scholarly journals Involvement of Nuclear Accumulation of Heat Shock Protein 27 in Leptomycin B-Induced Apoptosis in HeLa Cells

2005 ◽  
Vol 58 (12) ◽  
pp. 810-816 ◽  
Author(s):  
Ayako Tsuchiya ◽  
Etsu Tashiro ◽  
Minoru Yoshida ◽  
Masaya Imoto
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Heat Shock Protein 27 ◽  
Nuclear Accumulation ◽  
Leptomycin B ◽  
Induced Apoptosis

scholarly journals Anticancer Effects of LBA-ST Yogurt Supernatant on HeLa Cells via Heat Shock Protein 27 Decrease In Vitro

2017 ◽  
Vol 6 (1) ◽  
pp. 16
Author(s):  
Liziyyannida Liziyyannida ◽  
Wibi Riawan
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Short Chain Fatty Acids ◽  
Heat Shock Protein 27 ◽  
Lactobacillus Bulgaricus ◽  
Culture Cells ◽  
Response To Stress ◽  
And Migration

Heat Shock Protein 27 (Hsp27) is overexpressed in cervical cancer as a response to stress conditions. Hsp27 overexpression increase invasion, migration, and adhesion pathways of cancer cells. The Yogurt supernatant contains Short-Chain Fatty Acids (SCFA) include acetate, lactate, and butyrate which have anticancer activity. This study aimed to investigate supernatant of LBA-ST (Lactobacillusbulgaricus-acidophilus, Streptococcusthermophillus) Yogurt can decrease the expression of Hsp27 in HeLa culture cells. The mechanism on how supernatant yogurt inhibit invasion, migration, and adhesion was studied by immunocytochemistry. The data was then collected and analyzed using One-Way ANOVA. From this study, it can be concluded that the expression of proteins that play a role in invasion, adhesion, and migration of the Hsp27 was proven to be decreased (p< 0.05 ± 0.005).Keywords: HeLa cells, yogurt supernatant, Lactobacillus bulgaricus-acidophilus, Streptococcus thermophillus, Hsp27

scholarly journals Upregulation of heat shock protein 27 confers resistance to actinomycin D-induced apoptosis in cancer cells

FEBS Journal ◽  
2013 ◽  
Vol 280 (18) ◽  
pp. 4612-4624 ◽  
Author(s):  
Wenbo Ma ◽  
Yan Teng ◽  
Hui Hua ◽  
Jinlin Hou ◽  
Ting Luo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Actinomycin D ◽  
Heat Shock Protein 27 ◽  
Induced Apoptosis ◽  
Apoptosis In Cancer Cells

scholarly journals Inhibition of Daxx-Mediated Apoptosis by Heat Shock Protein 27

2000 ◽  
Vol 20 (20) ◽  
pp. 7602-7612 ◽  
Author(s):  
Steve J. Charette ◽  
Josée N. Lavoie ◽  
Herman Lambert ◽  
Jacques Landry
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Major Change ◽  
Heat Shock Protein 27 ◽  
Supramolecular Organization ◽  
Protective Function ◽  
Cellular Protection ◽  
Hsp27 Phosphorylation ◽  
Fas Pathway ◽  
Induced Apoptosis

ABSTRACT Heat shock protein 27 (HSP27) confers cellular protection against a variety of cytotoxic stresses and also against physiological stresses associated with growth arrest or receptor-mediated apoptosis. Phosphorylation modulates the activity of HSP27 by causing a major change in the supramolecular organization of the protein, which shifts from oligomers to dimers. Here we show that phosphorylated dimers of HSP27 interact with Daxx, a mediator of Fas-induced apoptosis, preventing the interaction of Daxx with both Ask1 and Fas and blocking Daxx-mediated apoptosis. No such inhibition was observed with an HSP27 phosphorylation mutant that is only expressed as oligomers or when apoptosis was induced by transfection of a Daxx mutant lacking its HSP27 binding domain. HSP27 expression had no effect on Fas-induced FADD- and caspase-dependent apoptosis. However, HSP27 blocked Fas-induced translocation of Daxx from the nucleus to the cytoplasm and Fas-induced Daxx- and Ask1-dependent apoptosis. The observations revealed a new level of regulation of the Fas pathway and suggest a mechanism for the phosphorylation-dependent protective function of HSP27 during stress and differentiation.

Small Heat Shock Protein 27 (HSP27) Associates with Tubulin/Microtubules in HeLa Cells

2000 ◽  
Vol 271 (1) ◽  
pp. 164-169 ◽  
Author(s):  
Mizuki Hino ◽  
Kazuki Kurogi ◽  
Masa-Aki Okubo ◽  
Maki Murata-Hori ◽  
Hiroshi Hosoya
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Small Heat Shock Protein ◽  
Heat Shock Protein 27
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