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| Content Provider | Springer Nature Link |
|---|---|
| Author | Miao An, Shu Dan Dan, Tu Pan, Zhang Chen, Long Wen Bin, Gu Zhong Kai, Zhou |
| Copyright Year | 2017 |
| Abstract | Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays important roles in modulating multiple cellular stress responses. In this study, full-length complementary DNA of hsp90 from the giant spiny frog Quasipaa spinosa (Qs) was first isolated and designated as Qshsp90. This gene consisted of 2801 nucleotides with a complete open reading frame of 2172 nucleotides encoding a putative protein of 724 amino acids. Sequence analysis revealed that QsHSP90 shared high similarity with other known HSP90 and belonged to a vertebrate HSP90β subtype. Tissue distribution analysis showed that Qshsp90 was present in all of the test tissues, and its expression in liver, skin and kidney was significantly up-regulated after heat shock for 3 or 6 h, while skin showed a prompt and durable response to such heat stress. Qshsp90 transcripts in kidney and liver also markedly increased in pathogen infection models such as Aeromonas hydrophila and polyinosinic polycytidylic acid. These results indicate that Qshsp90 may play critical roles in coping mechanisms for thermal stress, and may be involved in the immune response. |
| Starting Page | 251 |
| Ending Page | 258 |
| Page Count | 8 |
| File Format | |
| ISSN | 09199268 |
| Journal | Fisheries Science |
| Volume Number | 83 |
| Issue Number | 2 |
| e-ISSN | 14442906 |
| Language | English |
| Publisher | Springer Japan |
| Publisher Date | 2017-01-16 |
| Publisher Place | Tokyo |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Heat stress Aeromonas hydrophila Polyinosinic polycytidylic acid Fish & Wildlife Biology & Management Freshwater & Marine Ecology Food Science |
| Content Type | Text |
| Resource Type | Article |
| Subject | Aquatic Science |
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