The versican C-type lectin domain recognizes the adhesion protein tenascin-R

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Reumatologi och inflammation
Originalspråkengelska
Sidor (från-till)10590-10594
TidskriftProceedings of the National Academy of Sciences
Volym92
Utgivningsnummer23
StatusPublished - 1995
PublikationskategoriForskning
Peer review utfördJa