THE VERSICAN C-TYPE LECTIN DOMAIN RECOGNIZES THE ADHESION PROTEIN TENASCIN-R

被引:118
作者
ASPBERG, A [1 ]
BINKERT, C [1 ]
RUOSLAHTI, E [1 ]
机构
[1] LA JOLLA CANC RES FDN, CANC RES CTR, LA JOLLA, CA 92037 USA
关键词
J1-160; 180; JANUSIN;
D O I
10.1073/pnas.92.23.10590
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
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页码:10590 / 10594
页数:5
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