Effects of sodium salicylate on the expression of HSP27 protein during oxidative stress in tissue-cultured human lens epithelial cells

Zhi Wang , Yanli Zhou

Current Medical Science ›› 2006, Vol. 26 ›› Issue (36) : 753 -755.

PDF
Current Medical Science ›› 2006, Vol. 26 ›› Issue (36) : 753 -755. DOI: 10.1007/s11596-006-0636-y
Article

Effects of sodium salicylate on the expression of HSP27 protein during oxidative stress in tissue-cultured human lens epithelial cells

Author information +
History +
PDF

Abstract

The effects of sodium salicylate on the expression of heat shock protein 27 (HSP27) during oxidative stress in tissue-cultured human lens epithelial cells were investigated. Cultured human lens epithelial cells (HLB-3) were divided into 3 groups: control group (group A), oxidation injury group (group B) and sodium salicylate group (group C). Apoptosis of human lens epithelial cells cultured in vitro was induced in the presence of 150 μmol/L H2O2. Cells viability and the expression of HSP27 were analyzed. Viability of the cells was measured by methyl thiazole tetrazolium (MTT) chromatometry. The expression of HSP27 in HLB-3 cells was detected by using immunohistochemistry and image analysis system. Sodium salicylate could induce the expression of HSP27, and the cells viability in group C was significantly higher than in group B (0.2667±0.01414 vs 0.2150±0.01080, P=0.012<0.05). The average gray value of HSP27 in group B was less than that in group C (P=0.000<0.05). The increased expression of HSP27 by sodium salicylate might play an important role in the protection of hydrogen peroxide-induced injury of human lens epithelial cells, suggesting that sodium salicylate could suppress, at least in part, the apoptosis of human lens epithelial cells.

Keywords

apoptosis / human lens epithelial cells / heat shock protein 27 / sodium salicylate / hydrogen peroxide

Cite this article

Download citation ▾
Zhi Wang, Yanli Zhou. Effects of sodium salicylate on the expression of HSP27 protein during oxidative stress in tissue-cultured human lens epithelial cells. Current Medical Science, 2006, 26(36): 753-755 DOI:10.1007/s11596-006-0636-y

登录浏览全文

4963

注册一个新账户 忘记密码

References

[1]

BagchiM., KatarM., MaiselH.. Effect of exogenous stress on the tissue-cultured mouse lens epithelial cells. J Cell Biochem, 2002, 86(2): 302-306

[2]

RaberghC. M., AiraksinenS., SoitamoA., et al.. Tissue-specific expression of zebrafish (Daniorerio) heat shock factor 1 mRNAs in response to heat stress. J Exp Biol, 2000, 203(12): 177-181

[3]

BukanB., DewerlingE., PfundC., et al.. Getting newly synthesized proteins into shape. Cell, 2000, 101: 119-122

[4]

FinkA. L.. Chaperone-mediated protein folding. Physiol Rev, 1999, 79(2): 425-449

[5]

KamradtM. C., ChenF., SamS., et al.. The small heat shock protein alpha B-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J Biol Chem, 2002, 2(41): 38 731-38 736

[6]

HorwitzJ.. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA, 1992, 89: 10 449-10 453

[7]

BagchiM., KatarM., MaiselH.. Heat shock proteins of adult and embryonic human ocular lenses. J Cell Biochem, 2002, 84: 278-284

[8]

JianT.. Progress on pathogenesis of cataract. J Yanke Xinjinzhan (Chinese), 2003, 23(1): 52-55

[9]

MorrisonL. E., HooverH. E., ThueraufD. J., et al.. Mimicking phosphorylation alphaB-crystallin on serine-59 is necessary and sufficient to provide maximal protection of cardiac myocytes from apoptosis. Circ Res, 2003, 92(2): 203-211

[10]

BuL., JinY. P., ShiY. F., et al.. Mutant DNA-binding domain of HSF 4 is associated with autosomal dominant lamellar and Marner cataract. Nat Genet, 2002, 31(7): 1-3

[11]

StruckH. G., HeiderC., LautenschagerC.. Changes in the lens epithelium of diabetic and non-diabetic patients with various forms of opacities in senile cataract. Klim Monatsbl Augenheilkd, 2000, 216(4): 204-209

AI Summary AI Mindmap
PDF

89

Accesses

0

Citation

Detail

Sections
Recommended

AI思维导图

/