The versican C-type lectin domain recognizes the adhesion protein tenascin-R
Aspberg, Anders LU
; Binkert, Christoph
and Ruoslahti, Erkki
(1995)
In Proceedings of the National Academy of Sciences
92(23).
p.10590-10594
- Abstract
- The core proteins of large chondroitin sulfate proteoglycans contain a C-type lectin domain. The lectin domain of one of these proteoglycans, versican, was expressed as a recombinant 15-kDa protein and shown to bind to insolubilized fucose and GlcNAc. The lectin domain showed strong binding in a gel blotting assay to a glycoprotein doublet in rat brain extracts. The binding was calcium dependent and abolished by chemical deglycosylation treatment of the ligand glycoprotein. The versican-binding glycoprotein was identified as the cell adhesion protein tenascin-R, and versican and tenascin-R were both found to be localized in the granular layer of rat cerebellum. These results show that the versican lectin domain is a binding domain with a... (More)
- The core proteins of large chondroitin sulfate proteoglycans contain a C-type lectin domain. The lectin domain of one of these proteoglycans, versican, was expressed as a recombinant 15-kDa protein and shown to bind to insolubilized fucose and GlcNAc. The lectin domain showed strong binding in a gel blotting assay to a glycoprotein doublet in rat brain extracts. The binding was calcium dependent and abolished by chemical deglycosylation treatment of the ligand glycoprotein. The versican-binding glycoprotein was identified as the cell adhesion protein tenascin-R, and versican and tenascin-R were both found to be localized in the granular layer of rat cerebellum. These results show that the versican lectin domain is a binding domain with a highly targeted specificity. It may allow versican to assemble complexes containing proteoglycan, an adhesion protein, and hyaluronan. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1109764
- author
- Aspberg, Anders
LU
; Binkert, Christoph
and Ruoslahti, Erkki
- organization
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Proceedings of the National Academy of Sciences
- volume
- 92
- issue
- 23
- pages
- 10590 - 10594
- publisher
- National Academy of Sciences
- external identifiers
-
- pmid:7479846
- scopus:0028783449
- ISSN
- 1091-6490
- language
- English
- LU publication?
- yes
- 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
- 70c6d56a-a447-460f-8111-206e42f35004 (old id 1109764)
- alternative location
- http://www.pnas.org/content/92/23/10590
- http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=40657&blobtype=pdf
- date added to LUP
- 2016-04-01 11:45:29
- date last changed
- 2021-02-07 06:53:14
@article{70c6d56a-a447-460f-8111-206e42f35004,
abstract = {{The core proteins of large chondroitin sulfate proteoglycans contain a C-type lectin domain. The lectin domain of one of these proteoglycans, versican, was expressed as a recombinant 15-kDa protein and shown to bind to insolubilized fucose and GlcNAc. The lectin domain showed strong binding in a gel blotting assay to a glycoprotein doublet in rat brain extracts. The binding was calcium dependent and abolished by chemical deglycosylation treatment of the ligand glycoprotein. The versican-binding glycoprotein was identified as the cell adhesion protein tenascin-R, and versican and tenascin-R were both found to be localized in the granular layer of rat cerebellum. These results show that the versican lectin domain is a binding domain with a highly targeted specificity. It may allow versican to assemble complexes containing proteoglycan, an adhesion protein, and hyaluronan.}},
author = {{Aspberg, Anders and Binkert, Christoph and Ruoslahti, Erkki}},
issn = {{1091-6490}},
language = {{eng}},
number = {{23}},
pages = {{10590--10594}},
publisher = {{National Academy of Sciences}},
series = {{Proceedings of the National Academy of Sciences}},
title = {{The versican C-type lectin domain recognizes the adhesion protein tenascin-R}},
url = {{http://www.pnas.org/content/92/23/10590}},
volume = {{92}},
year = {{1995}},
}