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PH and the Recycling of Transferrin During Receptor-mediated Endocytosis

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Specialty Science
Date 1983 Apr 1
PMID 6300903
Citations 362
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Abstract

At pH 5.4 apotransferrin (iron-free transferrin) binds to cell-surface transferrin receptors to the same extent and with the same affinity as does diferric transferrin at pH 7.0. Apotransferrin is quickly dissociated from its receptor when the pH is raised to 7.0. These and other results strongly support a simple model that explains the cycling of transferrin during a single cycle of receptor-mediated endocytosis. Diferric transferrin binds to cell-surface receptors, and the transferrin-receptor complex is endocytosed. The pH of the endocytic vesicle is lowered to 5.5 or below; this causes dissociation of iron from the transferrin-receptor complex, but apotransferrin remains bound to its receptor. The iron remains within the cell, and the apotransferrin-receptor complex is recycled to the cell surface. Upon encountering the neutral pH of the medium, apotransferrin is dissociated from the cell.

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References
1.
ASHWELL G, Morell A . The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv Enzymol Relat Areas Mol Biol. 1974; 41(0):99-128. DOI: 10.1002/9780470122860.ch3. View

2.
PRINCIOTTO J, ZAPOLSKI E . Difference between the two iron-binding sites of transferrin. Nature. 1975; 255(5503):87-8. DOI: 10.1038/255087a0. View

3.
Sullivan A, Grasso J, WEINTRAUB L . Micropinocytosis of transferrin by developing red cells: an electron-microscopic study utilizing ferritin-conjugated transferrin and ferritin-conjugated antibodies to transferrin. Blood. 1976; 47(1):133-43. View

4.
LESTAS A . The effect of pH upon human transferrin: selective labelling of the two iron-binding sites. Br J Haematol. 1976; 32(3):341-50. DOI: 10.1111/j.1365-2141.1976.tb00937.x. View

5.
Carpenter G, Cohen S . 125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblasts. J Cell Biol. 1976; 71(1):159-71. PMC: 2109737. DOI: 10.1083/jcb.71.1.159. View