The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion
Miura, R ; Aspberg, Anders LU
; Ethell, I M
; Hagihara, K
; Schnaar, R L
; Ruoslahti, E
and Yamaguchi, Y
(1999)
In Journal of Biological Chemistry
274(16).
p.11431-11438
- Abstract
- The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and... (More)
- The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1116012
- author
- Miura, R
; Aspberg, Anders
LU
; Ethell, I M
; Hagihara, K
; Schnaar, R L
; Ruoslahti, E
and Yamaguchi, Y
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 274
- issue
- 16
- pages
- 11431 - 11438
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- pmid:10196237
- scopus:0033574427
- ISSN
- 1083-351X
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Connective Tissue Biology (013230151)
- id
- 4d6e146a-afed-48e4-8167-305a3cc47540 (old id 1116012)
- alternative location
- http://www.jbc.org/cgi/content/full/274/16/11431
- date added to LUP
- 2016-04-01 12:07:43
- date last changed
- 2022-01-26 23:14:02
@article{4d6e146a-afed-48e4-8167-305a3cc47540,
abstract = {{The lecticans are a group of chondroitin sulfate proteoglycans characterized by the presence of C-type lectin domains. Despite the suggestion that their lectin domains interact with carbohydrate ligands, the identity of such ligands has not been elucidated. We previously showed that brevican, a nervous system-specific lectican, binds the surface of B28 glial cells (Yamada, H., Fredette, B., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., and Yamaguchi, Y. (1997) J. Neurosci. 17, 7784-7795). In this paper, we demonstrate that two classes of sulfated glycolipids, sulfatides and HNK-1-reactive sulfoglucuronylglycolipids (SGGLs), act as cell surface receptors for brevican. The lectin domain of brevican binds sulfatides and SGGLs in a calcium-dependent manner as expected of a C-type lectin domain. Intact, full-length brevican also binds both sulfatides and SGGLs. The lectin domain immobilized as a substrate supports adhesion of cells expressing SGGLs or sulfatides, which was inhibited by monoclonal antibodies against these glycolipids or by treatment of the substrate with SGGLs or sulfatides. Our findings demonstrate that the interaction between the lectin domains of lecticans and sulfated glycolipids comprises a novel cell substrate recognition system, and suggest that lecticans in extracellular matrices serve as substrate for adhesion and migration of cells expressing these glycolipids in vivo.}},
author = {{Miura, R and Aspberg, Anders and Ethell, I M and Hagihara, K and Schnaar, R L and Ruoslahti, E and Yamaguchi, Y}},
issn = {{1083-351X}},
language = {{eng}},
number = {{16}},
pages = {{11431--11438}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{The proteoglycan lectin domain binds sulfated cell surface glycolipids and promotes cell adhesion}},
url = {{http://www.jbc.org/cgi/content/full/274/16/11431}},
volume = {{274}},
year = {{1999}},
}