Document Detail


Molecular cloning of heat shock protein 60 (PtHSP60) from Portunus trituberculatus and its expression response to salinity stress.
MedLine Citation:
PMID:  22434146     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Heat shock protein 60 (HSP60) is a highly conserved and multi-functional molecular chaperone that plays an essential role in both cellular metabolism and stress response. Portunus trituberculatus is an important marine fishery and aquaculture species, and water salinity condition influenced its artificial propagations significantly. In order to investigate the function of P. trituberculatus HSP60 against osmotic stress, P. trituberculatus HSP60 gene was firstly cloned. The full-length cDNA of PtHSP60 contains 1,743 nucleotides encoding 577 amino acids with a calculated molecular weight of 61.25 kDa. Multiple alignments indicated that the deduced amino acid sequences of PtHSP60 shared a high level of identity with invertebrate and vertebrate HSP60 sequence including shrimp, fruit fly, zebrafish, and human. The expression profiles of PtHSP60 at mRNA and protein levels under salinity treatment were investigated by semi-quantitative reverse transcriptase-polymerase chain reaction (RT-PCR) and Western blot analysis, respectively. It was found that the mRNA transcripts of PtHSP60 gene varied among different tissues under normal salinity conditions, and the antennal gland showed the highest expression level among the tissues tested. As for low salinity challenge, the mRNA expression of PtHSP60 gene was higher in the gill and appendicular muscle compared with other tissues, and gill and hypodermis represented the higher gene expressions during the hyperosmotic stress, which indicated that those tissues were salinity-sensitive tissues. In addition, salinity challenges significantly altered the expression of PtHSP60 at mRNA and protein level in a salinity- and time-dependent manner in P. trituberculatus gill tissue. The results indicate that PtHSP60 played important roles in mediating the salinity stress in P. trituberculatus.
Authors:
Qianghua Xu; Ye Qin
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-03-22
Journal Detail:
Title:  Cell stress & chaperones     Volume:  17     ISSN:  1466-1268     ISO Abbreviation:  Cell Stress Chaperones     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-07-26     Completed Date:  2012-11-27     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  9610925     Medline TA:  Cell Stress Chaperones     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  589-601     Citation Subset:  IM    
Affiliation:
Key Laboratory of Sustainable Exploitation of Oceanic Fisheries Resources, Ministry of Education, College of Marine Sciences, Shanghai Ocean University, Lingang New Harbor, People's Republic of China. qhxu@shou.edu.cn
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Brachyura / classification,  genetics*,  metabolism*
Chaperonin 60 / genetics,  metabolism*
Cloning, Molecular
Molecular Sequence Data
Phylogeny
Salinity*
Sequence Alignment
Stress, Physiological*
Up-Regulation / drug effects
Chemical
Reg. No./Substance:
0/Chaperonin 60
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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