Expression of Cu/Zn SOD Protein Is Suppressed in hsp 70.1 Knockout Mice

Choi, S-Mi; Park, Kyung-Ae; Lee, Hee Joo; Park, Myoung Sook; Lee, Joung Hee; Park, Kyoung Chan; Kim, Manho; Lee, Seung‐Hoon; Seo, Jong-Soo; Yoon, Byung‐Woo

doi:10.5483/bmbrep.2005.38.1.111

Cited by 30 publications

(23 citation statements)

References 25 publications

(29 reference statements)

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“…GPx and GR are both the major regulating enzymes in the glutathione antioxidant system. Superoxide dismutase activities were significantly decreased in hsp 70.1 knock-out mice than in the wild-type littermates (Choi et al 2005). The present study showed that hydrogen peroxide-induced superoxide accumulation is decreased by heat-shock response.…”

Section: Discussionmentioning

confidence: 93%

Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance

Chiu

Tsao

Yang

2009

Cell Stress and Chaperones

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The present study was designed to investigate ex vivo the protective mechanisms of heat-shock response against H 2 O 2 -induced oxidative stress in peripheral blood mononuclear cells (PBMCs) of rats. Twenty-four hours later, heat-shock treatment was executed in vivo; rat PBMCs were collected and treated with H 2 O 2 . The accumulation of reactive oxygen species and the mitochondrial membrane potential were evaluated by intracellular fluorescent dHE and JC-1 dye staining, respectively, and expression of HSP72 and cytochrome c was detected by Western blot analysis. Cellular apoptosis was assayed by TUNEL staining and double staining of Annexin V and PI. The results showed that H 2 O 2 -induced oxidative stress leads to intracellular superoxide accumulation and collapse of the mitochondrial membrane potential in rat PBMCs. Moreover, cellular apoptosis was detected after H 2 O 2 treatment, and the release of mitochondrial cytochrome c from mitochondria to cytosol was significantly enhanced. Heat-shock pretreatment decreases the accumulation of intracellular superoxide in PBMCs during H 2 O 2 -induced oxidative stress. Moreover, heat-shock treatment prevents the collapse of the mitochondrial membrane potential and cytochrome c release from mitochondria during H 2 O 2 -induced oxidative stress. In conclusion, mitochondria are critical organelles of the protective effects of heat-shock treatment. Cellular apoptosis during H 2 O 2 -induced oxidative stress is decreased by heat-shock treatment through a decrease in superoxide induction and preservation of the mitochondrial membrane potential.

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Section: Discussionmentioning

confidence: 93%

Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance

Chiu

Tsao

Yang

2009

Cell Stress and Chaperones

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“…Therefore, the higher post-ischemic expression of HSP-27 and -72 in WHWadministered mice may account for the reduced inflammatory responses, disruption of cytoskeleton in the tubular epithelium, and oxidative stress (Park et al, 2001Vayssier and Polla, 1998;Kelly, 2005;Huot et al, 1996). Choi et al found that deletion of hsp 70.1 gene in mice decreased the activity and expression of both CuZnSOD and MnSOD, indicating that HSP-70 is involved in regulation of oxidative stress (Choi et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Wen-pi-tang-Hab-Wu-ling-san attenuates kidney ischemia/reperfusion injury in mice

Seok

Kim

Choi

et al. 2007

Journal of Ethnopharmacology

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“…Newly synthesized proteins in the cytosol destined to mitochondria interact with chaperones in the cytosol, which include HSP90 and HSP70 (18,27,38,45,51). Previous studies have shown that the activity of both SOD-1 and SOD-2 was significantly decreased in HSP70.1 knockout mice compared with the wildtype littermates (17). However, the nature of this interaction between SOD-2 and its chaperone remains unknown.…”

mentioning

confidence: 94%

Inducible HSP70 regulates superoxide dismutase-2 and mitochondrial oxidative stress in the endothelial cells from developing lungs

