Intracellular sorting of galectin-8 based on carbohydrate fine specificity

Research output: Contribution to journalArticle


Galectin-8 has two carbohydrate recognition domains (CRDs), both of which bind beta-galactosides, but have different. ne specificity for larger saccharides. Previously we found that both CRDs were needed for efficient cell surface binding and signaling by soluble galectin-8, but unexpectedly binding of the N-CRD to its best ligands, alpha 2-3-sialylated galactosides, was not needed. In search for another role for this. ne specificity, we now compared endocytosis of galectin-8 in Chinese hamster ovary (CHO) cells and in a mutant (Lec2) lacking sialylated glycans, by fluorescence microscopy. Galectin-8 was endocytosed in both cells by a non-clathrin and non-cholesterol dependent pathway, but surprisingly, the pathway after endocytosis differed dramatically. In wild type (wt) cells, galectin-8 was found along the plasma membrane, near the nucleus, and in small vesicles. In the Lec2 cells, galectin-8 was found in larger vesicles evenly spread in the cell, but not along the plasma membrane or near the nucleus. Agalectin-8 mutant with an N-CRD having reduced affinity to sialylated glycans and increased affinity for other glycans, gave a Lec2 like pattern in the wt CHO cells, but a wt pattern in the Lec2 cells. Moreover, the pattern of galectin-3 after endocytosis differed from that of both the wt and mutant galactin-8. These data clearly demonstrate a role of galectin. ne specificity for intracellular targeting.


Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Biochemistry and Molecular Biology


  • galectin, endocytosis, sialic acid, intracellular, sorting
Original languageEnglish
Pages (from-to)906-912
Issue number9
Publication statusPublished - 2007
Publication categoryResearch

Related research output

Susanne Nordenfelt, 2007, Institution of Laboratory Medicine, Section of Microbiology, Immunology and Glycobiology (MIG). 132 p.

Research output: ThesisDoctoral Thesis (compilation)

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