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© 1992 Oxford University Press

RESEARCH-ARTICLE

The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor

Angela M. Christiano1, Louise M. Rosenbaum3, Linda C. Chung-Honet1, M. Gabriela Parente1, David T. Woodley4, Te-Cheng Pan1, Rui Zhu Zhang2, Mon-Li Chu2, Robert E. Burgeson3 and Jouni Uitto1,2,*

1Departments of Dermatology, Jefferson Medical College, The Section of Molecular Dermatology, Jefferson Institute of Molecular Medicine, Thomas Jefferson University Philadelphia, PA 2Departments of Biochemistry and Molecular Biology, Jefferson Medical College, The Section of Molecular Dermatology, Jefferson Institute of Molecular Medicine, Thomas Jefferson University Philadelphia, PA 3Shriner's Hospital for Crippled Children, Oregon Health Science University Portland, OR 4Department of Dermatology, Stanford University School of Medicine Stanford, CA, USA

*To whom correspondence should be addressed at: Department of Dermatology, Thomas Jefferson University, 233 South 10th Street, Room 450, Philadelphia, PA 19107, USA

Received July 22, 1992; Revised August 27, 1992; Accepted August 27, 1992

Type VII collagen, the major component of anchoring fibrils, consists of a central collagenous triple-helical segment flanked by non-collagenous domains, NC-1 and NC-2. In this study, we examined the domain organization of human type VII collagen through analysis of deduced amino acid sequences derived from cloned complementary and genomic DNAs, as compared to peptide segments derived from amniotic membrane type VII collagen. The results revealed that the peptide segments derived from the NC-1 domain of type VII collagen could be assigned to the 5' portion of the composite cDNA, indicating that NC-1 resides at the amino terminal end of the molecule. Several sub-domains with homology to adhesive molecules were also identified within NC-1. These protein domains may confer adhesive properties to NC-1, thereby facilitating the binding of type VII collagen to the lamina densa in the cutaneous basement membrane and the anchoring plaques within the dermis.


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