Advanced

Intracellular sorting of galectin-8 based on carbohydrate fine specificity

Nordenfelt, Susanne LU ; Carlsson, Michael LU and Leffler, Hakon LU (2007) In Glycobiology 17(9). p.906-912
Abstract
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
galectin, endocytosis, sialic acid, intracellular, sorting
in
Glycobiology
volume
17
issue
9
pages
906 - 912
publisher
Oxford University Press
external identifiers
  • wos:000249821000002
  • scopus:34548736515
ISSN
1460-2423
DOI
10.1093/glycob/cwm059
language
English
LU publication?
yes
id
7e609e6c-ce0c-46fd-b88f-213ccd8b31b4 (old id 656141)
date added to LUP
2007-12-05 15:52:20
date last changed
2017-10-01 04:43:05
@article{7e609e6c-ce0c-46fd-b88f-213ccd8b31b4,
  abstract     = {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.},
  author       = {Nordenfelt, Susanne and Carlsson, Michael and Leffler, Hakon},
  issn         = {1460-2423},
  keyword      = {galectin,endocytosis,sialic acid,intracellular,sorting},
  language     = {eng},
  number       = {9},
  pages        = {906--912},
  publisher    = {Oxford University Press},
  series       = {Glycobiology},
  title        = {Intracellular sorting of galectin-8 based on carbohydrate fine specificity},
  url          = {http://dx.doi.org/10.1093/glycob/cwm059},
  volume       = {17},
  year         = {2007},
}