Intracellular sorting of galectin-8 based on carbohydrate fine specificity
(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:
https://lup.lub.lu.se/record/656141
- author
- Nordenfelt, Susanne LU ; Carlsson, Michael LU and Leffler, Hakon LU
- organization
- publishing date
- 2007
- 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
- 2016-04-01 16:16:14
- date last changed
- 2022-01-28 18:28:39
@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}},
keywords = {{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}},
doi = {{10.1093/glycob/cwm059}},
volume = {{17}},
year = {{2007}},
}