层粘连蛋白
基底膜
化学
胶原蛋白,I型,α1
IV型胶原
生物物理学
纤维
生物化学
细胞外基质
细胞生物学
生物
作者
Raymond Brittingham,Jouni Uitto,Andrzej Fertala
标识
DOI:10.1016/j.bbrc.2006.03.034
摘要
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.
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