Brittingham Raymond, Uitto Jouni, Fertala Andrzej
Department of Dermatology and Cutaneous Biology, Jefferson Medical College, and Jefferson Institute of Molecular Medicine, Thomas Jefferson University, Philadelphia, PA 19107, USA.
Biochem Biophys Res Commun. 2006 May 12;343(3):692-9. doi: 10.1016/j.bbrc.2006.03.034. Epub 2006 Mar 15.
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 a Kd value 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.
Ⅶ型胶原的锚定功能取决于其形成同型纤维以及与其他大分子结合形成异型复合物的能力。采用基于生物传感器的结合试验来分析Ⅶ型胶原NC1结构域介导的与层粘连蛋白5、Ⅳ型胶原和Ⅰ型胶原结合的动力学。我们发现Ⅶ型胶原与层粘连蛋白5和Ⅳ型胶原相互作用，解离常数（Kd）值为10⁻⁹ M。相比之下，NC1介导的与Ⅰ型胶原的结合较弱，Kd值为10⁻⁶ M。结合试验还表明，NC1结构域利用相同区域与层粘连蛋白5和Ⅳ型胶原结合。我们推测，NC1结构域与层粘连蛋白5和Ⅳ型胶原高亲和力结合的能力有助于基底膜自身结构的稳定，并且NC1与Ⅰ型胶原的相互作用对真皮 - 表皮连接的稳定可能不太重要。
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