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- W2022352275 abstract "Abstract p-formaldehyde-promoted membrane vesiculation of preiodinated cultures lead to the release of surface proteins of about 68 kd in normal and transformed rat liver epithelial cells and rat fibroblasts, concurrent with a marked decrease in surface-associated fibronectin. Membrane vesiculation in the presence of soybean trypsin inhibitor permitted the detection of an 18 kd surface protein in membrane vesicles and the increased expression of a 70 kd external component in normal but not in transformed epithelial cells. Our results show that the membrane vesiculation process is associated both with the release and selective degradation of specific cell surface proteins in a process which may involve surface protease activation. Our data also suggest the potential of the chemical vesiculation process as a probe to monitor differences in surface topography between different cell types." @default.
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- W2022352275 date "1982-01-01" @default.
- W2022352275 modified "2023-09-26" @default.
- W2022352275 title "Loss of fibronectin among the selective surface protein changes associated with p-formaldehyde promoted membrane vesiculation" @default.
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- W2022352275 doi "https://doi.org/10.1016/0006-291x(82)90714-8" @default.
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