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Intracellular sorting of galectin-8 based on carbohydrate fine specificity

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Author

Summary, in English

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.

Publishing year

2007

Language

English

Pages

906-912

Publication/Series

Glycobiology

Volume

17

Issue

9

Document type

Journal article

Publisher

Oxford University Press

Topic

  • Biochemistry and Molecular Biology

Keywords

  • galectin
  • endocytosis
  • sialic acid
  • intracellular
  • sorting

Status

Published

ISBN/ISSN/Other

  • ISSN: 1460-2423