Characterization of the transferrin receptor in tunicamycin-treated A431 cells

C. L. Reckhow, C. A. Enns

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37 Scopus citations


The transferrin receptor undergoes extensive co- and post-translational modifications during its biosynthesis. In this study, the functional and structural properties of the transferrin receptor from tunicamycin-treated A431 cells were examined. Incubation of A431 cells with this inhibitor of asparagine-linked glycosylation results in a shift of the apparent molecular weight of the transferrin receptor from 94,000 to 79,000. The electrophoretic mobility of the receptor from treated cells is that of a monomer under nonreducing conditions, whereas the transferrin receptor in untreated cells has the mobility of a dimer under identical conditions. This result indicates a lack of disulfide bond formation between subunits of the receptor from tunicamycin-treated cells. In solution no dimers can be detected with cross-linking studies. This unglycosylated receptor does not appear to stably bind transferrin as demonstrated by a lack of isolation of this form of the receptor with transferrin-linked Sepharose. It is not transported to the surface of A431 cells.

Original languageEnglish (US)
Pages (from-to)7297-7301
Number of pages5
JournalJournal of Biological Chemistry
Issue number15
StatePublished - 1988
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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