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      Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes

      research-article
      The Journal of Cell Biology
      The Rockefeller University Press

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          Abstract

          Using ferritin-labeled protein A and colloidal gold-labeled anti-rabbit IgG, the fate of the sheep transferrin receptor has been followed microscopically during reticulocyte maturation in vitro. After a few minutes of incubation at 37 degrees C, the receptor is found on the cell surface or in simple vesicles of 100-200 nm, in which the receptor appears to line the limiting membrane of the vesicles. With time (60 min or longer), large multivesicular elements (MVEs) appear whose diameter may reach 1-1.5 micron. Inside these large MVEs are round bodies of approximately 50-nm diam that bear the receptor at their external surfaces. The limiting membrane of the large MVEs is relatively free from receptor. When the large MVEs fuse with the plasma membrane, their contents, the 50-nm bodies, are released into the medium. The 50-nm bodies appear to arise by budding from the limiting membrane of the intracellular vesicles. Removal of surface receptor with pronase does not prevent exocytosis of internalized receptor. It is proposed that the exocytosis of the approximately 50-nm bodies represents the mechanism by which the transferrin receptor is shed during reticulocyte maturation.

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          Author and article information

          Journal
          J Cell Biol
          The Journal of Cell Biology
          The Rockefeller University Press
          0021-9525
          1540-8140
          1 September 1985
          : 101
          : 3
          : 942-948
          Article
          85289521
          10.1083/jcb.101.3.942
          2113705
          2993317
          741a5d16-b89d-4c5d-a1a7-f064cba89c63
          History
          Categories
          Articles

          Cell biology
          Cell biology

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