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A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge

文献类型：期刊论文

作者Zhou, Zhi1,2; Wang, Lingling1; Gao, Yang1,2; Wang, Mengqiang1,2; Zhang, Huan1; Wang, Leilei1,2; Qiu, Limei1; Song, Linsheng1
刊名DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
出版日期2011-07-01
卷号35期号:7页码:799-807
关键词Monoamine Oxidase (Mao) Monoamine Immunomodulation Innate Immunity Scallop
ISSN号0145-305X
DOI10.1016/j.dci.2011.03.014
文献子类Article
英文摘要Monoamine oxidase (MAO) is an essential enzyme in the catabolism of monoamines, and implicated in the immune response of vertebrates. In the present study, the full-length cDNA encoding monoamine oxidase (designated CfMAO) was cloned from Chlamys farreri by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfMAO cDNA encoded 519 amino acids, which shared 73.9% similarity with that from oyster Crassostrea gigas, and 64.5-66.3% similarity with those from vertebrates. A conserved Amino_oxidase domain and a transmembrane domain were identified in the deduced CfMAO protein. The mRNA transcripts of CfMAO could be detected in all the tested tissues, including haemocytes, hepatopancreas. kidney, adductor muscle, mantle, gill and gonad. The mRNA expression of CfMAO was up-regulated significantly in haemocytes of scallops during 6-48 h after bacteria Vibrio anguillarum challenge, and it reached the peak (25.9-fold, P < 0.05) at 12 h. The cDNA fragment encoding the mature peptide of CfMAO was expressed in the prokaryotic expression system. and 1 mg of the recombinant protein (rCfMAO) could catalyze the deamination of 3665.59 nmol serotonin, 2061.89 nmol norepinephrine, 2104.85 nmol epinephrine or 3040.34 nmol dopamine within 1 min (nmol min(-1) mg(-1)) in vitro. When the reaction mixture was coincubated with 0.1 mmol L(-1) MAO inhibitor clorgyline, its catalyzing activity to deaminize serotonin and dopamine was decreased significantly to 1603.69 and 955.39 nmol min(-1) mg(-1) (P < 0.05) respectively. These results indicated that CfMAO, as the homologue of monoamine oxidase in scallop C. farreri, could modulate the immune response of scallops through the deamination of monoamines. (C) 2011 Elsevier Ltd. All rights reserved.; Monoamine oxidase (MAO) is an essential enzyme in the catabolism of monoamines, and implicated in the immune response of vertebrates. In the present study, the full-length cDNA encoding monoamine oxidase (designated CfMAO) was cloned from Chlamys farreri by using rapid amplification of cDNA ends (RACE) approaches and expression sequence tag (EST) analysis. The open reading frame of CfMAO cDNA encoded 519 amino acids, which shared 73.9% similarity with that from oyster Crassostrea gigas, and 64.5-66.3% similarity with those from vertebrates. A conserved Amino_oxidase domain and a transmembrane domain were identified in the deduced CfMAO protein. The mRNA transcripts of CfMAO could be detected in all the tested tissues, including haemocytes, hepatopancreas. kidney, adductor muscle, mantle, gill and gonad. The mRNA expression of CfMAO was up-regulated significantly in haemocytes of scallops during 6-48 h after bacteria Vibrio anguillarum challenge, and it reached the peak (25.9-fold, P < 0.05) at 12 h. The cDNA fragment encoding the mature peptide of CfMAO was expressed in the prokaryotic expression system. and 1 mg of the recombinant protein (rCfMAO) could catalyze the deamination of 3665.59 nmol serotonin, 2061.89 nmol norepinephrine, 2104.85 nmol epinephrine or 3040.34 nmol dopamine within 1 min (nmol min(-1) mg(-1)) in vitro. When the reaction mixture was coincubated with 0.1 mmol L(-1) MAO inhibitor clorgyline, its catalyzing activity to deaminize serotonin and dopamine was decreased significantly to 1603.69 and 955.39 nmol min(-1) mg(-1) (P < 0.05) respectively. These results indicated that CfMAO, as the homologue of monoamine oxidase in scallop C. farreri, could modulate the immune response of scallops through the deamination of monoamines. (C) 2011 Elsevier Ltd. All rights reserved.
学科主题Immunology ; Zoology
URL标识查看原文
语种英语
WOS记录号WOS:000291071900010
公开日期2012-07-03
源URL[http://ir.qdio.ac.cn/handle/337002/11750]  
专题海洋研究所_实验海洋生物学重点实验室
海洋研究所_海洋腐蚀与防护研究发展中心
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714		 Zhou, Zhi,Wang, Lingling,Gao, Yang,et al. A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2011,35(7):799-807.
APA Zhou, Zhi.,Wang, Lingling.,Gao, Yang.,Wang, Mengqiang.,Zhang, Huan.,...&Song, Linsheng.(2011).A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,35(7),799-807.
MLA Zhou, Zhi,et al."A monoamine oxidase from scallop Chlamys farreri serving as an immunomodulator in response against bacterial challenge".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 35.7(2011):799-807.

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来源：海洋研究所

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