Molecular cloning, characterization and mRNA expression of peroxiredoxin in Zhikong scallop Chlamys farreri

被引：26

作者：

Cong, Ming ^{[1
,2
]}

Ni, Duojiao ^{[1
,2
]}

Song, Linsheng ^{[1
]}

Wang, Lingling ^{[1
]}

Zhao, Jianmin ^{[1
]}

Qiu, Limei ^{[1
]}

Li, Ling ^{[1
,2
]}

机构：

[1] Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Shandong, Peoples R China

[2] Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China

来源：

MOLECULAR BIOLOGY REPORTS | 2009年 / 36卷 / 06期

关键词：

Chlamys farreri; Fluorescent real-time quantitative PCR; Immune response; Listonella anguillarum; Peroxiredoxin; ANTIOXIDANT ENZYME PEROXIREDOXIN-5; THIOREDOXIN PEROXIDASE; OXIDATIVE STRESS; MYTILUS-EDULIS; NITRIC-OXIDE; HUMAN TENDON; HUMAN LUNG; GENE; APOPTOSIS; FAMILY;

D O I：

10.1007/s11033-008-9335-z

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Peroxiredoxin V (PRX V) is known as an atypical 2-cysteine peroxiredoxin that protects the organisms against various oxidative stresses and functions in signal transduction. The cDNA of a PRX V gene (designated as CfPRX) was cloned from scallop Chlamys farreri. The full-length sequence of CfPRX cDNA was of 2,179 bp with a 564 bp open reading frame encoding a peptide of 187 amino acids. Sequence comparison showed that CfPRX shared higher identities with PRX Vs than that with other isoforms of PRX, indicating CfPRX was a member of the PRX V family. Fluorescent real-time quantitative PCR analysis revealed the presence of CfPRX transcripts in gill filaments, adductor muscle, heart, gonad, kidney and hemocytes, and the stimulation of Listonella anguillarum significantly (P < 0.01) enhanced the mRNA expression of CfPRX in hemocyte. These results indicated that CfPRX was a constitutive and inducible acute-phase protein which was involved in the immune resistance to L. anguillarum stimulation.

引用

页码：1451 / 1459

页数：9

共 56 条

[51] Spliced leader RNA trans-splicing in dinoflagellates [J].

Zhang, Huan ;

Hou, Yubo ;

Miranda, Lilibeth ;

Campbell, David A. ;

Sturm, Nancy R. ;

Gaasterland, Terry ;

Lin, Senjie .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (11) :4618-4623

[52] Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2 [J].

Zhang, P ;

Liu, B ;

Kang, SW ;

Seo, MS ;

Rhee, SG ;

Obeid, LM .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1997, 272 (49) :30615-30618

[53] Molecular cloning, expression of a peroxiredoxin gene in Chinese shrimp Fenneropenaeus chinensis and the antioxidant activity of its recombinant protein [J].

Zhang, Qingli ;

Li, Fuhua ;

Zhang, Jiquan ;

Wang, Bing ;

Gao, Hongwei ;

Huang, Bingxin ;

Jiang, Hao ;

Xiang, Jianhai .

MOLECULAR IMMUNOLOGY, 2007, 44 (14) :3501-3509

[54]

Zhang X, 1999, J UNIV SCI TECHNOL B, V6, P47

[55] Construction and characterization of two bacterial artificial chromosome libraries of Zhikong scallop, Chlamys farreri Jones et Preston, and identification of BAC clones containing the genes involved in its innate immune system [J].

Zhang, Yang ;

Zhang, Xiaojun ;

Scheuring, Chantel F. ;

Zhang, Hong-Bin ;

Huan, Pin ;

Li, Fuhua ;

Xiang, Jianhai .

MARINE BIOTECHNOLOGY, 2008, 10 (04) :358-365

[56] Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis [J].

Zhou, Y ;

Kok, KH ;

Chun, ACS ;

Wong, CM ;

Wu, HW ;

Lin, MCM ;

Fung, PCW ;

Kung, HF ;

Jin, DY .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2000, 268 (03) :921-927

← 1 2 3 4 5 6 →