P4.22 In vivo decrease of elevated protein thiol oxidation and protection of dystrophic muscle from exercise induced damage, using the thiol containing antioxidant N-acetylcysteine in dystrophic mdx mice

2011 ◽  
Vol 21 (9-10) ◽  
pp. 710-711
Author(s):  
J.R. Terrill ◽  
H.G. Radley-Crabb ◽  
M.D. Grounds ◽  
P.G. Arthur
Keyword(s):  
Mdx Mice ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Dystrophic Muscle ◽  
Elevated Protein ◽  
Exercise Induced ◽  
Protein Thiol Oxidation

scholarly journals Rapid disruption of intestinal epithelial tight junction and barrier dysfunction by ionizing radiation in mouse colon in vivo: protection by N-acetyl-l-cysteine

2016 ◽  
Vol 310 (9) ◽  
pp. G705-G715 ◽  
Author(s):  
Pradeep K. Shukla ◽  
Ruchika Gangwar ◽  
Bhargavi Manda ◽  
Avtar S. Meena ◽  
Nikki Yadav ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Ionizing Radiation ◽  
Actin Cytoskeleton ◽  
Barrier Function ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Radiation Induced ◽  
Stress Dependent ◽  
Protein Thiol Oxidation

The goals of this study were to evaluate the effects of ionizing radiation on apical junctions in colonic epithelium and mucosal barrier function in mice in vivo. Adult mice were subjected to total body irradiation (4 Gy) with or without N-acetyl-l-cysteine (NAC) feeding for 5 days before irradiation. At 2–24 h postirradiation, the integrity of colonic epithelial tight junctions (TJ), adherens junctions (AJ), and the actin cytoskeleton was assessed by immunofluorescence microscopy and immunoblot analysis of detergent-insoluble fractions for TJ and AJ proteins. The barrier function was evaluated by measuring vascular-to-luminal flux of fluorescein isothiocyanate (FITC)-inulin in vivo and luminal-to-mucosal flux in vitro. Oxidative stress was evaluated by measuring protein thiol oxidation. Confocal microscopy showed that radiation caused redistribution of occludin, zona occludens-1, claudin-3, E-cadherin, and β-catenin, as well as the actin cytoskeleton as early as 2 h postirradiation, and this effect was sustained for at least 24 h. Feeding NAC before irradiation blocked radiation-induced disruption of TJ, AJ, and the actin cytoskeleton. Radiation increased mucosal permeability to inulin in colon, which was blocked by NAC feeding. The level of reduced-protein thiols in colon was depleted by radiation with a concomitant increase in the level of oxidized-protein thiol. NAC feeding blocked the radiation-induced protein thiol oxidation. These data demonstrate that radiation rapidly disrupts TJ, AJ, and the actin cytoskeleton by an oxidative stress-dependent mechanism that can be prevented by NAC feeding.

N-Acetylcysteine treatment of dystrophic mdx mice results in protein thiol modifications and inhibition of exercise induced myofibre necrosis

2012 ◽  
Vol 22 (5) ◽  
pp. 427-434 ◽  
Author(s):  
Jessica R. Terrill ◽  
Hannah G. Radley-Crabb ◽  
Miranda D. Grounds ◽  
Peter G. Arthur
Keyword(s):  
Mdx Mice ◽  
Protein Thiol ◽  
Exercise Induced

scholarly journals Early metabolic changes measured by 1H MRS in healthy and dystrophic muscle after injury

2012 ◽  
Vol 113 (5) ◽  
pp. 808-816 ◽  
Author(s):  
Su Xu ◽  
Stephen J. P. Pratt ◽  
Espen E. Spangenburg ◽  
Richard M. Lovering
Keyword(s):  
Skeletal Muscle ◽  
Muscle Injury ◽  
Tibialis Anterior Muscle ◽  
Metabolic Changes ◽  
Mdx Mice ◽  
Resonance Spectroscopy ◽  
Dystrophic Muscle ◽  
1H Mrs ◽  
Skeletal Muscle Injury

