Phospholipase A 2 activity, heat shock protein, and superoxide dismutase in rat remnant kidney

2000 ◽  
Vol 14 (2) ◽  
pp. 128-131 ◽  
Author(s):  
G. Dorsam ◽  
R. J. Krieg, Jr. ◽  
W. Chan ◽  
G. Ereso ◽  
K. -C. Lin ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Phospholipase A ◽  
Remnant Kidney ◽  
Phospholipase A 2

Phospholipase A 2 mRNA in remnant kidney is modulated by dietary alpha-tocopherol

1999 ◽  
Vol 3 (4) ◽  
pp. 250-253
Author(s):  
G. Dorsam ◽  
N. B. Kuemmerle ◽  
R. J. Krieg ◽  
R. C. Franson ◽  
J. C. M. Chan
Keyword(s):  
Alpha Tocopherol ◽  
Phospholipase A ◽  
Remnant Kidney ◽  
Phospholipase A 2

scholarly journals Heat Shock Protein 72 Enhances Manganese Superoxide Dismutase Activity During Myocardial Ischemia-Reperfusion Injury, Associated With Mitochondrial Protection and Apoptosis Reduction

Circulation ◽  
2002 ◽  
Vol 106 (12_suppl_1) ◽  
Author(s):  
Ken Suzuki ◽  
Bari Murtuza ◽  
Ivan A. Sammut ◽  
Najma Latif ◽  
Jay Jayakumar ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Manganese Superoxide Dismutase ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Heat Shock Protein 72 ◽  
Manganese Superoxide

Background Heat shock protein 72 (HSP72) is known to provide myocardial protection against ischemia-reperfusion injury by its chaperoning function. Target molecules of this effect are presumed to include not only structural proteins but also other self-preservation proteins. The details, however, remain unknown. Manganese superoxide dismutase (Mn-SOD) is an enzyme that preserves mitochondria, a key organelle for cellular respiration, from reperfusion injury and limits mitochondria-related apoptosis. We hypothesized that Mn-SOD would play a role in HSP72-mediated cardioprotection. Methods and Results Rat hearts were transfected with human HSP72 by intra-coronary infusion of Hemagglutinating Virus of Japan-liposome, resulting in global myocardial overexpression of HSP72. After ischemia-reperfusion injury, cardiac function (left ventricular systolic pressure, maximum dP/dt, minimum dP/dt, and coronary flow) was improved in the HSP72-transfected hearts compared with control-transfected ones, corresponding with less leakage of creatine kinase and mitochondrial aspartate aminotransferase. Postischemic Mn-SOD content and activity in the HSP72-transfected hearts were enhanced in comparison with the controls (content: 96.9±4.1 versus 85.5±2.5% to the preischemic level, P =0.038; activity: 93.9±2.2 versus 82.2±3.7%, P =0.022), associated with improved mitochondrial respiratory function (postischemic percent respiratory control index; NAD + -linked: 81.3±3.8 versus 18.5±4.4%; FAD-linked: 71.8±5.5 versus 20.7±5.3%, P <0.001). In addition, incidence of postischemic cardiomyocyte apoptosis was attenuated in the HSP72-transfected hearts (4.0±1.1 versus 10.3±3.3%, P =0.036), correlating with an increased Bcl-2 level and reduced up-regulation of caspase-3. Conclusions These data suggest that the enhanced Mn-SOD activity during ischemia-reperfusion injury, which is associated with mitochondrial protection and apoptosis reduction, is a possible mechanism of HSP72-induced cardioprotection.

scholarly journals Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS

2007 ◽  
Vol 102 (5) ◽  
pp. 1497-1505 ◽  
Author(s):  
Hirofumi Yamashita ◽  
Jun Kawamata ◽  
Katsuya Okawa ◽  
Rie Kanki ◽  
Tomoki Nakamizo ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein

scholarly journals Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function

2016 ◽  
Vol 292 (6) ◽  
pp. 2369-2378 ◽  
Author(s):  
Adeleye J. Afolayan ◽  
Maxwell Alexander ◽  
Rebecca L. Holme ◽  
Teresa Michalkiewicz ◽  
Ujala Rana ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Glutamic Acid ◽  
Heat Shock Protein 70 ◽  
Domain Mapping ◽  
Superoxide Dismutase 2

scholarly journals Systemic Response of Antioxidants, Heat Shock Proteins, and Inflammatory Biomarkers to Short-Lasting Exercise Training in Healthy Male Subjects

