Literature DB >> 21484287

The molecular characterization and expression of heat shock protein 90 (Hsp90) and 26 (Hsp26) cDNAs in sea cucumber (Apostichopus japonicus).

Huan Zhao1, Hongsheng Yang, Heling Zhao, Muyan Chen, Tianming Wang.   

Abstract

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.

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Year:  2011        PMID: 21484287      PMCID: PMC3156262          DOI: 10.1007/s12192-011-0260-z

Source DB:  PubMed          Journal:  Cell Stress Chaperones        ISSN: 1355-8145            Impact factor:   3.667


  36 in total

Review 1.  Mammalian stress response: cell physiology, structure/function of stress proteins, and implications for medicine and disease.

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Journal:  Physiol Rev       Date:  1992-10       Impact factor: 37.312

2.  The mitochondrial 60-kDa heat shock protein in marine invertebrates: biochemical purification and molecular characterization.

Authors:  Omer Choresh; Yossi Loya; Werner E G Müller; Jörg Wiedenmann; Abdussalam Azem
Journal:  Cell Stress Chaperones       Date:  2004-03       Impact factor: 3.667

Review 3.  Structure and mechanism of the Hsp90 molecular chaperone machinery.

Authors:  Laurence H Pearl; Chrisostomos Prodromou
Journal:  Annu Rev Biochem       Date:  2006       Impact factor: 23.643

Review 4.  Heat-shock protein 90, a chaperone for folding and regulation.

Authors:  D Picard
Journal:  Cell Mol Life Sci       Date:  2002-10       Impact factor: 9.261

Review 5.  Stress proteins in aquatic organisms: an environmental perspective.

Authors:  B M Sanders
Journal:  Crit Rev Toxicol       Date:  1993       Impact factor: 5.635

Review 6.  Role of the major heat shock proteins as molecular chaperones.

Authors:  C Georgopoulos; W J Welch
Journal:  Annu Rev Cell Biol       Date:  1993

7.  Cloning of an orange-spotted grouper Epinephelus coioides heat shock protein 90AB (HSP90AB) and characterization of its expression in response to nodavirus.

Authors:  Young-Mao Chen; Cham-En Kuo; Ting-Yu Wang; Pei-Shiuan Shie; Wei-Chen Wang; Shao-Ling Huang; Tieh-Jung Tsai; Peng-Peng Chen; Jiann-Chu Chen; Tzong-Yueh Chen
Journal:  Fish Shellfish Immunol       Date:  2010-02-11       Impact factor: 4.581

8.  Identification and expression of a small heat shock protein in two lines of the endoparasitic wasp Venturia canescens.

Authors:  A Reineke
Journal:  Comp Biochem Physiol A Mol Integr Physiol       Date:  2005-05       Impact factor: 2.320

9.  Identification of the small heat shock protein, HSP21, of shrimp Penaeus monodon and the gene expression of HSP21 is inactivated after white spot syndrome virus (WSSV) infection.

Authors:  Po-Yu Huang; Shih-Ting Kang; Wei-Yu Chen; Tai-Ching Hsu; Chu-Fang Lo; Kuan-Fu Liu; Li-Li Chen
Journal:  Fish Shellfish Immunol       Date:  2008-06-18       Impact factor: 4.581

10.  DNA binding of heat shock factor to the heat shock element is insufficient for transcriptional activation in murine erythroleukemia cells.

Authors:  J O Hensold; C R Hunt; S K Calderwood; D E Housman; R E Kingston
Journal:  Mol Cell Biol       Date:  1990-04       Impact factor: 4.272

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  5 in total

1.  Expression analysis of immune related genes identified from the coelomocytes of sea cucumber (Apostichopus japonicus) in response to LPS challenge.

Authors:  Ying Dong; Hongjuan Sun; Zunchun Zhou; Aifu Yang; Zhong Chen; Xiaoyan Guan; Shan Gao; Bai Wang; Bei Jiang; Jingwei Jiang
Journal:  Int J Mol Sci       Date:  2014-10-27       Impact factor: 5.923

2.  Understanding the Heat Shock Response in the Sea Cucumber Apostichopus japonicus, Using iTRAQ-Based Proteomics.

Authors:  Dongxue Xu; Lina Sun; Shilin Liu; Libin Zhang; Hongsheng Yang
Journal:  Int J Mol Sci       Date:  2016-02-04       Impact factor: 5.923

3.  An optimized, broadly applicable piggyBac transposon induction system.

Authors:  Zongtai Qi; Michael Nathaniel Wilkinson; Xuhua Chen; Sumithra Sankararaman; David Mayhew; Robi David Mitra
Journal:  Nucleic Acids Res       Date:  2017-04-20       Impact factor: 16.971

4.  Lysine Acetylation is an Important Post-Translational Modification that Modulates Heat Shock Response in the Sea Cucumber Apostichopus japonicus.

Authors:  Dongxue Xu; Xuan Wang
Journal:  Int J Mol Sci       Date:  2019-09-09       Impact factor: 5.923

5.  Heat stress-induced HSP90 expression is dependent on ERK and HSF1 activation in turbot (Scophthalmus maximus) kidney cells.

Authors:  Shuangshuang Yang; Tingting Zhao; Aijun Ma; Zhihui Huang; Jingkun Yang; Chenhao Yuan; Xiaoli Guo; Chunyue Zhu
Journal:  Cell Stress Chaperones       Date:  2020-10-06       Impact factor: 3.667

  5 in total

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