Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms

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Abstract

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.

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Subject classification (UKÄ) – MANDATORY

  • Medical Biotechnology

Keywords

  • Galectin, transferrin, glycoforms, trafficking, endocytosis
Original languageEnglish
Pages (from-to)28398-28408
JournalJournal of Biological Chemistry
Volume288
Issue number39
Publication statusPublished - 2013
Publication categoryResearch
Peer-reviewedYes