2021 ◽  
Vol 2021 ◽  
pp. 1-15
Author(s):  
Ivan Dimauro ◽  
Elisa Grazioli ◽  
Veronica Lisi ◽  
Flavia Guidotti ◽  
Cristina Fantini ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Lipid Oxidation ◽  
Immune Cells ◽  
Aerobic Training ◽  
Fold Change ◽  
Carbonyl Content ◽  
Short Term

Regular physical activity can enhance immune function and effectively prevents the spread of the cytokine response, thus reducing systemic low-grade inflammation and improving various immune markers. Moreover, regular exercise maintains redox homeostasis in skeletal muscle and other tissues, including immune cells, but the interconnection between the anti-inflammatory effects of exercise with the redox status of immune cells is still poorly understood. With the aim to verify the overall beneficial effect of regular training on the immune system, we have examined the acute and short-term effect of a 5-day exercise program on the modulation of protein and lipid oxidation, antioxidants (i.e., superoxide dismutase-1 (SOD1) and superoxide dismutase-2 (SOD2), glutathione peroxide 1 (GPx1), thioredoxin reductase-1 (TrxR1), and catalase (CAT)), and heat shock protein expression (i.e., heat shock protein-70 (HSP70) and heat shock protein-27 (HSP27)), at both mRNA and protein levels, as well as the activation of the nuclear factor kappa light chain enhancer of activated B cells (NFκB) in peripheral blood mononuclear cells (PBMCs). Moreover, plasmatic markers of oxidative stress, inflammation, and stress response (i.e., protein carbonyl content, interleukin-6 (IL6), interleukin-8 (IL8), interleukin-10 (IL10), interleukin-17E (IL17E), interleukin-17F (IL17F), interleukin-21 (IL21), interleukin-22 (IL22), and interleukin-23 (IL23)) were analyzed in active untrained young adult subjects. Even in the absence of an increased amount of protein or lipid oxidation, we confirmed a PBMC upregulation of SOD1 ( 1.26 ± 0.07 fold change, p < 0.05 ), HSP70 ( 1.59 ± 0.28 fold change, p < 0.05 ), and HSP27 gene expression ( 1.49 ± 0.09 fold change, p < 0.05 ) after 3 hours from the first bout of exercise, followed by an increase in proteins’ amount at 24 hours (SOD1, 1.80 ± 0.34 fold change; HSP70, 3.40 ± 0.58 fold change; and HSP27, 1.81 ± 0.20 fold change, p < 0.05 ) and return to basal levels after the 5 days of aerobic training. Indeed, the posttraining basal levels of oxidized molecules in plasma and PBMCs were statistically lower than the pretraining levels (carbonyl content, 0.50 ± 0.05 fold change, p < 0.01 ), paralleled by a lower expression of SOD2, Gpx1, and TrxR1, at mRNA (SOD2, 0.63 ± 0.06 ; GPx1, 0.69 ± 0.07 ; and TrxR1, 0.69 ± 0.12 fold change, p < 0.05 ) and protein (TrxR1, 0.49 ± 0.11 fold change, p < 0.05 ) levels. These results verified the existence of an early phase of redox adaptation to physical exercise already achievable after 5 days of moderate, regular aerobic training. More interestingly, this phenomenon was paralleled by the degree of NFκB activation in PBMCs and the decrease of plasmatic proinflammatory cytokines IL8, IL21, and IL22 in the posttraining period, suggesting an interconnected, short-term efficacy of aerobic exercise towards systemic oxidative stress and inflammation.

