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• W2005207514 endingPage "1534" @default.
• W2005207514 startingPage "1527" @default.
• W2005207514 abstract "We investigated the effect of heat shock on cytochrome P-450 activity in rat hepatocytes and report a significant, selective, and time-dependent enhancement of cytochrome P-450 activity in heatshocked hepatocytes. Stable long-term cultures of rat hepatocytes were heat shocked (42.5°C) for 1 to 3 h and allowed to recover at 37°C. Cytochrome P-450-dependent ethoxyresorufin O-dealkylase (EROD) and benzyloxyresorufin O-dealkylase (BROD) activities were measured up to 48 h after heat shock treatment. In general, the optimal heat shock exposure time was between 2 and 3 h. BROD activity (induced by sodium phenobarbital) increased approximately 6-fold in hepatocytes heat shocked for 3 h in comparison with hepatocytes maintained at 37°C. EROD activity (induced by 3-methylcholanthrene) increased 2-fold on exposure to heat shock for 2 h. The expression of inducible heat shock proteins Hsp70 and Hsp32 was verified by Western immunoblot analyses. In the absence of the appropriate inducer, heat shock treatment did not enhance cytochrome P-450 activity. Furthermore, enhanced P-450 enzyme activity was delayed for heat-shocked hepatocytes. It is hypothesized that heat shock treatment attenuates the negative effects triggered by the addition of the toxic inducers and possibly stabilizes the levels of cytochrome P-450 proteins. These results suggest that heat shock treatment may be used to enhance the functionality of hepatocytes, specifically, in bioartificial liver assist devices." @default.
• W2005207514 created "2016-06-24" @default.
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• W2005207514 date "2005-09-01" @default.
• W2005207514 modified "2023-09-27" @default.
• W2005207514 title "Selective Enhancement of Cytochrome P-450 Activity in Rat Hepatocytes by in Vitro Heat Shock" @default.
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• W2005207514 doi "https://doi.org/10.1089/ten.2005.11.1527" @default.
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