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| Main Authors: | , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Biology
2025
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| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40906129/ |
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| _version_ | 1868266157464616960 |
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| author | Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao |
| author_facet | Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao |
| collection | PubMed - marine biology |
| contents | HSP90's Function Under Low Temperature Stress. Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao Molecular chaperones, especially heat shock proteins (HSPs) have vital functions in cells' responses to stress. Here, we cloned and sequenced the complete complementary DNA encoding HSP90 () from the shrimp . The cDNA comprised 3162 bp, including a 2172 bp coding region encoding a 724 amino acid-protein (predicted molecular mass = 83.12 kDa). Homology and phylogenetic analyses showed that MjHSP90 was highly conserved and most homologous to HSP90. is expressed in all tested tissues, with high expression in gill tissue and the hepatopancreas. Cold stress significantly upregulated expression in the gill and hepatopancreas ( < 0.05). Following RNA interference knockdown of , the cold stress-related death rate of the shrimp increased significantly, accompanied by significantly upregulated expression of apoptosis-related genes and ( < 0.05) and an increase in the number of apoptotic cells. The results indicated that might play a pivotal role in the shrimp's immune response to cold stress. |
| format | Artículo científico |
| id | pubmed_40906129 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Biology |
| record_format | pubmed |
| spellingShingle | HSP90's Function Under Low Temperature Stress. Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao HSP90's Function Under Low Temperature Stress. Bian, Xueqiong Ren, Xianyun Jia, Shaoting Gao, Tian Wang, Junxia Wang, Jiajia Liu, Ping Li, Jian Li, Jitao Molecular chaperones, especially heat shock proteins (HSPs) have vital functions in cells' responses to stress. Here, we cloned and sequenced the complete complementary DNA encoding HSP90 () from the shrimp . The cDNA comprised 3162 bp, including a 2172 bp coding region encoding a 724 amino acid-protein (predicted molecular mass = 83.12 kDa). Homology and phylogenetic analyses showed that MjHSP90 was highly conserved and most homologous to HSP90. is expressed in all tested tissues, with high expression in gill tissue and the hepatopancreas. Cold stress significantly upregulated expression in the gill and hepatopancreas ( < 0.05). Following RNA interference knockdown of , the cold stress-related death rate of the shrimp increased significantly, accompanied by significantly upregulated expression of apoptosis-related genes and ( < 0.05) and an increase in the number of apoptotic cells. The results indicated that might play a pivotal role in the shrimp's immune response to cold stress. |
| title | HSP90's Function Under Low Temperature Stress. |
| url | https://pubmed.ncbi.nlm.nih.gov/40906129/ |