Collagen-binding recombinant fibronectin fragments containing type II domains
نویسندگان
چکیده
منابع مشابه
Chondrocyte migration to fibronectin, type I collagen, and type II collagen.
It is well known that cellular interactions, such as cell adhesion, migration, invasion, between cells and the extracellular matrix are mediated by the integrin family of cell surface receptors. Chondrocytes are surrounded by an abundant extracellular matrix, but there is less information on the cellular receptors which interact with this matrix. In our studies, fibronectin, type I collagen, an...
متن کاملHuman fibronectin and MMP-2 collagen binding domains compete for collagen binding sites and modify cellular activation of MMP-2.
The region of fibronectin (FN) surrounding the two type II modules of FN binds type I collagen. However, little is known about interactions of this collagen binding domain with other collagen types or extracellular matrix molecules. Among several expressed recombinant (r) human FN fragments from the collagen binding region of FN, only rI6-I7, which included the two type II modules and both flan...
متن کاملFibronectin binding site in type I collagen regulates fibronectin fibril formation
Mov13 fibroblasts, which do not express endogenous alpha 1(I) collagen chains due to a retroviral insertion, were used to study the role of type I collagen in the process of fibronectin fibrillogenesis. While Mov13 cells produced a sparse matrix containing short fibronectin fibrils, transfection with a wild type pro alpha 1(I) collagen gene resulted in the production of an extensive matrix cont...
متن کاملFibronectin fragments cause release and degradation of collagen-binding molecules from equine explant cultures.
OBJECTIVE Previous experiments have shown that addition of fragmented fibronectin can induce cartilage chondrolysis. In this study we investigated the fate of the collagen- and cell-binding molecules Cartilage oligomeric matrix protein (COMP) and chondroadherin. DESIGN Equine articular cartilage explants were stimulated with the C-terminal and the N-terminal heparin-binding fragments of fibro...
متن کاملIdentification and structural analysis of type I collagen sites in complex with fibronectin fragments.
Collagen and fibronectin are major components of vertebrate extracellular matrices. Their association and distribution control the development and properties of diverse tissues, but thus far no structural information has been available for the complex formed. Here, we report binding of a peptide, derived from the alpha(1) chain of type I collagen, to the gelatin-binding domain of human fibronec...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1994
ISSN: 0014-5793
DOI: 10.1016/0014-5793(94)80604-7