Afolayan

Teng

Eis

et al. 2014

American Journal of Physiology-Lung Cellular and Molecular Phys

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is synthesized in the cytosol and imported into the mitochondrial matrix, where it is activated and functions as the primary antioxidant for cellular respiration. The specific mechanisms that target SOD-2 to the mitochondria remain unclear. We hypothesize that inducible heat shock protein 70 (iHSP70) targets SOD-2 to the mitochondria via a mechanism facilitated by ATP, and this process is impaired in persistent pulmonary hypertension of the newborn (PPHN). We observed that iHSP70 interacts with SOD-2 and targets SOD-2 to the mitochondria. Interruption of iHSP70-SOD-2 interaction with 2-phenylethylenesulfonamide-(PFT-, a specific inhibitor of substrate binding to iHSP70 COOH terminus) and siRNA-mediated knockdown of iHSP70 expression disrupted SOD-2 transport to mitochondria. Increasing intracellular ATP levels by stimulation of respiration with CaCl 2 facilitated the mitochondrial import of SOD-2, increased SOD-2 activity, and decreased the mitochondrial superoxide (O 2 ·Ϫ ) levels in PPHN pulmonary artery endothelial cells (PAEC) by promoting iHSP70-SOD-2 dissociation at the outer mitochondrial membrane. In contrast, oligomycin, an inhibitor of mitochondrial ATPase, decreased SOD-2 expression and activity and increased O 2 ·Ϫ levels in the mitochondria of control PAEC. The basal ATP levels and degree of iHSP70-SOD-2 dissociation were lower in PPHN PAEC and lead to increased SOD-2 degradation in cytosol. In normal pulmonary arteries (PA), PFT-impaired the relaxation response of PA rings in response to nitric oxide (NO) donor, S-nitroso-N-acetyl-penicillamine. Pretreatment with Mito-Q, a mitochondrial targeted O 2 ·Ϫ scavenger, restored the relaxation response in PA rings pretreated with PFT-. Our observations suggest that iHSP70 chaperones SOD-2 to the mitochondria. Impaired SOD-2-iHSP70 dissociation decreases SOD-2 import and contributes to mitochondrial oxidative stress in PPHN.persistent pulmonary hypertension of the newborn; pulmonary artery endothelium; oxidative stress; vasodilation; nitric oxide OXIDATIVE STRESS PLAYS A KEY ROLE in the pathogenesis of pulmonary hypertension (14, 41a). Persistent pulmonary hypertension of the newborn (PPHN) is associated with increased generation of reactive oxygen species (ROS), including superoxide radical (O 2 ·Ϫ ) (10). ROS induces pulmonary vascular remodeling, which leads to increased vascular resistance and impaired pulmonary vasodilation in PPHN (46). Studies in a fetal lamb model of PPHN induced by prenatal constriction of the ductus arteriosus have previously identified increased NA-DPH oxidase activity and uncoupling of endothelial nitric oxide synthase (eNOS) as the major sources of O 2 ·Ϫ in the cytosol (10,33,36 ·Ϫ generation in the mitochondria, which in turn plays a major role in the toxicity of hyperoxia (44). Newborns are at risk of experiencing oxidative stress because O 2 concentrations increase by several times at birth compared with in utero environment. Adaptive increases in cellular antioxidant defenses, particularly superoxide dismutases (SODs), du...

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Expression of Cu/Zn SOD Protein Is Suppressed in hsp 70.1 Knockout Mice

Cited by 30 publications

References 25 publications

Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance

Heat-shock response protects peripheral blood mononuclear cells (PBMCs) from hydrogen peroxide-induced mitochondrial disturbance

Wen-pi-tang-Hab-Wu-ling-san attenuates kidney ischemia/reperfusion injury in mice

Inducible HSP70 regulates superoxide dismutase-2 and mitochondrial oxidative stress in the endothelial cells from developing lungs

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