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Updated: Sep 9, 2025

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
Published on: January 20, 2023
Marsupenaeus japonicus HSP90's Function Under Low Temperature Stress
Xueqiong Bian1,2,3, Xianyun Ren1,2, Shaoting Jia1,2
1State Key Laboratory of Mariculture Biobreeding and Sustainable Goods, Yellow Sea Fisheries Research Institute, Chinese Academy of Fishery Sciences, Qingdao 266071, China.
Heat shock protein 90 (HSP90) in the shrimp Marsupenaeus japonicus is crucial for surviving cold stress. Its reduced expression increases mortality and apoptosis, highlighting its role in the shrimp immune response.
Area of Science:
- Molecular Biology
- Marine Biology
- Immunology
Background:
- Molecular chaperones, particularly heat shock proteins (HSPs), are essential for cellular stress responses.
- HSP90 is a critical chaperone involved in protein folding and cellular homeostasis.
Purpose of the Study:
- To clone and characterize the HSP90 gene (MjHSP90) from the shrimp Marsupenaeus japonicus.
- To investigate the role of MjHSP90 in the shrimp's response to cold stress and its involvement in apoptosis.
Main Methods:
- cDNA cloning and sequencing of MjHSP90.
- Homology and phylogenetic analyses.
- Gene expression analysis under cold stress using qPCR.
- RNA interference (RNAi) for gene knockdown.
- Apoptosis assays and analysis of apoptosis-related gene expression.
Main Results:
- The MjHSP90 cDNA sequence was determined, encoding a 724 amino acid protein.
- MjHSP90 expression was highest in gill and hepatopancreas tissues and significantly upregulated by cold stress.
- Knockdown of MjHSP90 increased shrimp mortality under cold stress and upregulated apoptosis-related genes (Mjcaspase-3, Mjbcl-2).
Conclusions:
- MjHSP90 plays a significant role in the immune response of Marsupenaeus japonicus to cold stress.
- The protein is involved in regulating apoptosis pathways during cold exposure.
- MjHSP90 is vital for shrimp survival under environmental stress conditions.
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