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Scophthalmus maximus cystatin B enhances head kidney macrophage-mediated bacterial killing
Xiao, Ping-ping1,2; Hu, Yong-hua1; Sun, Li1
2010-12-01
发表期刊DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN0145-305X
卷号34期号:12页码:1237-1241
文章类型Article
摘要Cystatins form a large family of cysteine protease inhibitors found in a wide arrange of organisms. Studies have indicated that mammalian cystatins play important roles under both physiological and pathological conditions. However, much less is known about fish cystatins. In this report, we described the identification and analysis of a cystatin B homologue, SmCytB, from turbot Scophthalmus maximus. The open reading frame of SmCytB is 300 bp, which encodes a 99-residue protein that shares high levels of sequence identities with the cystatin B of a number of fish species and contains the conserved cysteine protease inhibitor motif of cystatin B. Constitutive expression of SmCytB is high in muscle, brain, heart and liver, and low in spleen. blood, gill and kidney. Bacterial infection upregulates SmCytB expression in kidney, spleen, liver and brain but not in muscle or heart. Functional analysis showed that recombinant SmCytB purified from Escherichia colt exhibits apparent cysteine protease inhibitor activity. Transient overexpression of SmCytB in head kidney macrophages enhances macrophage bactericidal activity probably through a nitric oxide-independent mechanism. These results indicate that SmCytB is involved in the immune defense of turbot against bacterial infection. (C) 2010 Elsevier Ltd. All rights reserved.; Cystatins form a large family of cysteine protease inhibitors found in a wide arrange of organisms. Studies have indicated that mammalian cystatins play important roles under both physiological and pathological conditions. However, much less is known about fish cystatins. In this report, we described the identification and analysis of a cystatin B homologue, SmCytB, from turbot Scophthalmus maximus. The open reading frame of SmCytB is 300 bp, which encodes a 99-residue protein that shares high levels of sequence identities with the cystatin B of a number of fish species and contains the conserved cysteine protease inhibitor motif of cystatin B. Constitutive expression of SmCytB is high in muscle, brain, heart and liver, and low in spleen. blood, gill and kidney. Bacterial infection upregulates SmCytB expression in kidney, spleen, liver and brain but not in muscle or heart. Functional analysis showed that recombinant SmCytB purified from Escherichia colt exhibits apparent cysteine protease inhibitor activity. Transient overexpression of SmCytB in head kidney macrophages enhances macrophage bactericidal activity probably through a nitric oxide-independent mechanism. These results indicate that SmCytB is involved in the immune defense of turbot against bacterial infection. (C) 2010 Elsevier Ltd. All rights reserved.
关键词Cystatin b Scophthalmus Maximus Macrophage Bacterial Infection
学科领域Immunology ; Zoology
DOI10.1016/j.dci.2010.07.008
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收录类别SCI
语种英语
WOS记录号WOS:000283270700001
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被引频次:34[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/337002/5914
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
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Xiao, Ping-ping,Hu, Yong-hua,Sun, Li. Scophthalmus maximus cystatin B enhances head kidney macrophage-mediated bacterial killing[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2010,34(12):1237-1241.
APA Xiao, Ping-ping,Hu, Yong-hua,&Sun, Li.(2010).Scophthalmus maximus cystatin B enhances head kidney macrophage-mediated bacterial killing.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,34(12),1237-1241.
MLA Xiao, Ping-ping,et al."Scophthalmus maximus cystatin B enhances head kidney macrophage-mediated bacterial killing".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 34.12(2010):1237-1241.
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