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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)
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published
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in
Proceedings of the National Academy of Sciences
volume
92
issue
23
pages
10590 - 10594
publisher
National Acad Sciences
external identifiers
  • pmid:7479846
  • scopus:0028783449
ISSN
1091-6490
language
English
LU publication?
yes
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
2008-07-29 15:03:42
date last changed
2017-01-01 04:30:48
@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 Acad Sciences},
  series       = {Proceedings of the National Academy of Sciences},
  title        = {The versican C-type lectin domain recognizes the adhesion protein tenascin-R},
  volume       = {92},
  year         = {1995},
}