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Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

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Author

Summary, in English

Transferrin internalization via clathrin-mediated endocytosis and subsequent recycling after iron delivery has been extensively studied. Here we demonstrate a previously unrecognized parameter regulating this recycling -the binding of galectin-3 to particular glycoforms of transferrin. Two fractions of transferrin, separated by affinity chromatography based on their binding or not to galectin-3, are targeted to kinetically different endocytic pathways in HFL-1 cells expressing galectin-3 but not in SKBR3 cells lacking galectin-3; the SKBR3 cells, however can acquire the ability to target these transferrin glycoforms differently after preloading with exogenously added galectin-3. In all, this study provides the first evidence of a functional role for transferrin glycans, in intracellular trafficking after uptake. Moreover, the galectin-3 bound glycoform increased in cancer, suggesting a pathophysiological regulation. These are novel aspects of transferrin cell biology, which has previously considered only degree of iron loading, but not other forms of heterogeneity.

Publishing year

2013

Language

English

Pages

28398-28408

Publication/Series

Journal of Biological Chemistry

Volume

288

Issue

39

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Medical Biotechnology

Keywords

  • Galectin
  • transferrin
  • glycoforms
  • trafficking
  • endocytosis

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X