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Whole-body hyperthermia-induced thermotolerance is associated with the induction of Heat Shock Protein 70 in mice

Yueh-Tsu King, Chih-Sheng Lin, Jyh-Hung Lin and Wen-Chuan Lee*

Cardiovascular Research Center, Department of Comparative Medicine, Pig Research Institute Taiwan, PO Box 23, Chunan, Miaoli 35099, Taiwan, Republic of China



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Fig. 1. A representative immunoblot of HSP70 in mouse liver. Mice were preconditioned at 41°C for 30 min and then allowed to recover for 48 h. For one-dimensional gel electrophoresis, liver tissues of the mice from control (sham-treated; SC) or preconditioned (PC) groups were collected, processed and immunoblotted as described in Materials and methods. HSP90, HSP with a molecular mass of 90 kDa; HSP70, HSP with a molecular mass of 70 kDa.

 


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Fig. 2. Verification of HSP70 by 2D-PAGE and immunoblot analysis in mouse liver. Liver tissues from control (A,C) and preconditioned (B,D) mice were the same as those described in Fig. 1. Gel electrophoresis and immunoblotting are described in Materials and methods. Commassie Blue-stained gels (A,B) and immunoblots for HSP70i (C,D) are shown. Larger arrowheads indicate the HSP70i locations; smaller arrowheads indicate other members of the HSP70 family. IEF, isoelectrofocusing; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Molecular mass of the protein spots (in kDa) and the pH value for the range of IEF gels are indicated to the right and bottom, respectively.

 


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Fig. 3. Quantitation of HSP70i level in mouse liver. Liver tissue from control (sham-treated, SC; N=8) and preconditioned (PC; N=12) mice were the same as those described in Fig. 1. The procedures for performing immunoblotting and quantification of the HSP70i levels are described in Materials and methods. Levels of HSP70i in control and preconditioned tissues were significantly different (P<0.0001).

 





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