Document Type
Article
Publication Date
8-24-2006
Abstract
Anchoring functions of collagen VII depend on its ability to form homotypic fibrils and to bind to other macromolecules to form heterotypic complexes. Biosensor-based binding assays were employed to analyze the kinetics of the NC1 domain-mediated binding of collagen VII to laminin 5, collagen IV, and collagen I. We showed that collagen VII interacts with laminin 5 and collagen IV with Kd values of 10-9 M. In contrast, the NC1-mediated binding to collagen I was weak with a Kd value of 10-6 M. Binding assays also showed that the NC1 domain utilizes the same region to bind to both laminin 5 and collagen IV. We postulate that the ability of the NC1 domains to bind with high affinities to laminin 5 and collagen IV facilitates stabilization of the structure of the basement membrane itself and that the NC1-collagen I interaction may be less important for stabilization of the dermal-epidermal junction.
Recommended Citation
Brittingham, Raymond; Uitto, Jouni; and Fertala, Andrzej, "High-Affinity Binding of the NC1 Domain of Collagen VII to Laminin 5 and Collagen IV" (2006). Department of Dermatology and Cutaneous Biology Faculty Papers. Paper 2.
https://jdc.jefferson.edu/dcbfp/2
Comments
This article has been peer-reviewed. It was published in Biochemical and Biophysical Research Communications 343(3):692-9, 2006. The publisher's version is available at http://dx.doi.org/10.1016/j.bbrc.2006.03.034. Copyright (c) 2006 Elsevier, Inc.