Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)

doi:10.1016/j.fsi.2010.01.013

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	Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)
	Zheng, Wen-jiang 1,2; Hu, Yong-hua 1; Xiao, Zhi-zhong 1; Sun, Li 1
	2010-05-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
卷号	28 期号:5-6 页码:829-836
文章类型	Article
摘要	Ferritin is an evolutionarily conserved protein that plays an important role in iron storage and detoxification. In this study, the gene encoding a ferritin H subunit homologue (SmFer1) was cloned from turbot (Scophthalmus maximus) and analyzed at the expression and functional levels. The open reading frame of SmFer1 is 534 bp and preceded by a 5'-untranslated region that contains a putative Iron Regulatory Element (IRE). The deduced amino acid sequence of SmFer1 shares extensive sequence identities with the H ferritins of a number of fish species and contains the ferroxidase center that is preserved in ferritin H subunits. Examination of tissue specific expression indicated that SmFer1 expression was most abundant in muscle, liver, and blood. Experimental infection with bacterial pathogens induced significant induction of SmFer1: however, the magnitudes of induction effected by Gram-negative pathogens were much higher than that induced by Gram-positive pathogen. Consistently, lipopolysaccharide (LPS) challenge drastically augmented SmFer1 expression. in addition to bacterial pathogens and LPS, poly(I:C) also induced a strong but transient induction of SmFer1 which differs in profile from those induced by bacterial pathogens. In vitro iron-chelating analysis showed that recombinant SmFer1 purified from Escherichia coli was able to bind ferrous iron in a concentration-dependent manner. To examine whether SmFer1, with its iron-chelating capacity, could have any effect on the infection of bacterial pathogens, purified recombinant SmFer1 was subjected to bacteriostatic analysis and proved to be able to inhibit the growth of the fish pathogen Listonella anguillarum which enhanced SmFer1 expression upon infection. Taken together, these results suggest that SmFer1 is likely to play a role in both iron storage and immune defense against microbial infections. (C) 2010 Elsevier Ltd. All rights reserved.
关键词	Ferritin Iron Scophthalmus Maximus Immune Defense
DOI	10.1016/j.fsi.2010.01.013
收录类别	SCI
语种	英语
WOS记录号	WOS:000277822100012
引用统计	被引频次：71[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/32779
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Zheng, Wen-jiang,Hu, Yong-hua,Xiao, Zhi-zhong,et al. Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)[J]. FISH & SHELLFISH IMMUNOLOGY,2010,28(5-6):829-836.
APA	Zheng, Wen-jiang,Hu, Yong-hua,Xiao, Zhi-zhong,&Sun, Li.(2010).Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus).FISH & SHELLFISH IMMUNOLOGY,28(5-6),829-836.
MLA	Zheng, Wen-jiang,et al."Cloning and analysis of a ferritin subunit from turbot (Scophthalmus maximus)".FISH & SHELLFISH IMMUNOLOGY 28.5-6(2010):829-836.

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