Heat Shock Protein Expression in Endotoxin Treated Renal Epithelial Cells

다국어 초록 (Multilingual Abstract)

Recent studies have reported that markedly increased concentrations of a number of different classes of protein are initially identified by the marked increase in their concentration in cells after various stresses including heat shock. In this study, putative interactions between apoptosis and heat-shock proteins disturbed by endotoxin as aseptic shock model were investigated. The direct cellular damages were assessed by the LDH release from the cytoplasm of the human tubular epithelial cells(HK-2 cells) after lipopolysaccharides(LPS) treatment. And the expressions of Bcl2 and BAX mRNA that had been employed as an index of apoptosis to assess by what extent apoptosis contributed to tubular cell damage and the expression of heat shock protein(HSP)90, 72 and 27 with the Bcl2/BAX ratio in septic shock model were studied also. LPS treatment let HK-2 cells release SDH markely(14.33+/-1.55 vs. 61.00+/- 2.65, p<0.01). LDH release was greater significantly from the cells that had not been heat preconditioned than that of heat preconditioned(61.00+/- 2.65vs. 41.33 +/- 3.21,p<0.05)
LPS treatment itself did not up-regulated Bcl2 significantly. But the expression of Bcl2 was marked with heat preconditioning. The expression of BAX was increased with LPS treatment but did not increase significantly with heat preconditioning(165% vs. 1496%).
We did not see any contribution of heat preconditioning on the expression of HSP90. HSP72 expression was slightly increased with LPS treatment. But the expression of HSP27 was more evident after preconditioning with LPS treatment HSP27 expression was evident after LPS treatment. This study showed that the heat preconditioning was able to provide protection on the human tubular epithlial cells from LPS treatment extensively. The protection from cytolytic damage and increase of Bcl2/BAX ratio was closely related with the increase of HSP72 and HSP27, especially with LPS treatment.