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
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
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DOI：
10.1073/pnas.94.19.10116
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发表时间：
1997-09-16
影响因子：
11.1
通讯作者：
Yamaguchi, Y
中科院分区：
文献类型：
--
作者：
Aspberg, A;Miura, R;Yamaguchi, Y
凝集素是硫酸软骨素蛋白多糖的一个家族，包括聚集素、多聚糖、神经聚糖和短链多糖。凝集素的C端球状结构域在结构上与选择素相关，由C型凝集素结构域和补体调节蛋白结构域组成，C型凝集素结构域与神经系统特异表达的细胞外基质蛋白tenascin-R结合，这种相互作用被认为是由糖-蛋白质相互作用介导的。本文证明了在神经系统中特异表达的另一种凝集素--短链凝集素的C型凝集素结构域也与Tenascin-R结合，这种相互作用是通过Tenascin-R的纤维连接蛋白III型结构域3-5的蛋白-蛋白质相互作用介导的，而不依赖于任何碳水化合物或硫化氨基酸。Versicans和其他凝集素的凝集素结构域也通过蛋白质-蛋白质相互作用与Tenascin a的相同结构域结合，表面等离子共振分析表明，短链凝集素凝集素与其他凝集素凝集素的亲和力至少是其他凝集素凝集素的10倍。Tenascin-R与成年大鼠脑提取物中的Brevican共沉淀。提示Tenascin-R和Brivican在体内形成复合体，这些结果表明C型凝集素结构域可以通过蛋白质-蛋白质相互作用与纤维连接蛋白III型结构域相互作用，提示Brivican是成人脑中一种生理性的Tenascin-R配体。
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 a 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.