Oxidant stress increases heat shock protein 70 mRNA in isolated perfused rat heart

1994 ◽  
Vol 267 (6) ◽  
pp. H2213-H2219 ◽  
Author(s):  
R. C. Kukreja ◽  
M. C. Kontos ◽  
K. E. Loesser ◽  
S. K. Batra ◽  
Y. Z. Qian ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Rat Heart ◽  
Heat Shock Protein 70 ◽  
Coronary Flow ◽  
Oxidant Stress ◽  
Recovery Period ◽  
Hsp 70 ◽  
Developed Pressure

Ischemia/reperfusion (I/R) and preconditioning of the heart by coronary artery occlusions increase expression of heat shock protein 70 (HSP 70). Because free radicals are generated during I/R, we hypothesized that the oxidant stress might contribute to an increased expression of HSP 70. Isolated rat hearts were perfused with free radical-generating systems such as xanthine/xanthine oxidase (X/XO), irradiated rose bengal (RB) generating singlet oxygen, and H2O2 for 15 min followed by 30 min of recovery period. Significant decrease in developed pressure and coronary flow occurred after perfusion with X/XO, H2O2, and RB. During I/R, the developed pressure and coronary flow were 60 +/- 8 and 80 +/- 5%, respectively, of control, which improved significantly with superoxide dismutase. The expression of HSP 70 mRNA increased over 13-fold in hearts perfused with X/XO, 6- to 7-fold with RB, and over 5-fold with H2O2. With I/R, an over 10-fold increase in HSP 70 mRNA was observed, which decreased significantly in the presence of superoxide dismutase. These results demonstrate that oxidant stress directly increases HSP 70 mRNA in the rat heart. It is concluded that one of the potential mechanisms of expression of HSP 70 by I/R may be oxygen radicals.

Heat shock protein 70 and cellular disturbances in cochlear cisplatin ototoxicity model

2010 ◽  
Vol 124 (6) ◽  
pp. 599-609 ◽  
Author(s):  
J R García-Berrocal ◽  
J Nevado ◽  
J Á González-García ◽  
C Sánchez-Rodríguez ◽  
R Sanz ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 70 ◽  
Auditory Brainstem ◽  
State Response ◽  
Auditory Steady State Response ◽  
Brainstem Response ◽  
Response Thresholds ◽  
Total Superoxide Dismutase

AbstractBackground:Exposure to cisplatin leads to cochlear cell death by apoptosis; these changes are most marked on the seventh day after exposure. Heat shock proteins are induced in inner ear cells in response to a variety of stimuli. This study examined the role of heat shock protein 70 in cisplatin-induced cochlear cell death.Methods:Fifty-six Sprague–Dawley rats were involved. Some were injected with cisplatin (5 mg/kg body weight), some with cisplatin plus the caspase inhibitor Z-Asp(OMe)-Glu(OMe)-Val-Asp(OME)-fluoromethylketone (5 mg/kg body weight) and others were left as controls (being injected only with saline). Seven days later, we examined the expression of heat shock protein 70 and several other apoptosis-related proteins within the rat cochlear cells; we also assessed total superoxide dismutase activity, auditory brainstem response and auditory steady state response.Results:Seven days after cisplatin injection, significantly increased expression of heat shock protein 70 was found within the rat cochleae. This correlated with increased executioner caspase levels, total superoxide dismutase activity and auditory brainstem response thresholds, and a significant elevation in auditory steady state response thresholds. Inhibition of caspase-3 activity significantly reduced cochlear heat shock protein 70 expression and total superoxide dismutase activity, and improved auditory brainstem response and auditory steady state response thresholds.Conclusions:Seven days after cisplatin exposure, we found disturbances of the cochlear cellular machinery involving heat shock protein 70, other apoptotic proteins and total superoxide dismutase.

scholarly journals Expression of heat shock protein 47 is increased in remnant kidney and correlates with disease progression

1998 ◽  
Vol 79 (3) ◽  
pp. 133-140 ◽  
Author(s):  
MASAAKI SUNAMOTO ◽  
KOGO KUZE ◽  
NORIYUKI IEHARA ◽  
HIROYA TAKEOKA ◽  
KAZUHIRO NAGATA ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Disease Progression ◽  
Heat Shock Protein 47 ◽  
Remnant Kidney
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