AN INFLUENCE OF PHYSICAL ACTIVITY AND CARBOHYDRATE RATION ON SUPEROXIDE DISMUTASE (SOD) ACTIVITY AND DIENE CONCENTRATIONS IN BLOOD AND SKELETAL MUSCLE OF RATS

Shock ◽  
1995 ◽  
Vol 4 (Supplement) ◽  
pp. 55
Author(s):  
V. I. Morozov ◽  
S. A. Logosha ◽  
V. A. Rogozkin
Keyword(s):  
Physical Activity ◽  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Sod Activity

Superoxide dismutase gene expression in skeletal muscle: fiber-specific adaptation to endurance training

1999 ◽  
Vol 277 (3) ◽  
pp. R856-R862 ◽  
Author(s):  
J. Hollander ◽  
R. Fiebig ◽  
M. Gore ◽  
J. Bejma ◽  
T. Ookawara ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Protein Content ◽  
Endurance Training ◽  
Citrate Synthase ◽  
Vastus Lateralis ◽  
Mrna Level ◽  
Treadmill Running ◽  
Type I ◽  
Sod Activity

The effects of endurance training on the enzyme activity, protein content, and mRNA abundance of Mn and CuZn superoxide dismutase (SOD) were studied in various phenotypes of rat skeletal muscle. Female Sprague-Dawley rats were randomly divided into trained (T, n = 8) and untrained (U, n = 8) groups. Training, consisting of treadmill running at 27 m/min and 12% grade for 2 h/day, 5 days/wk for 10 wk, significantly increased citrate synthase activity ( P < 0.01) in the type I (soleus), type IIa (deep vastus lateralis, DVL), and mixed type II (plantaris) muscles but not in type IIb (superficial vastus lateralis, SVL) muscle. Mitochondrial (Mn) SOD activity was elevated by 80% ( P < 0.05) with training in DVL. SVL and plantaris muscle in T rats showed 54 and 42% higher pooled immunoreactive Mn SOD protein content, respectively, than those in U rats. However, no change in Mn SOD mRNA level was found in any of the muscles. CuZn SOD activity, protein content, and mRNA level in general were not affected by training, except for a 160% increase in pooled CuZn SOD protein in SVL. Training also significantly increased glutathione peroxidase and catalase activities ( P < 0.05), but only in DVL muscle. These data indicate that training adaptations of Mn SOD and other antioxidant enzymes occur primarily in type IIa fibers, probably as a result of enhanced free radical generation and modest antioxidant capacity. Differential training responses of mRNA, enzyme protein, and activity suggest that separate cellular signals may control pre- and posttranslational regulation of SOD.

Endurance training alters antioxidant enzyme gene expression in rat skeletal muscle

1998 ◽  
Vol 76 (12) ◽  
pp. 1139-1145 ◽  
Author(s):  
M Gore ◽  
R Fiebig ◽  
J Hollander ◽  
C Leeuwenburgh ◽  
H Ohno ◽  
...  
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Glutathione Peroxidase ◽  
Protein Content ◽  
Endurance Training ◽  
Vastus Lateralis ◽  
Mrna Abundance ◽  
Vastus Lateralis Muscle ◽  
Sod Activity

The effects of endurance training on gene expression of superoxide dismutase (SOD) and glutathione peroxidase (GPX) were investigated in type 2a and 2b skeletal muscles, as well as heart and liver, in the rat. Female Sprague-Dawley rats (4 months old, 300-320 g) were randomly divided into a trained (T, n = 11) and a control (C, n = 10) group and were pair fed a diet consisting of 66% cornstarch and 34% basal diet that contained all essential nutrients. Training was conducted on a treadmill at 25 m·min-1, 10% grade for 2 h per day, 5 days per week for 10 weeks, resulting in a 79% (p < 0.01) increase in citrate synthase activity in the deep portion of vastus lateralis muscle (DVL, type 2a). Cu-Zn SOD activity was 35% higher (p < 0.01) in DVL of T versus C rats, and Cu-Zn SOD mRNA abundance showed a 125% increase with training (p < 0.05). Cu-Zn SOD protein content was not altered in DVL, but increased significantly (p < 0.05) in the superficial portion of vastus lateralis (type 2b) with training. Trained rats showed a 66% higher (p < 0.05) Mn SOD protein content in DVL, but Mn SOD activity and mRNA abundance were not affected. Training also significantly increased GPX activity by 62% (p < 0.05), without changing its mRNA abundance, in the DVL. Heart and liver showed a 112 and 58% increase (p < 0.01) in Cu-Zn SOD mRNA abundance with training, respectively, but no other training adaptation was detected. These data indicate that endurance training can promote gene expression of muscle antioxidant enzymes in a fiber-specific manner. Training appears to upregulate Cu-Zn SOD mRNA abundance in a number of aerobic tissues, whereas Mn SOD and GPX induction observed in DVL may occur at the post-transcriptional levels.Key words: glutathione peroxidase, mRNA, skeletal muscle superoxide dismutase, training.

