Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis
| Autor: | Éva Monostori, Roberta Fajka-Boja, Andrea Blaskó, Gábor J. Szebeni, G. K. Tóth, F. Kovács-Sólyom |
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| Rok vydání: | 2008 |
| Předmět: |
Glycosylation
Time Factors Galectin 1 media_common.quotation_subject Golgi Apparatus Antigens CD7 G(M1) Ganglioside Biology Ligands Endocytosis Clathrin Bulk endocytosis Cell Line Cellular and Molecular Neuroscience symbols.namesake Membrane Microdomains Animals Humans Cell adhesion Internalization Molecular Biology media_common Pharmacology Temperature Lectin Cell Biology Receptor-mediated endocytosis Golgi apparatus Rats Cell biology Protein Transport biology.protein symbols Thermodynamics Molecular Medicine |
| Zdroj: | Cellular and Molecular Life Sciences. 65:2586-2593 |
| ISSN: | 1420-9071 1420-682X |
| Popis: | Mammalian galectin-1 (Gal-1), a beta-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 degrees 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. |
| Databáze: | OpenAIRE |
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