Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia
Li, Fuhua1; Luan, Wei1,2; Zhang, Chengsong1,2; Zhang, Jiquan1; Wang, Bing1; Xie, Yusu1,2; Li, Shihao1,2; Xiang, Jianhai1
刊名CELL STRESS & CHAPERONES
2009-03-01
卷号14期号:2页码:161-172
关键词Heat Shock Protein 90 Fenneropenaeus Chinensis Heat Shock Hypoxia
ISSN号1355-8145
DOI10.1007/s12192-008-0069-6
文献子类Article
英文摘要Heat shock protein 90 (HSP90) works as a multi-functional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25A degrees C to 35A degrees C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.; Heat shock protein 90 (HSP90) works as a multi-functional chaperone and is involved in the regulation of many essential cellular pathways. In this study, we have identified a full-length complementary DNA (cDNA) of HSP90 (FcHSP90) from Chinese shrimp Fenneropenaeus chinensis. FcHSP90 full-length cDNA comprised 2,552 bp, including a 2,181-bp open reading frame encoding 726 amino acids. Both homology analyses using alignment with previously identified HSP90 and a phylogeny tree indicated that FcHSP90 was a cytoplasmic HSP90. Real-time reverse transcription polymerase chain reaction analysis revealed that FcHSP90 was ubiquitously expressed in all the examined tissues but with highest levels in ovary of F. chinensis. FcHSP90 mRNA levels were sensitively induced by heat shock (from 25A degrees C to 35A degrees C) and reached the maximum at 6 h during heat shock treatment. Under hypoxia conditions, FcHSP90 mRNA levels, in both hemocytes and gill, were induced at 2 h and depressed at 8 h during hypoxia stress. The assessment of FcHSP90 mRNA levels under heat shock and hypoxia stresses indicated that the transcription of FcHSP90 was very sensitive to heat shock and hypoxia, so we deduced that FcHSP90 might play very important roles for shrimp to cope with environmental stress.
学科主题Cell Biology
URL标识查看原文
语种英语
WOS记录号WOS:000263352800006
公开日期2010-12-22
内容类型期刊论文
源URL[http://ir.qdio.ac.cn/handle/337002/2947]  
专题海洋研究所_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 Sch, Beijing 100039, Peoples R China
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Li, Fuhua,Luan, Wei,Zhang, Chengsong,et al. Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia[J]. CELL STRESS & CHAPERONES,2009,14(2):161-172.
APA Li, Fuhua.,Luan, Wei.,Zhang, Chengsong.,Zhang, Jiquan.,Wang, Bing.,...&Xiang, Jianhai.(2009).Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia.CELL STRESS & CHAPERONES,14(2),161-172.
MLA Li, Fuhua,et al."Cloning of cytoplasmic heat shock protein 90 (FcHSP90) from Fenneropenaeus chinensis and its expression response to heat shock and hypoxia".CELL STRESS & CHAPERONES 14.2(2009):161-172.
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