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首页> 外文期刊>Comparative biochemistry and physiology, Part B. Biochemistry & molecular biology >Identification and expression of a ferritin homolog in amphioxus Branchiostoma belcheri: Evidence for its dual role in immune response and iron metabolism
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Identification and expression of a ferritin homolog in amphioxus Branchiostoma belcheri: Evidence for its dual role in immune response and iron metabolism

机译:鉴定和表达双歧杆菌Belcheriostoma belcheri中的铁蛋白同源物:在免疫应答和铁代谢中双重作用的证据

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Ferritin plays a key role in cellular iron metabolism including iron storage and detoxification, which has been identified in a wide range of organisms including bacteria, fungi, plants and animals. However, little information is available regarding ferritin in the protochordates to date. Here we demonstrate the presence of a ferritin gene homolog, BbFRT, in amphioxus Branchiostoma belcheri. Analysis of the BURT 5'-UTR indicated the existence of a putative iron-responsive element (IRE) with a predicated stem-loop structure. BbFRT encoded a deduced protein of 172 amino acids with the conserved motif for ferroxidase center typical of heavy chains of vertebrate ferritins. Sequence comparison showed that BbFRT shared more identity to H-chains (68%) of vertebrate ferritins than to the L-chains (46-51%). Both in situ hybridization histochemistry and immunohistochemical staining revealed that BURT was ubiquitously expressed in B. belcheri. In addition, BbFRT expression was up-regulated by 1.6-fold and 1.5-fold, respectively, following exposure to LPS at both transcriptional and translational levels. Similarly, exposure to iron resulted in about 1.6-fold increase in BbFRT in the humoral fluids. These suggest that BbFRT seems a protein with a dual function functioning in both immune response and iron metabolism. (C) 2008 Elsevier Inc. All rights reserved.
机译:铁蛋白在细胞的铁代谢中起着关键作用,包括铁的存储和排毒,这已在包括细菌,真菌,植物和动物在内的多种生物中得到了证实。但是,到目前为止,关于原蛋白中铁蛋白的信息很少。在这里,我们证明了铁蛋白基因同源物BbFRT在双歧杆菌Belcheri belcheri中的存在。对BURT 5'-UTR的分析表明存在假定的铁环结构推测的铁响应元件(IRE)。 BbFRT编码一个172个氨基酸的推导蛋白,具有脊椎动物铁蛋白重链典型特征的铁氧化酶中心的保守基序。序列比较表明,BbFRT与脊椎动物铁蛋白的H链(68%)比与L链(46-51%)具有更多的同一性。原位杂交组织化学和免疫组织化学染色均表明,BURT在belcheri。belcheri中普遍存在。另外,在转录和翻译水平下暴露于LPS后,BbFRT表达分别上调了1.6倍和1.5倍。同样,暴露于铁导致体液中BbFRT升高约1.6倍。这些提示BbFRT似乎是一种在免疫反应和铁代谢中均具有双重功能的蛋白质。 (C)2008 Elsevier Inc.保留所有权利。

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