Abstract.
Mammalian galectin-1 (Gal-1), a β-galactoside-binding lectin has a prominent role in regulating cell adhesion, cell growth and immune responses. Downregulation of these biological functions may occur via internalization of Gal-1. In the present study we have investigated the mechanism and possible mediator(s) of Gal-1 endocytosis. We show that internalization occurs at a temperature higher than 22 °C in an energy dependent fashion. After one hour incubation Gal-1 localizes in the Golgi system within the cells, and then disappears without accumulation in degradation compartments, such as lysosomes. Based on their strong intracellular co-localization, two glycoconjugates, GM1 ganglioside and CD7 are implicated in the sorting of internalized Gal-1 into Golgi. Other known Gal-1 binding glycoproteins on T cells (CD2, CD3, CD43 and CD45) do not cointernalize with the lectin. Internalization of Gal-1 depends on its lectin activity and follows dual pathways involving clathrin-coated vesicles and raft-dependent endocytosis.
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Received 20 March 2008; received after revision 04 June 2008; accepted 05 June 2008
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Fajka-Boja, R., Blaskó, A., Kovács-Sólyom, F. et al. Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis. Cell. Mol. Life Sci. 65, 2586–2593 (2008). https://doi.org/10.1007/s00018-008-8143-x
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DOI: https://doi.org/10.1007/s00018-008-8143-x