Mechanism of oxidative stress in skeletal muscle atrophied by immobilization

1993 ◽  
Vol 265 (6) ◽  
pp. E839-E844 ◽  
Author(s):  
H. Kondo ◽  
I. Nakagaki ◽  
S. Sasaki ◽  
S. Hori ◽  
Y. Itokawa
Keyword(s):  
Oxidative Stress ◽  
Skeletal Muscle ◽  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
High Performance ◽  
Superoxide Anions ◽  
Glutathione S Transferase ◽  
Sod Activity ◽  
Cytochemical Study ◽  
Male Wistar Rats

To clarify the mechanism of oxidative stress in skeletal muscle atrophied by immobilization, we measured the activities of antioxidant enzymes and xanthine oxidase (XOD) and carried out the cytochemical study of hydrogen peroxide in a typical slow red muscle, the soleus. Male Wistar rats (15 wk old), of which ankle joints of one hindlimb were immobilized in the fully extended position, were killed after 4, 8, or 12 days. The activities of Mn-containing superoxide dismutase (Mn-SOD), Cu-Zn-containing superoxide dismutase (Cu-Zn-SOD), Se-dependent glutathione peroxidase (Se-GSHPx), glutathione S-transferase, catalase, and glutathione reductase were measured spectrophotometrically. The XOD activity and the concentrations of hypoxanthine, xanthine, and urate were measured using a high-performance liquid chromatography. The cytochemical study of hydrogen peroxide in short-term organ culture was performed using an electron microscope. Increased Cu-Zn-SOD and decreased Mn-SOD in atrophy might reflect increased generation of superoxide anions in the cytoplasm rather than in the mitochondria. The source of superoxide anions in the cytoplasm might be the increased superoxide-producing XOD. Enhanced generation of superoxide anions and increased Cu-Zn-SOD activity in atrophy suggested the enhanced generation of hydrogen peroxide in the cytoplasm. Due to the unchanged activity of Se-GSHPx and the unchanged or slightly increased activity of catalase in atrophy, the ability to degrade hydrogen peroxide might not increase so much. Hence, hydrogen peroxide is expected to be increased in atrophy. The cytochemical study supported this expectation.(ABSTRACT TRUNCATED AT 250 WORDS)

Superoxide dismutase (SOD) activity in hypoxic mammalian systems

1977 ◽  
Vol 42 (1) ◽  
pp. 107-110 ◽  
Author(s):  
J. Liu ◽  
L. M. Simon ◽  
J. R. Phillips ◽  
E. D. Robin
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Cardiac Muscle ◽  
Alveolar Macrophages ◽  
Oxygen Toxicity ◽  
Peritoneal Macrophages ◽  
Sod Activity ◽  
O2 Supply

Superoxide Dismutase (SOD) activity was compared in rabbit peritoneal macrophages (ambient PO2 approximately 15 Torr) and alveolar macrophages (ambient PO2 approximately 100 Torr) and in brain, lung, cardiac muscle, and skeletal muscle of chromically hypoxic mice(ambient PO2 approximately 50 Torr) and normoxic mice (ambient PO2 approximately 150 Torr). Peritoneal macrophages (PM) have significantly less SOD activity than alveolar macrophages (AM) (PM: 2.94 +/- 0.49 (mean +/- SD); AM:6.03 +/- 1.60 units-mg protein -1 (P less than 0.01)). SOD activity of lung and brain homogenates from the hypoxic mice was significantly less than from the normoxic controls. Heart and skeletal muscle SOD activities were not significantly different. These studies show that limitations of O2 supply are associated with reductions in SOD and are consistent with the thesis that SOD plays an important role in protection against oxygen toxicity in mammalian systems.

