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The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus)
Zhao, Huan1,2; Yang, Hongsheng1; Zhao, Heling1,2; Chen, Muyan3; Wang, Tianming1,2
2011-09-01
发表期刊CELL STRESS & CHAPERONES
ISSN1355-8145
卷号16期号:5页码:481-493
文章类型Article
摘要The heat shock proteins (HSPs) are a family of proteins whose expression is enhanced in response to environmental stressors. The Apostichopus japonicus hsp90 and hsp26 genes were cloned using expressed sequence tag and rapid amplification of cDNA ends techniques. The full-length cDNA of Aphsp90 and Aphsp26 contains 3,458 and 1,688 nucleotides encoding 720 and 236 amino acids, respectively. Multiple alignments indicated that the deduced amino acid sequences of ApHsp90 and ApHsp26 shared a high level of identity with Hsp90 and small SHPs (sHSPs) sequences of zebrafish, ant, acorn worms, etc., and shared identical structural features with Hsp90 and sHSPs. The expression profiles of these two genes under heat treatment were investigated by real-time quantitative PCR. It was found that the messenger RNA (mRNA) transcripts of the two A. japonicus genes varied among different tissues under normal conditions and heat shock, and that the mRNA expression of the two genes was higher in the intestine compared to other tissues. Heat shock significantly elevated the expression of Aphsp90 and Aphsp26 mRNA in a temperature- and time-dependent manner. The results indicate that Aphsp90 and Aphsp26 played important roles in mediating the environmental stress in A. japonicus.; The heat shock proteins (HSPs) are a family of proteins whose expression is enhanced in response to environmental stressors. The Apostichopus japonicus hsp90 and hsp26 genes were cloned using expressed sequence tag and rapid amplification of cDNA ends techniques. The full-length cDNA of Aphsp90 and Aphsp26 contains 3,458 and 1,688 nucleotides encoding 720 and 236 amino acids, respectively. Multiple alignments indicated that the deduced amino acid sequences of ApHsp90 and ApHsp26 shared a high level of identity with Hsp90 and small SHPs (sHSPs) sequences of zebrafish, ant, acorn worms, etc., and shared identical structural features with Hsp90 and sHSPs. The expression profiles of these two genes under heat treatment were investigated by real-time quantitative PCR. It was found that the messenger RNA (mRNA) transcripts of the two A. japonicus genes varied among different tissues under normal conditions and heat shock, and that the mRNA expression of the two genes was higher in the intestine compared to other tissues. Heat shock significantly elevated the expression of Aphsp90 and Aphsp26 mRNA in a temperature- and time-dependent manner. The results indicate that Aphsp90 and Aphsp26 played important roles in mediating the environmental stress in A. japonicus.
关键词Apostichopus Japonicus Hsp90 Hsp26 Mrna Expression Heat Shock
学科领域Cell Biology
DOI10.1007/s12192-011-0260-z
URL查看原文
收录类别SCI
语种英语
WOS记录号WOS:000293965500002
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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/337002/11719
专题海洋生态与环境科学重点实验室
作者单位1.Chinese Acad Sci, Key Lab Marine Ecol & Environm Sci, Inst Oceanol, Qingdao 266071, Shandong, Peoples R China
2.Grad Univ, Chinese Acad Sci, Beijing 100049, Peoples R China
3.Univ Calif Irvine, Dept Dev & Cell Biol, Irvine, CA 92697 USA
第一作者单位中国科学院海洋研究所
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Zhao, Huan,Yang, Hongsheng,Zhao, Heling,et al. The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus)[J]. CELL STRESS & CHAPERONES,2011,16(5):481-493.
APA Zhao, Huan,Yang, Hongsheng,Zhao, Heling,Chen, Muyan,&Wang, Tianming.(2011).The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus).CELL STRESS & CHAPERONES,16(5),481-493.
MLA Zhao, Huan,et al."The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus)".CELL STRESS & CHAPERONES 16.5(2011):481-493.
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