Abstract
REICH and colleagues have reported that a variety of embryo fibroblasts in tissue culture show fibrinolytic activity after viral transformation1,2. This effect is attributable to the action of a plasminogen activator, which is a serine protease3 and is present at higher concentrations in transformed than untransformed fibroblasts4; this activator converts plasminogen, present in the serum, to the fibrinolytic enzyme plasmin5,6. Certain characteristics of transformed cells, such as altered morphology and multilayering, may be plasmin dependent7,8. Plasmin may also induce changes in untransformed cells; this is supported by the observation that normal fibroblasts cocultured with viral transformants developed similar morphology to that of the transformed cells8. Furthermore, proteolytic activity released from transformed cells induced lectin-mediated agglutination, and stimulated thymidine incorporation in non-dividing cultures of untransformed fibroblasts and epithelial cells9. The possibility therefore exists that untransformed cells may express in coculture certain features of transformed cells as a result of environmental plasminogen activation. In support of this we report here the plasminogen-dependent enhancement of agglutination by concanavalin A (con A) of untransformed cells in coculture with transformed cells.
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References
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WHUR, P., KOPPEL, H., URQUHART, C. et al. Plasmin-mediated agglutination by concanavalin A of 3T3 cells cocultured with SV40–3T3 transformants. Nature 260, 709–710 (1976). https://doi.org/10.1038/260709a0
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DOI: https://doi.org/10.1038/260709a0
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