10-gingerol induces oxidative stress through HTR1A in cumulus cells: in-vitro and in-silico studies

2020 ◽  
Vol 0 (0) ◽  
Author(s):  
Kiptiyah Kiptiyah ◽  
Widodo Widodo ◽  
Gatot Ciptadi ◽  
Aulanni’am Aulanni’Am ◽  
Mohammad A. Widodo ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Cell Culture ◽  
Superoxide Dismutase ◽  
In Silico ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Sod Activity ◽  
In Silico Studies ◽  
Incubation Periods

AbstractBackgroundWe investigated whether 10-gingerol is able to induce oxidative stress in cumulus cells.MethodsFor the in-vitro research, we used a cumulus cell culture in M199, containing 10-gingerol in various concentrations (0, 12, 16, and 20 µM), and detected oxidative stress through superoxide dismutase (SOD) activity and malondialdehyde (MDA) concentrations, with incubation periods of 24, 48, 72, and 96 h. The obtained results were confirmed by in-silico studies.ResultsThe in-vitro data revealed that SOD activity and MDA concentration increased with increasing incubation periods: SOD activity at 0 µM (1.39 ± 0.24i), 12 µM (16.42 ± 0.35ab), 16 µM (17.28 ± 0.55ab), 20 µM (17.81 ± 0.12a), with a contribution of 71.1%. MDA concentration at 0 µM (17.82 ± 1.39 l), 12 µM (72.99 ± 0.31c), 16 µM (79.77 ± 4.19b), 20 µM (85.07 ± 2.57a), with a contribution of 73.1%. Based on this, the in-silico data uncovered that 10˗gingerol induces oxidative stress in cumulus cells by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.Conclusions10-gingerol induces oxidative stress in cumulus cells through enhancing SOD activity and MDA concentration by inhibiting HTR1A functions and inactivating GSK3B and AKT˗1.

scholarly journals Effect of lemon peel flavonoids on anti-fatigue and anti-oxidation capacities of exhaustive exercise mice

2020 ◽  
Vol 63 (1) ◽  
Author(s):  
Guili Bao ◽  
Yinglong Zhang ◽  
Xiaoguang Yang
Keyword(s):  
Skeletal Muscle ◽  
Superoxide Dismutase ◽  
Manganese Superoxide Dismutase ◽  
Fatty Acid Content ◽  
Hepatic Tissue ◽  
Control Group ◽  
Dependent Manner ◽  
Lemon Peel ◽  
Tnf Α ◽  
Dose Dependent

AbstractIn this study, lemon peel flavonoids (LPF) were administered to investigate its effect on the anti-fatigue and antioxidant capacity of mice that undergo exercise until exhaustion. LPF (88.36 min in LPFH group mice) significantly increased the exhaustion swimming time compare to the untreated mice (40.36 min), increased the liver glycogen and free fatty acid content in mice and reduce lactic acid and BUN content in a dose-dependent manner. As the concentration of lemon peel flavonoids increased, the serum creatine kinase, aspartate aminotransferase, and alanine aminotransferase levels of mice gradually decreased. LPF increases superoxide dismutase (SOD) and catalase (CAT) levels in mice and reduces malondialdehyde levels in a dose-dependent manner. And LPF raises hepatic tissue SOD, CAT activities and reduces skeletal muscle tissue iNOS, TNF-α levels of mice compared to the control group. LPF also enhanced the expression of copper/zinc-superoxide dismutase (Cu/Zn-SOD), manganese-superoxide dismutase (Mn-SOD), and CAT mRNA in mouse liver tissue. LPF also enhanced the expression of alanine/serine/cysteine/threonine transporter 1 (ASCT1) mRNA and attenuate the expression of syncytin-1, inducible nitric oxide synthase (iNOS), and tumor necrosis factor (TNF)-α in mouse skeletal muscle. According to high-performance liquid chromatography (HPLC) analysis, it was found that LPF contains flavonoids such as rutin, astragalin, isomangiferin, naringin, and quercetin. Our experimental data show that LPF has good anti-fatigue effects and anti-oxidation ability. In summary, LPF has high prospects to be developed and added to nutritional supplements.

scholarly journals Attenuation of renal excretory responses to ANG II during inhibition of superoxide dismutase in anesthetized rats

2010 ◽  
Vol 298 (2) ◽  
pp. F401-F407 ◽  
Author(s):  
Md. Abdul Hye Khan ◽  
Mohammed Toriqul Islam ◽  
Alexander Castillo ◽  
Dewan Syed Abdul Majid
Keyword(s):  
Superoxide Dismutase ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Ang Ii ◽  
Sod Activity ◽  
Doppler Flowmetry ◽  
Nadph Oxidase Activity ◽  
Blood Flows ◽  
Renal Responses

