pubmed-article:9294172 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
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pubmed-article:9294172 | lifeskim:mentions | umls-concept:C0872079 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C0168310 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
pubmed-article:9294172 | lifeskim:mentions | umls-concept:C0332291 | lld:lifeskim |
pubmed-article:9294172 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:9294172 | pubmed:dateCreated | 1997-10-21 | lld:pubmed |
pubmed-article:9294172 | pubmed:abstractText | The lecticans are a family of chondroitin sulfate proteoglycans including aggrecan, versican, neurocan, and brevican. The C-terminal globular domains of lecticans are structurally related to selectins, consisting of a C-type lectin domain flanked by epidermal growth factor and complement regulatory protein domains. The C-type lectin domain of versican has been shown to bind tenascin-R, an extracellular matrix protein specifically expressed in the nervous system, and the interaction was presumed to be mediated by a carbohydrate-protein interaction. In this paper, we show that the C-type lectin domain of brevican, another lectican that is specifically expressed in the nervous system, also binds tenascin-R. Surprisingly, this interaction is mediated by a protein-protein interaction through the fibronectin type III domains 3-5 of tenascin-R, independent of any carbohydrates or sulfated amino acids. The lectin domains of versican and other lecticans also bind the same domain of tenascin-R by protein-protein interactions. Surface plasmon resonance analysis revealed that brevican lectin has at least a 10-fold higher affinity than the other lectican lectins. Tenascin-R is coprecipitated with brevican from adult rat brain extracts, suggesting that tenascin-R and brevican form complexes in vivo. These results demonstrate that the C-type lectin domain can interact with fibronectin type III domains through protein-protein interactions, and suggest that brevican is a physiological tenascin-R ligand in the adult brain. | lld:pubmed |
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pubmed-article:9294172 | pubmed:language | eng | lld:pubmed |
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pubmed-article:9294172 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:9294172 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9294172 | pubmed:month | Sep | lld:pubmed |
pubmed-article:9294172 | pubmed:issn | 0027-8424 | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:MiuraRR | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:SchachnerMM | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:YamaguchiYY | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:RuoslahtiEE | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:AspbergAA | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:ShimonakaMM | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:BourdoulousSS | lld:pubmed |
pubmed-article:9294172 | pubmed:author | pubmed-author:HeinegârdDD | lld:pubmed |
pubmed-article:9294172 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9294172 | pubmed:day | 16 | lld:pubmed |
pubmed-article:9294172 | pubmed:volume | 94 | lld:pubmed |
pubmed-article:9294172 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9294172 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9294172 | pubmed:pagination | 10116-21 | lld:pubmed |
pubmed-article:9294172 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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pubmed-article:9294172 | pubmed:year | 1997 | lld:pubmed |
pubmed-article:9294172 | pubmed:articleTitle | The C-type lectin domains of lecticans, a family of aggregating chondroitin sulfate proteoglycans, bind tenascin-R by protein-protein interactions independent of carbohydrate moiety. | lld:pubmed |
pubmed-article:9294172 | pubmed:affiliation | The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA. | lld:pubmed |
pubmed-article:9294172 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9294172 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9294172 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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