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首页> 外文期刊>Bioconjugate Chemistry >Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium
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Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium

机译:蜱肠唾液蛋白evaSin-3允许通过与沉积在活性内皮上的CXC型趋化因子的相互作用来可视化动脉中的炎症

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摘要

Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.
机译:动脉粥样硬化是发达国家和发展中国家死亡的主要原因之一。 动脉粥样硬化发育的发作伴有几种炎症趋化因子的过度表达。 通过趋化因子结合剂中和这些趋化因子衰减动脉粥样硬化进展。 在这里,我们研究了蜱蛋白evaSin-3的结构结合特征至趋化因子(C-X-C motif)配体1(CXCL1)。 我们表明EvaSin-3结合的CXCl1不能激活CXCR2受体,但保留对甘氨酸氨基 - 聚糖的亲和力。 通过通过荧光EvaNIN-3缀合物可视化沉积在人内皮细胞和鼠颈动脉的细胞壁上的一组密切相关的CXC型趋化因子来检测该观察。 这项工作突出了蜱衍生的趋化因子结合缀合物作为炎症成像开发新试剂的平台的适用性。

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