Fibronectin collagen binding

Elice MJ, Urry LA, Hemler ME. Receptor frmcrions for the int rin VLA-3 fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J Cell Biol 1991 112 169-181. 

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. 

TGF-P also regulates cell-substratum interactions by a selectively increasing expression of integrins, a major class of cell-adhesion receptors. Integrins bind fibronectin, collagens, and other ECM proteins28-29 and thus modulate the adhesion cascade, which modulates cell migration. 

The specific interaction of fibronectin with collagen has functional significance. While it has been demonstrated that fibronectin can bind to the cell surface without the addition of... 

Integrins Transmembrane a)S-heterodimer a 165 kDa j , 90-120 kDa Plasmalemma Binding to laminins, fibronectin, collagen specificity depends on a)S composition Maintenance of cell to basement membrane and extracellular matrix binding... 

Fibronectin mediates the adhesion of cells to collagen by first binding to the collagen substrate followed by attachment of the cells to the fibronectin-collagen complex. Bovine brain gangliosides prevented the adhesion of cells to the fibronectin-collagen complex, but had no effect on the initial formation of the fibronectin-collagen complex. The order of efficiency was and G > Gd, j Gj > was not an inhibitor. Only the carbohydrate portions of... 

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... 

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