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Receptor binding and internalization of immobilized transcobalamin II by mouse leukaemia cells

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Abstract

Membrane transport of vitamin B12 (cyanocobalamin; Cbl) into mammalian cells is mediated by the serum protein transcobalamin II (TCII)1–3. In mouse leukaemia L1210 cells, TCII–Cbl binds to membrane receptors in a rapid, temperature-independent step and is internalized by a slow, temperature-dependent process4. To delineate the location of receptors on these cells, we have constructed a visual probe by covalently coupling purified TCII–Cbl to submicrometre latex particles5 (minibeads). We report here that when L1210 cells are incubated with minibeads containing TCII–Cbl at 4 °C and examined by scanning electron microscopy (SEM), the particles are found attached predominantly to microvilli. Incubation of the cells at 37 °C results in the internalization of the minibeads. As visualized by transmission electron microscopy (TEM), this endocytotic process seems to occur in clathrin-coated pits and vesicles6,7 at the cell surface.

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Authors and Affiliations

  1. Department of Clinical Research, Scripps Clinic and Research Foundation, La Jolla, California, 92037

    Kiyoshi Takahashi & Mehdi Tavassoli

  2. Department of Biochemistry, Scripps Clinic and Research Foundation, La Jolla, California, 92037

    Donald W. Jacobsen

Authors
  1. Kiyoshi Takahashi
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  2. Mehdi Tavassoli
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  3. Donald W. Jacobsen
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Takahashi, K., Tavassoli, M. & Jacobsen, D. Receptor binding and internalization of immobilized transcobalamin II by mouse leukaemia cells. Nature 288, 713–715 (1980). https://doi.org/10.1038/288713a0

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  • DOI: https://doi.org/10.1038/288713a0

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