Skeletal muscle injury is often assessed by clinical findings (history, pain, tenderness, strength loss), by imaging, or by invasive techniques. The purpose of this work was to determine if in vivo proton magnetic resonance spectroscopy (1H MRS) could reveal metabolic changes in murine skeletal muscle after contraction-induced injury. We compared findings in the tibialis anterior muscle from both healthy wild-type (WT) muscles (C57BL/10 mice) and dystrophic ( mdx mice) muscles (an animal model for human Duchenne muscular dystrophy) before and after contraction-induced injury. A mild in vivo eccentric injury protocol was used due to the high susceptibility of mdx muscles to injury. As expected, mdx mice sustained a greater loss of force (81%) after injury compared with WT (42%). In the uninjured muscles, choline (Cho) levels were 47% lower in the mdx muscles compared with WT muscles. In mdx mice, taurine levels decreased 17%, and Cho levels increased 25% in injured muscles compared with uninjured mdx muscles. Intramyocellular lipids and total muscle lipid levels increased significantly after injury but only in WT. The increase in lipid was confirmed using a permeable lipophilic fluorescence dye. In summary, loss of torque after injury was associated with alterations in muscle metabolite levels that may contribute to the overall injury response in mdx mice. These results show that it is possible to obtain meaningful in vivo 1H MRS regarding skeletal muscle injury.

scholarly journals FAD Transport and FAD-dependent Protein Thiol Oxidation in Rat Liver Microsomes

2003 ◽  
Vol 279 (5) ◽  
pp. 3370-3374 ◽  
Author(s):  
Marianne Varsányi ◽  
András Szarka ◽  
Eszter Papp ◽  
Dóra Makai ◽  
Gábor Nardai ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Microsomes ◽  
Rat Liver Microsomes ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Dependent Protein ◽  
Protein Thiol Oxidation

Iron-initiated tissue oxidation: Lipid peroxidation, vitamin e destruction and protein thiol oxidation

1993 ◽  
Vol 45 (7) ◽  
pp. 1477-1482 ◽  
Author(s):  
Kelly L. Linseman ◽  
Philip Larson ◽  
J.Mark Braughler ◽  
John M. McCALL
Keyword(s):  
Lipid Peroxidation ◽  
Vitamin E ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Protein Thiol Oxidation

scholarly journals Protein thiol oxidation in the rat lung following e-cigarette exposure

Redox Biology ◽  
2020 ◽  
Vol 37 ◽  
pp. 101758
Author(s):  
Juan Wang ◽  
Tong Zhang ◽  
Carl J. Johnston ◽  
So-Young Kim ◽  
Matthew J. Gaffrey ◽  
...  
Keyword(s):  
Rat Lung ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Protein Thiol Oxidation

scholarly journals Vesiculation of sickle erythrocytes during thermal stress

Blood ◽  
1988 ◽  
Vol 72 (3) ◽  
pp. 1060-1063 ◽  
Author(s):  
BH Rank ◽  
NL Moyer ◽  
RP Hebbel
Keyword(s):  
Thermal Stress ◽  
Membrane Protein ◽  
Strong Correlation ◽  
Phenazine Methosulfate ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Functional Abnormality ◽  
Sickle Erythrocytes ◽  
Protein Thiol Oxidation

Abstract Since it is not known why sickle RBCs tend to undergo microvesiculation, we have investigated their susceptibility to thermal stress. While normal RBCs start to vesiculate at 49.0 +/- 0 degrees C (n = 14), sickle RBCs begin to vesiculate at 47.9 +/- 0.5 degrees C, with a range of 46.5 to 48.5 degrees C (n = 14). This abnormality is reproduced by treating normal RBCs with phenazine methosulfate (PMS), which stimulates the excess intracellular generation of superoxide characteristic of sickle RBCs. For PMS-treated RBCs, there is a strong correlation between membrane protein thiol oxidation and vesiculation temperature (r = .977, P less than .001). The abnormal vesiculation temperature of both unmanipulated sickle RBCs and PMS-treated RBCs is significantly improved by treatment of the RBCs with dithiothreitol. The most dense sickle RBCs are most prone to vesiculation during thermal stress, and they are the subpopulation having the greatest amount of thiol oxidation. We conclude that the tendency of sickle RBCs to vesiculate during thermal stress is further evidence for functional abnormality of the RBC cytoskeleton due to thiol oxidation.

scholarly journals Proximity-based Protein Thiol Oxidation by H2O2-scavenging Peroxidases

2009 ◽  
Vol 284 (46) ◽  
pp. 31532-31540 ◽  
Author(s):  
Marcus Gutscher ◽  
Mirko C. Sobotta ◽  
Guido H. Wabnitz ◽  
Seda Ballikaya ◽  
Andreas J. Meyer ◽  
...  
Keyword(s):  
Thiol Oxidation ◽  
Protein Thiol ◽  
Protein Thiol Oxidation
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