tailieunhanh - Báo cáo khoa học: Inhibition of Hsp90 function delays and impairs recovery from heat shock

The induction of the heat shock response as well as its termination is auto-regulated by heat shock protein activities. In this study we have investi-gated whether Hsp90 functional protein levels influence the characteristics and duration of the heat shock response. Treatment of cells with several benzoquinone ansamycin inhibitors of Hsp90 (geldanamycin, herbimycin A) activated a heat shock response in the absence of heat shock, as reported previously. | iFEBS Journal Inhibition of Hsp90 function delays and impairs recovery from heat shock Roger F Duncan1 2 1 Department of Molecular Pharmacology and Toxicology University of Southern California Schoolof Pharmacy Los Angeles CA USA 2 Department of Molecular Microbiology and Immunology University of Southern California Schoolof Medicine Los Angeles CA USA Keywords geldanamycin heat shock herbimycin Hsp90 Hsp function Correspondence R. F. Duncan Schoolof Medicine Department of Molecular Microbiology and Immunology University of Southern California Schoolof Pharmacy Los Angeles CA USA Fax 1 323 442 1681 Tel 323 442 1449 E-mail rduncan@ Received 6 July 2005 accepted 1 7 August 2005 doi The induction of the heat shock response as well as its termination is autoregulated by heat shock protein activities. In this study we have investigated whether Hsp90 functional protein levels influence the characteristics and duration of the heat shock response. Treatment of cells with several benzoquinone ansamycin inhibitors of Hsp90 geldanamycin herbimycin A activated a heat shock response in the absence of heat shock as reported previously. Pretreatment of cells with the Hsp90 inhibitors significantly delayed the rate of restoration of normal protein synthesis following a brief heat shock. Concurrently the rate of Hsp synthesis and accumulation was substantially increased and prolonged. The cessation of heat shock protein synthesis did not occur until the levels of Hsp70 were substantially elevated relative to its standard threshold for autoregulation. The elevated levels of Hsps 22-28 the small Hsps and Hsp70 are not able to promote thermotolerance when Hsp90 activity is repressed by ansamycins rather a suppression of thermotolerance is observed. These results suggest that a multicomponent protein chaperone complex involving both Hsp90 and Hsp70 signals the cessation of heat shock protein synthesis the restoration of normal translation and .

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