Cell surface molecules that bind fibronectin's matrix assembly domain
نویسندگان
چکیده
منابع مشابه
Cell surface molecules that bind fibronectin's matrix assembly domain.
The assembly of fibronectin into disulfide cross-linked extracellular matrices requires the interaction of mesenchymal cells with two distinct sites on fibronectin, the Arg-Gly-Asp cell adhesive site and an amino-terminal site contained within the first five type I homologous repeats (Quade, B. J., and McDonald, J. A. (1988) J. Biol. Chem. 263, 19602-19609). Proteolytically derived 29-kDa fragm...
متن کاملFibronectin's cell-adhesive domain and an amino-terminal matrix assembly domain participate in its assembly into fibroblast pericellular matrix.
Fibroblasts organize the modular cell-adhesive glycoprotein fibronectin into a highly structured pericellular matrix by poorly understood mechanisms. Previous studies implicated an amino-terminal domain in matrix assembly and suggested that fibronectin's cell-adhesive domain and the corresponding fibroblast receptor were not involved in this process. To further elucidate the fibronectin region(...
متن کاملاهمیت فیبرونکتین در تکوین، ترمیم و درمان: مقاله مروری
Fibronectin (FN) is one of the essential component of the extra cellular matrix and their important role is as regulator of cellular activities and also fibronectin is an important scaffold for maintaining tissue. Fibronectin conformational changes expose additional binding sites that participate in fibril formation and in conversion of fibrils into a stabilized, insoluble form. In fact fibrone...
متن کاملPhagocytic Cell Molecules That Bind the Collagen - like Region of C l q INVOLVEMENT IN
C l q binds to and elicits cellular responses by several cell types, including monocytes, macrophages, neutrophils, B cells, and fibroblasts. The cell-binding domain is located within the collagen-like pepsin-resistant region of the Clq molecule (Clq tails). An affinity matrix of Clq tails coupled to Sepharose was used to select Clq-binding proteins from detergent extracts of surface-iodinated ...
متن کاملNucleosomes bind to cell surface proteoglycans.
Material on the surface of activated T-cells was displaced following incubation with a sulfated polysaccharide, dextrin 2-sulfate (D2S), and purified by anion-exchange chromatography. This revealed a complex comprising histones H2A, H2B, H3, and H4 and DNA fragmented into 180-base pair units characteristic of mono-, di-, tri, and polynucleosomes, a pattern of fragmentation similar to that found...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1991
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)92876-0