Glutathione in tissue

Methyl chloride causes toxicity in rodents in the liver, kidney and central nervous system. It may deplete glutathione in tissues. 

Muscari, C., Pappagallo, M., Ferrari, D., Giordano, E., Capanni, C., Caldarera, C. M., and Guarnieri, C., Simultaneous detection of reduced and oxidized glutathione in tissues and mitochondria by capillary electrophoresis, J. Chromatogr. B Biomed. Sci. Appl, 101, 301-307, 1998. 

Distribution of acrylonitrile (ACN) in tissues of control and glutathione (GSH) depleted B6C3F1 mice... 

M2. Mapson, L. W., Enzyme systems associated with the oxidation and reduction of glutathione in plant tissues. Biochem. Soc. Symposia (Cambridge, Engl.) 17, 28-42 (1959). 

Vasodilation is attributable to nitric oxide (NO), which is produced either directly from the nitroester or liberated by decomposition of NO intermediates (Feelisch and Noack 1987). Either glutathione in cells of vascular tissue or sulfhydryl groups of proteins in these tissues may be responsible for converting nitrates to NO. Nitric oxide activates guanylyl cyclase, which increases intracellular levels of cyclic guanosine 3 5 -monophosphate and thereby produces vasodilation (Kelly and Smith 1996 Robertson and Robertson 1996). 

Sazuka, Y., Tanizawa, H. andTakino, Y. (1989). Effect of adriamycin on the activities of superoxide dismutase, glutathione peroxidase and catalase in tissues of mice. Journal of Cancer Research, 80 80-94. 

Cote et al. (1984) and Vodicka et al. (1990) observed marked decreases in glutathione levels in a variety of organs such as brain, lung, liver and kidney of rats dosed with acrylonitrile either subcutaneously (75 mg/kg bw) or by inhalation (75-300 mg/m3). These effects were less pronounced in mouse and hamster tissues. Covalent binding to tissue protein, a dose-dependent decrease in tissue glutathione, and an... 

Both acrylonitrile and cyanoethylene oxide can conjugate with glutathione, leading to detoxification of these reactive compounds. At high doses of acrylonitrile, as used in animal studies, glutathione in certain tissues may be depleted. Such glutathione depletion will probably not occur at low-level human exposure. 

Internal burdens of epoxybutene in humans resulting from exposure to butadiene were predicted from models by Kohn and Melnick (1993), Johanson and Filser (1996) and Csanady et al. (1996) and were compared with simulations for rats and mice. In the model of Kohn and Melnick (1993), metabolic parameters were incorporated which had been obtained by Csanady et al. (1992) by measuring butadiene and epoxybutene oxidation and epoxybutene hydrolysis in human liver and lung microsomes in vitro, and conjugation of epoxybutene with glutathione in human liver and lung cytosol. Tissue blood partition coefficients were theoretically derived. The body burden of epoxy butene following exposure to 100 ppm butadiene for 6 h was predicted to be 0.056 pmol/kg in humans. 

Teaf, C.M., Bishop, J.B. Harbison, R.D. (1990) Potentiation of ethyl methanesulfonate induced germ cell mutagenesis and depression of glutathione in male reproductive tissues by 1,2-dibromoethane. Teratog. Carcinog. Mutag., 10, 427-438... 

After absorption, methyl bromide or metabolites are rapidly distributed to many tissues including the lung, adrenal gland, kidney, liver, nasal turbinates, brain, testis and adipose tissue. In an inhalation study in rats, the methyl bromide concentrations in tissues reached a maximum after 1 h of exposure, but decreased rapidly. Methyl bromide is probably metabolized by glutathione conjugation, the fonned. S -mcthylglutathione being sequentially catabolized to. S -methyl-L-cystcinc and then to carbon dioxide. 

Little information about the mechanism of action of flavonoids is anticipated from in vivo studies. The mechanism of catechin and morin seems to be related to an increase of the activity of detoxifying enzymes like glutathione-S-transferase and NADPH quinone reductase [198, 211]. Similarly, EGCG effect at the colonic level is associated to an increase in tissue superoxide dismutase levels, suggesting that it may act through a potentiation of the antioxidative defense [210]. 

In its biochemical functions, ascorbic acid acts as a regulator in tissue respiration and tends to serve as an antioxidant in vitro by reducing oxidizing chemicals. The effectiveness of ascorbic acid as an antioxidant when added to various processed food products, such as meats, is described in entry on Antioxidants. In plant tissues, the related glutathione system of oxidation and reduction is fairly widely distributed and there is evidence that election transfer reactions involving ascorbic acid are characteristic of animal systems. Peroxidase systems also may involve reactions with ascorbic acid In plants, either of two copper-protein enzymes are commonly involved in the oxidation of ascorbic acid. 

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