Collagen cell surface binding

Cell Surface Binding Integrins, Fibronectin, and Collagen... 

The same ceUs that secrete collagen also secrete fi-bronectin, a large glycoprotein present on cell surfaces, in the extracellular matrix, and in blood (see below). Fi-bronectin binds to aggregating precollagen fibers and alters the kinetics of fiber formation in the pericellular matrix. Associated with fibronectin and procollagen in... 

Fibronectins are typical representatives of adhesive proteins. They are filamentous dimers consisting of two related peptide chains (each with a mass of 250 kDa) linked to each other by disulfide bonds. The fibronectin molecules are divided into different domains, which bind to cell-surface receptors, collagens, fibrin, and various proteoglycans. This is what gives fibronectins their molecular glue" characteristics. 

Staatz WD, Walsh JJ, Pexton T, Santoro SA The a2pi integrin cell surface collagen receptor binds to the al(I>CB3 peptide of collagen. J Biol Chem 265 4778-4781,1990... 

Integrins are the major type of cell surface receptors and are formed by a heterodimer with a and P subunits. Most integrins bind extracellular matrix components like fibronectin, collagen or intronectin. It seems that integrins activate PTKs clustering. 

AChE and BuChE subunits are synthesized within cells (e.g., nerve, muscle, liver, and some megakaryocytes), glycosylated within the Golgi apparatus, and secreted. Collagen-tailed forms become attached to the cell surface at specific binding sites. Globular forms are released into body fluids or bind to cell surfaces by ionic bonds. Antibodies have been prepared to several purified AChEs and BuChEs, and protein and nucleic acid sequences have been determined. 

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