To examine the functional interaction between superoxide dismutase (SOD) and NADPH oxidase activity, we assessed renal responses to acute intra-arterial infusion of ANG II (0.5 ng·kg−1·min−1) before and during administration of a SOD inhibitor, diethyldithiocarbamate (DETC, 0.5 mg·kg−1·min−1), in enalaprilat-pretreated (33 μg·kg−1·min−1) rats ( n = 11). Total (RBF) and regional (cortical, CBF; medullary; MBF) renal blood flows were determined by Transonic and laser-Doppler flowmetry, respectively. Renal cortical and medullary tissue NADPH oxidase activity in vitro was determined using the lucigenin-chemiluminescence method. DETC treatment alone resulted in decreases in RBF, CBF, MBF, glomerular filtration rate (GFR), urine flow (V), and sodium excretion (UNaV) as reported previously. Before DETC, ANG II infusion decreased RBF (−18 ± 3%), CBF (−16 ± 3%), MBF [−5 ± 6%; P = not significant (NS)], GFR (−31 ± 4%), V (−34 ± 2%), and UNaV (−53 ± 3%). During DETC infusion, ANG II also caused similar reductions in RBF (−20 ± 4%), CBF (−19 ± 3%), MBF (−2 ± 2; P = NS), and in GFR (−22 ± 7%), whereas renal excretory responses (V; −12 ± 2%; UNaV; −24 ± 4%) were significantly attenuated compared with those before DETC. In in vitro experiments, ANG II (100 μM) enhanced NADPH oxidase activity both in cortical [13,194 ± 1,651 vs. 20,914 ± 2,769 relative light units (RLU)/mg protein] and in medullary (21,296 ± 2,244 vs. 30,597 ± 4,250 RLU/mg protein) tissue. Application of DETC (1 mM) reduced the basal levels and prevented ANG II-induced increases in NADPH oxidase activity in both tissues. These results demonstrate that renal excretory responses to acute ANG II administration are attenuated during SOD inhibition, which seems related to a downregulation of NADPH oxidase in the deficient condition of SOD activity.

scholarly journals Female rats selectively bred for high intrinsic aerobic fitness are protected from ovariectomy-associated metabolic dysfunction

2015 ◽  
Vol 308 (6) ◽  
pp. R530-R542 ◽  
Author(s):  
Victoria J. Vieira-Potter ◽  
Jaume Padilla ◽  
Young-Min Park ◽  
Rebecca J. Welly ◽  
Rebecca J. Scroggins ◽  
...  
Keyword(s):  
Physical Activity ◽  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Energy Expenditure ◽  
Aerobic Fitness ◽  
Resting Energy Expenditure ◽  
Female Rats ◽  
Metabolic Dysfunction ◽  
Spontaneous Physical Activity ◽  
Resting Energy

Ovariectomized rodents model human menopause in that they rapidly gain weight, reduce spontaneous physical activity (SPA), and develop metabolic dysfunction, including insulin resistance. How contrasting aerobic fitness levels impacts ovariectomy (OVX)-associated metabolic dysfunction is not known. Female rats selectively bred for high and low intrinsic aerobic fitness [high-capacity runners (HCR) and low-capacity runners (LCR), respectively] were maintained under sedentary conditions for 39 wk. Midway through the observation period, OVX or sham (SHM) operations were performed providing HCR-SHM, HCR-OVX, LCR-SHM, and LCR-OVX groups. Glucose tolerance, energy expenditure, and SPA were measured before and 4 wk after surgery, while body composition via dual-energy X-ray absorptiometry and adipose tissue distribution, brown adipose tissue (BAT), and skeletal muscle phenotype, hepatic lipid content, insulin resistance via homeostatic assessment model of insulin resistance and AdipoIR, and blood lipids were assessed at death. Remarkably, HCR were protected from OVX-associated increases in adiposity and insulin resistance, observed only in LCR. HCR rats were ∼30% smaller, had ∼70% greater spontaneous physical activity (SPA), consumed ∼10% more relative energy, had greater skeletal muscle proliferator-activated receptor coactivator 1-alpha, and ∼40% more BAT. OVX did not increase energy intake and reduced SPA to the same extent in both HCR and LCR. LCR were particularly affected by an OVX-associated reduction in resting energy expenditure and experienced a reduction in relative BAT; resting energy expenditure correlated positively with BAT across all animals ( r = 0.6; P < 0.001). In conclusion, despite reduced SPA following OVX, high intrinsic aerobic fitness protects against OVX-associated increases in adiposity and insulin resistance. The mechanism may involve preservation of resting energy expenditure.

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