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Receptor-mediated endocytosis of the intrinsic factor-cobalamin complex in HT 29, a human colon carcinoma cell line.

Abstract
A HT 29 cell line derived from human colonic carcinoma was shown to express the intrinsic factor receptor, with about 5000 binding sites per cell and an association constant of 20 x 10(9) 1/mol at pH 7.4 and 4 degrees C. The number of binding sites increased dramatically between 7 and 10 days of culture time. Endocytosis of the intrinsic factor-cobalamin-receptor complex was inhibited by two ways: at 4 degrees C and at 37 degrees C by incubating the cells with vinblastine, monensin and chloroquine. The plasma membrane receptor was cross-linked to [57Co]cobalamin-intrinsic factor and solubilized with Triton X-100. The cross-linked complex had a relative molecular mass of 330 kDa in native PAGE.
AuthorsJ L Guéant, C Masson, H Schohn, M Girr, M Saunier, J P Nicolas
JournalFEBS letters (FEBS Lett) Vol. 297 Issue 3 Pg. 229-32 (Feb 10 1992) ISSN: 0014-5793 [Print] England
PMID1312012 (Publication Type: Journal Article)
Chemical References
  • Receptors, Cell Surface
  • Chloroquine
  • Intrinsic Factor
  • Vitamin B 12
Topics
  • Chloroquine (pharmacology)
  • Chromatography, Gel
  • Colonic Neoplasms
  • Electrophoresis, Polyacrylamide Gel
  • Endocytosis
  • Humans
  • Intrinsic Factor (metabolism)
  • Kinetics
  • Receptors, Cell Surface (metabolism)
  • Tumor Cells, Cultured
  • Vitamin B 12 (metabolism)

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