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Transferrin is required for proliferation of most cells in culture. This effect is presumably mediated by the binding of transferrin to its receptor, a surface glycoprotein which is preferentially expressed by actively growing cells. Here we show that normal human fibroblasts cultured in serum, and other media containing transferrin express transferrin receptors in a distinctly non-random way; punctate foci of the receptor were seen only at the leading lamellae of the cells, whereas cells grown without serum, or in transferrin-depleted serum showed a random distribution of the receptor. In contrast, malignant fibrosarcoma cells showed the receptor uniformly throughout the cell surface in all media tested, including those containing transferrin. The data suggest that the ligand causes a directional lateral movement of the receptor in normal but not in malignant cells. Application of the receptor antibody caused a rapid internalization of the receptor in both cell types.
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Ekblom et al. (1983) studied this question.
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