Mammalian Small Stress Proteins Protect against Oxidative Stress through Their Ability to Increase Glucose-6-phosphate Dehydrogenase Activity and by Maintaining Optimal Cellular Detoxifying Machinery

Préville, Xavier; Salvemini, Francesca; Giraud, Stéphane; Chaufour, Sylvain; Paul, Catherine; Stepien, Georges; Ursini, Matilde Valeria; Arrigo, André‐Patrick

doi:10.1006/excr.1998.4347

Cited by 271 publications

(220 citation statements)

References 94 publications

Supporting

Mentioning

194

Contrasting

Unclassified

Order By: Relevance

“…through several possible mechanisms (22). This information led us to hypothesize that down-regulation of Hsp27 may lead to decreased GSH levels and that this decrease may affect 17-AAG sensitivity.…”

Section: Resultsmentioning

confidence: 99%

“…Those studies have shown that Hsp27 expression increases survival after TNF-a treatment while lowering intracellular oxidative species (21). Depletion of GSH by buthionine sulfoximine (BSO), a compound that binds g-glutamylcysteinyl synthase and causes GSH production inhibition, showed that Hsp27 does not block TNF-a-induced cell death through another mechanism (22). More recent studies have shown that Hsp27 participates in regulation of several detoxifying enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…More recent studies have shown that Hsp27 participates in regulation of several detoxifying enzymes. In particular, Hsp27 overexpression increases expression and activity of glucose-6-phosphate dehydrogenase, an enzyme that functions to reduce NADP + during cellular recycling and reduction of GSH (22). Other detoxifying enzymes also have increased activity due to overexpression of Hsp27, such as glutathione-S-transferase and glutathione reductase, and Hsp27 expression serves to protect the activity of these enzymes after exposure to hydrogen peroxide (22).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Up-regulation of Heat Shock Protein 27 Induces Resistance to 17-Allylamino-Demethoxygeldanamycin through a Glutathione-Mediated Mechanism

McCollum¹,

TenEyck

Sauer³

et al. 2006

Cancer Research

151

152

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Up-regulation of Heat Shock Protein 27 Induces Resistance to 17-Allylamino-Demethoxygeldanamycin through a Glutathione-Mediated Mechanism

McCollum¹,

TenEyck

Sauer³

et al. 2006

Cancer Research

151

152

View full text Add to dashboard Cite

show abstract

“…Perhaps also related to chaperone functions, studies of Ding and Keller (2001) have suggested that Hsp might act to preserve proteasome function that is otherwise inhibited by oxidative stress. Protective functions of the small heat shock proteins have been linked to their ability to decrease the intracellular level of ROS by modulating metabolism of glutathione to maintain it in a reduced state (Arrigo, 1998;Preville et al, 1999;Baek et al, 2000). Another way in which Hsp may act to promote survival and prevent cell death is through suppression of other apoptotic signaling pathways.…”

Section: How Do Hsp Protect Cells Against Oxidative Damage?mentioning

confidence: 99%

Cellular response to oxidative stress: Signaling for suicide and survival*

Martindale

Holbrook

2002

Journal Cellular Physiology

2,089

1,596

View full text Add to dashboard Cite

Reactive oxygen species (ROS), whether produced endogenously as a consequence of normal cell functions or derived from external sources, pose a constant threat to cells living in an aerobic environment as they can result in severe damage to DNA, protein, and lipids. The importance of oxidative damage to the pathogenesis of many diseases as well as to degenerative processes of aging has becoming increasingly apparent over the past few years. Cells contain a number of antioxidant defenses to minimize fluctuations in ROS, but ROS generation often exceeds the cell's antioxidant capacity, resulting in a condition termed oxidative stress. Host survival depends upon the ability of cells and tissues to adapt to or resist the stress, and repair or remove damaged molecules or cells. Numerous stress response mechanisms have evolved for these purposes, and they are rapidly activated in response to oxidative insults. Some of the pathways are preferentially linked to enhanced survival, while others are more frequently associated with cell death. Still others have been implicated in both extremes depending on the particular circumstances. In this review, we discuss the various signaling pathways known to be activated in response to oxidative stress in mammalian cells, the mechanisms leading to their activation, and their roles in influencing cell survival. These pathways constitute important avenues for therapeutic interventions aimed at limiting oxidative damage or attenuating its sequelae. Published 2002 Wiley‐Liss, Inc.

show abstract

“…The most important function of sHsps is that they can inhibit the aggregation of incorrectly folded proteins by binding to non-native proteins, and maintain them in a refolding-competent state (Haslbeck and Buchner 2002). Moreover, they also have anti-apoptotic and antioxidant activities and can bind to the actin cytoskeleton and stabilize it (Arrigo et al 2002, Preville et al 1999, Wang and Spector 1996.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Tóth

Szegedi

Varga

et al. 2013

Cell Stress and Chaperones

View full text Add to dashboard Cite

Hsp27 belongs to the small heat shock protein family, which are ATP-independent chaperones. The most important function of Hsp27 is based on its ability to bind non-native proteins and inhibit the aggregation of incorrectly folded proteins maintaining them in a refolding-competent state. Additionally, it has anti-apoptotic and antioxidant activities. To study the effect of Hsp27 on memory and synaptic functions, amyloid-β (Aβ) accumulation, and neurodegeneration, we generated transgenic mice overexpressing human Hsp27 protein and crossed with APPswe/PS1dE9 mouse strain, a mouse model of Alzheimer's disease (AD). Using different behavioral tests, we found that spatial learning was impaired in AD model mice and was rescued by Hsp27 overexpression. Electrophysiological recordings have revealed that excitability of neurons was significantly increased, and long-term potentiation (LTP) was impaired in AD model mice, whereas they were normalized in Hsp27 overexpressing AD model mice. Using anti-amyloid antibody, we counted significantly less amyloid plaques in the brain of APPswe/PS1dE9/Hsp27 animals compared to AD model mice. These results suggest that overexpression of Hsp27 protein might ameliorate certain symptoms of AD.

show abstract

Mammalian Small Stress Proteins Protect against Oxidative Stress through Their Ability to Increase Glucose-6-phosphate Dehydrogenase Activity and by Maintaining Optimal Cellular Detoxifying Machinery

Cited by 271 publications

References 94 publications

Up-regulation of Heat Shock Protein 27 Induces Resistance to 17-Allylamino-Demethoxygeldanamycin through a Glutathione-Mediated Mechanism

Up-regulation of Heat Shock Protein 27 Induces Resistance to 17-Allylamino-Demethoxygeldanamycin through a Glutathione-Mediated Mechanism

Cellular response to oxidative stress: Signaling for suicide and survival*

Overexpression of Hsp27 ameliorates symptoms of Alzheimer's disease in APP/PS1 mice

Contact Info

Product

Resources

About