ABSTRACT
<p><b>OBJECTIVE</b>To establish a heat stress adaptation model in mouse fibroblast cell line NIH-3T3, and analyze the effect of stress and adaptation on protein synthesis.</p><p><b>METHODS</b>A heat stress adaptation cell model was established by heat preconditioning at 42 degrees C for 20 min. The total proteins were separated from the cell lysate by two-dimensional electrophoresis (2-DE), and analyzed using PDQUEST software. The effect of heat stress and preconditioning on protein synthesis was studied, and the protein spots related to stress adaptation were identified by peptide mass fingerprinting (PMF).</p><p><b>RESULTS</b>The proteins with increased expressions in cells with heat stress but not prior preconditioning represented mostly proteins with low molecular mass, whereas in cells exposed to heat stress following heat preconditioning, the upregulated proteins showed a wide spectrum of relative molecular mass.</p><p><b>CONCLUSIONS</b>In stress condition, the cells tend to give priority to synthesis of proteins with small molecular mass. Preconditioning of the cells may increase the intracellular reserve of the protective proteins for protection against challenge with potential stress condition.</p>