Abstract
The pericellular glycoprotein fibronectin, which has been localized in the pericellular matrix and at the adhesion sites of cells1–5, has been considered to be important in cell attachment to other cells and to surfaces1–8. Using the ionophore monensin, which blocks the secretion of endogenous fibronectin9,10, we have now shown that human fibroblasts do not require endogenous or exogenous fibronectin for adhesion and spreading, although its absence does prevent formation of the microfilament–vinculin system and the focal adhesion sites.
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Virtanen, I., Vartio, T., Badley, R. et al. Fibronectin in adhesion, spreading and cytoskeletal organization of cultured fibroblasts. Nature 298, 660–663 (1982). https://doi.org/10.1038/298660a0
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DOI: https://doi.org/10.1038/298660a0
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