is
associated with dystrophic epidermolysis bullosa and eliminates the
BMP-1 consensus sequence, abolished processing of procollagen VII, and
in mutant skin procollagen VII accumulated at the dermal-epidermal
junction. On the other hand, deficiency of BMP-1 in the skin of
knockout mouse embryos did not prevent processing of procollagen VII to mature collagen, suggesting that mTLL-1 and/or mTLL-2 can substitute for BMP-1 in the processing of procollagen VII in
situ.
*
This work was supported in part by the German Research
Council, DFG, Grant SFB 492-A3, the Interdisciplinary Center for
Clinical Research, University of Münster, Grant IZKF D-17 (to
L. B.-T.), and by National Institutes of Health Grants AR47746 and
GM63471 (to D. S. G.).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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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