Regulation of Hsp90 on oxidative stress signal transduction pathway: HSP90 is an important molecular chaperone in heat shock proteins, and the interacting substrate protein is special. The sequential interaction between HSP90 and substrate protein may be the basis of its protective effect. HSP90 can be used as a powerful tool to study the interaction of different signal pathways under oxidative stress and to screen key unknown signal protein molecules in oxidative stress adaptation pathways. Real-time fluorescent protein labeling was used to monitor oxidative stress, and quantitative protein proteomics (SILAC) labeling mass spectrometry was used to compare the changes of substrate protein spectrum. Combined with bioinformatics analysis, the cross-regulation of HSP90 on cell network pathway under different oxidative stress conditions was discussed. This will help to clarify the molecular mechanism of oxidative stress and lay a theoretical foundation for exploring the mechanism, treatment and prevention of related diseases.

Representative Papers: Chen Xuemei, Kang Hongyun, Zou Fei. Role of tubulin and heat shock protein 90 in oxidative stress preconditioning. China Journal of Pathophysiology. 2009; 25( 1): 104- 106.

Research topic:

1, protein spectrum and signal network regulation of heat shock protein 90 interaction in oxidative stress (No.30500580) The balance of the National Natural Science Foundation in 2006-2008 was 50,000.

2. Cross-regulation of heat shock protein 90 on oxidative stress signal transduction pathway (No.05300465) Guangdong Natural Science Foundation

3. The quality control mechanism of 3.Hsp90 on proteins related to cell cycle arrest induced by oxidative stress. The fund project of Guangdong Academy of Educational Sciences (approval number GW20 10XX) is 60,000 yuan. Total disposable funds at present: 1 10000.