热休克蛋白70在缺糖损伤的HeLa细胞中对Bax和Bcl-2以及Bax构象改变的影响

郝金玉;杨玲;刘晓宇;刘雯;左伋; 

解剖学报 ›› 2009, Vol. 40 ›› Issue (3) : 428-432.

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解剖学报 ›› 2009, Vol. 40 ›› Issue (3) : 428-432. DOI: 10.3969/j.issn.0529-1356.2009.03.017
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热休克蛋白70在缺糖损伤的HeLa细胞中对Bax和Bcl-2以及Bax构象改变的影响

  • 郝金玉1 ;杨玲1 ;刘晓宇1 ;刘雯1; 左伋1,2 * 

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Effect of heat shock protein 70 on the expression of Bax and Bcl-2 and the conformational change of Bax in glucose deprived HeLa cells

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Abstract

Objective To observe the effect of heat shock protein 70 (Hsp70) on apoptosis of HeLa cells induced by glucose deprivation and investigate the relationship between Hsp70 and the key proteins of apoptosis: Bcl-2 family members. Methods HeLa cells were stably transfected with the plasmid of pcDNA31(+)Hsp70 to establish the Hsp70 overexpressed cell model; Hsp70 normalexpression and overexpression cells cultured with glucose free medium to create stress models. Every detection had three parallel samples. MTT assay was applied to evaluate the cell viability; Hoechst 33258 and Giemsa stain were used to examine the rate of cell apoptosis. RT-PCR was used to determine the expression level of Bax and Bcl-2 and to calculate the ratio of Bax/Bcl-2; Immunofluorescence and immunocytochemistry were applied to examine the conformational change of Bax. Results Cell viability was increased and the rate of cell apoptosis was decreased in Hsp70 overexpression cells cultured with glucose free medium. At the same time, the expression of Bax and Bcl-2 and the conformational change of Bax were also inhibited by Hsp70. Conclusion Hsp7

关键词

缺糖 / 热休克蛋白70 / Bax / Bcl-2 / 荧光免疫法

Key words

Glucose deprivation / Heat shock protein 70 / Bax / Bcl-2 / Immunofluorescence

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郝金玉;杨玲;刘晓宇;刘雯;左伋; . 热休克蛋白70在缺糖损伤的HeLa细胞中对Bax和Bcl-2以及Bax构象改变的影响[J]. 解剖学报. 2009, 40(3): 428-432 https://doi.org/10.3969/j.issn.0529-1356.2009.03.017
Effect of heat shock protein 70 on the expression of Bax and Bcl-2 and the conformational change of Bax in glucose deprived HeLa cells[J]. Acta Anatomica Sinica. 2009, 40(3): 428-432 https://doi.org/10.3969/j.issn.0529-1356.2009.03.017
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