Skeletal muscle, oxidative stress

Mujahid A., Y. Akiba, C.H. Warden and M. Toyomizu, 2007. Sequential changes in superoxide production, anion carriers and substrate oxidation in skeletal muscle mitochondria of heat-stressed chickens. FEES Lett. 581, 3461-3467. Mujahid A., Y. Akiba and M. Toyomizu, 2009. Olive oil-supplemented diet alleviates acute heat stress-induced mitochondrial ROS production in chicken skeletal muscle. Am. J. Physiol. Regul. Comp. Physiol. 297, R690-698. 

Salo, D.C., Donovan, C.M., Davies, K.J, (1991). Hsp70 and other possible heat shock or oxidative stress proteins are induced in skeletal muscle, heart, and liver during exercise. Free Radic. Biol. Med 11,239-246. 

Malek, R.L., H. Sajadi, J. Abraham, M.A. Grundy, and G.S. Gerhard. 2004. The effects of temperature reduction on gene expression and oxidative stress in skeletal muscle from adult zebra fish. Comp. Biochem. Physiol. Part C 138 363-373. 

Also, HPLC methods with electrochemical or fluorescent detection are used (H19, M3). In proteins, dityrosine can be estimated by immunochemical methods employing dityrosine-specific antibodies (K5). Measurements of o,o -dityrosine and o-tyrosine levels in rat urine express dityrosine contents in skeletal muscle proteins, and have been proposed as the noninvasive oxidative stress test in vivo. One should be aware, however, that A-formylkynurenine, also formed in protein oxidation, has similar fluorescence properties as dityrosine (excitation 325 nm, emission at 400-450 nm) (G29). Also, oxidation of mellitin when excited at 325 nm produces an increase in fluorescence at 400—450 nm, despite the fact that mellitin does not contain tyrosine. Oxidation of noncontaining Trp residues ribonuclease A and bovine pancreatic trypsin inhibitor with "OH produces loss of tyrosine residues with no increase in fluorescence at 410 nm (S51). There are also methods measuring the increased hydrophobicity of oxidized proteins. Assays are carried out measuring protein binding of a fluorescent probe, 8-anilino-l-naphthalene-sulfonic acid (ANS). Increase in probe binding reflects increased surface hydrophobicity (C7). 

Milatovic, D., Gupta, R.C., Dekundy, A., Montine, T.J., Dettbam, W-D. (2005a). Carbofuran-induced oxidative stress in slow and fast skeletal muscles prevention by memantine. Toxicology 208 13-24. 

Critical illness is associated with alterations in muscle GSH metabolism [40-42]. Skeletal muscles are reduced and total GSH concentrations drop, thus indicating a condition of oxidative stress and an augmented release of GSH from this tissue. 

Age changes appeared in muscle tissue results in decreased stability to un-favorable factors, for example, to oxidative stress. The intensity of protein synthesis falls and muscle mass decreases (approximately by 25% to age of 70 compared to the age of 20), and efficiency of contractile response decreases as well. Muscle anti-oxidant system deficiency flings into a deficit and CRC content in heart and skeletal muscles is decreased [104,105]. While distinct correlation between age changes and muscle pathologies has not been found, in whole aging is a strong prognostic factor for several muscle myasthenia and other age disfunctions. 

The role of selenium in human medicine has been reviewed. Animal studies in the 1950s demonstrated the nutritionally beneficial, effects of selenium by showing that there was a selenium-responsive liver necrosis in vitamin E-deficient rats. There are important selenium-dependent diseases in farm animals, such as white muscle disease in sheep and cattle, and myopathy of cardiac and skeletal muscle in lambs and calves. In these animals, some cause of oxidative stress, such as increased physical activity or vitamin E deficiency—together witli dietary selenium deficiency—is required to elicit the disease. 

As acute strenuous exercise and chronic exercise training increase the requirement for various antioxidants, it is conceivable that dietary supplementation of specific antioxidants would be beneficial. Older subjects may be more susceptible to oxidative stress and may benefit from the antioxidant protection provided by vitamin E. During severe oxidative stress such as strenuous exercise, the enzymatic and nonenzymatic antioxidant systems of skeletal muscle are not able to cope with the massive free-radical formation, which results in an increase in lipid peroxidation. Vitamin E decreases exercise-induced lipid peroxidation. The exercise may increase superoxide anion generation in the heart, and the increase in the activity of superoxide dismutase (SOD) in skeletal muscle may be... 

The actions of epinephrine and norepinephrine in the liver, the adipocyte, the skeletal muscle cell, and the a and 3 cells of the pancreas direcdy influence fuel metabolism (Fig. 43.6). These catecholamines are counterregulatory hormones that have metabolic effects directed toward mobilization of fuels from their storage sites for oxidation by cells to meet the increased energy requirements of acute and chronic stress. They simultaneously suppress insulin secretion, which ensures that fuel fluxes will continue in the direction of fuel utilization rather than storage as long as the stressful stimulus persists. 

The lime course of changes in high-energy phosphates (HEPs) (ATP and PCr) and their metabolites in skeletal muscles of control rats and those acutely intoxicated with carbofuran (l.Smg/kg, sc) (Table 3) revealed that in controls the levels of ATP and PCr are higher in the EDL than in the soleus. At the time of maximal severity (i.e., 1 hr after carbofuran expo.sure), the levels of ATP, total adenine nucleotides (TAN = ATP + ADP + AMP), NAD, PCr, and total creatine compounds (TCC = PCr + Cr) were maximally reduced in both muscles. Slow recovery was seen after 2 or 3 hr, with complete recovery to control levels by 24 hr. The carbofuran-induced muscle hyperactivity increased mu,scle levels of p2-IsoPs and NO and reduced levels of HEPs and their metabolites and thus seemed to produce a rapid omset of oxidative Stress. 

Vitamin Bi, also called thiamine, is required for all tissues and high concentrations are found in skeletal muscle, heart, liver, kidneys and brain. Thiamine diphosphate (TDP) is the active form and it serves as a cofactor for several enzymes involved in carbohydrate catabolism. These enzymes are also important in the biosynthesis of many cellular constituents, including neurotransmitters, and for the production of reducing equivalents used in oxidant stress defenses (Ba 2008). Thiamine is considered an anti-stress vitamin because it strengthens the immune system and improves the body s ability to withstand stress conditions (Haas 1988). 

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