
doi: 10.1007/bf02790069
pmid: 7534098
Incubation of cells with selenite, under conditions in which there is no effect on cell viability, results in a decrease in the rate of their subsequent attachment to extracellular matrix proteins such as fibronectin (1). The attachment was inhibited by a pentapeptide containing the RGD sequence and by antibody against the cellular fibronectin receptor (alpha 5 beta 1 integrin), indicating that it is receptor-mediated. To investigate whether exposure to selenite has an effect on fibronectin receptors, we assayed for their presence on the cell surface by measuring the ability of cells to attach to a surface that had been coated with antibodies to the receptor. Brief exposure of cells to low concentrations of selenite resulted in a significant decrease in their ability to attach to monoclonal antibodies against the alpha 5 or beta 1 subunits of the fibronectin receptor, as well as to polyclonal antibodies against the complete receptor. This indicates that exposure to selenite results in a decrease in receptors that are present at the cell surface. Exposure of the cells to selenate, selenocystine or selenomethionine did not result in a significant decrease in cell surface receptors. Preincubation of the cells with selenite was required for the effect, indicating that selenite does not directly interfere with receptor structure or function.
Antibodies, Monoclonal, Membrane Proteins, Receptors, Cell Surface, Fibronectins, Epitopes, Receptors, Fibronectin, Sodium Selenite, Cell Adhesion, Humans, HeLa Cells
Antibodies, Monoclonal, Membrane Proteins, Receptors, Cell Surface, Fibronectins, Epitopes, Receptors, Fibronectin, Sodium Selenite, Cell Adhesion, Humans, HeLa Cells
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