Evidence that an RGD-dependent receptor mediates the binding of oligodendrocytes to a novel ligand in a glial-derived matrix.
A simple adhesion assay was used to measure the interaction between rat oligodendrocytes and various substrata, including a matrix secreted by glial cells. Oligodendrocytes bound to surfaces coated with fibronectin, vitronectin and a protein component of the glial matrix. The binding of cells to all of these substrates was inhibited by a synthetic peptide (GRGDSP) modeled after the cell-binding domain of fibronectin. The component of the glial matrix responsible for the oligodendrocyte interaction is a protein which is either secreted by the glial cells or removed from serum by products of these cultures; serum alone does not promote adhesion to the same extent as the glial-derived matrix. The interaction of cells with this glial-derived matrix requires divalent cations and is not mediated by several known RGD-containing extracellular proteins, including fibronectin, vitronectin, thrombospondin, type I and type IV collagen, and tenascin.[1]References
- Evidence that an RGD-dependent receptor mediates the binding of oligodendrocytes to a novel ligand in a glial-derived matrix. Cardwell, M.C., Rome, L.H. J. Cell Biol. (1988) [Pubmed]
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