Galectin-3 guides intracellular trafficking of some human serotransferrin glycoforms
Research output: Contribution to journal › Journal article › peer-review
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.
Original language | English |
---|---|
Journal | The Journal of Biological Chemistry |
ISSN | 0021-9258 |
DOIs | |
Publication status | Published - 7 Aug 2013 |
ID: 49740939