Cellular interactions with fibronectin as a model for redundant binding of cells to other extracellular matrix proteins.
Perhaps the most studied property of fibronectin (Fn) is its ability to bind to cells. Interestingly, there are multiple mechanisms by which cells can bind Fn involving as many as ten different cell surface molecules and perhaps six distinct sites within Fn. This apparent redundant binding system is not only restricted to Fn since cells bind other extracellular matrix proteins such as laminin, vitronectin and fibrinogen in a similar manner. The many binding interactions between cells and Fn may serve as a model for understanding redundant binding between cells and other matrix proteins.
Argraves
W S
WS
American Red Cross, Biochemistry Laboratory, Rockville, Maryland 20855.
Gehlsen
K R
KR
D000818:Animals; D001665:Binding Sites; D002477:Cells / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D006801:Humans; D016023:Integrins / Q000378:metabolism; D008958:Models, Molecular
D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D016023:Integrins