Abstract
During the process of inflammation oxygen radicals are produced by phagocytic cells like neutrophils, eosinophils, monocytes and macrophages. Little is known about the effects of oxygen radicals on lung tissue in inflammatory diseases such as asthma1. Activated phagocytes release Superoxide anions, synthesized by NADPH oxidase which is located in the cellular membrane. Superoxide anions dismutate to hydrogen peroxide enzymatically (superoxide dismutase) or non-enzymatically. These superoxide anions and hydrogen peroxide together form very reactive oxygen species, namely the hydroxyl radical and singlet oxygen. In these reactions iron plays a catalytic role2. Oxygen metabolites cause DNA strand breaks, protein destruction (particularly sulfhydryl groups are sensitive to oxidative stress) and lipid peroxidation. The lipid peroxidation reaction products are very toxic too and cause DNA and protein damage as well3,4.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
PJ. Barnes, K.F. Chung, and C.P. Page, Inflammatory mediators and asthma, Pharmacol Rev. 40:49 (1988).
D. Roos, and R.S. Weening, Defects of oxidative killing of micro-organisms by phagocytic leukocytes, in: Oxygen Free Radicals and Tissue Damage, Ciba Foundation Symposium 65, Exerpta Medica, Amsterdam (1979).
C.E. Vaca, J. Wilhelm, and M. Harms-Ringdahl, Interaction of lipid peroxidation products with DNA, Mutation Res. 195:137 (1988).
R. Leurs, B. Rademaker, K. Kramer, H. Timmerman, and A. Bast, The effects of 4-hydroxy-2,3-trans-nonenal on ß-adrenoceptors of rat lung membranes, Chem.-Biol. Interactions 59:211 (1986).
K. Kramer, C.J.A. Doelman, H. Timmerman, and A. Bast, A disbalance between beta-adrenergic and muscarinic responses caused by hydrogen peroxide in rat airways in vitro, Biochem. Biophys. Res. Comm, 145:337 (1987).
N. Ben-Arie, C. Gileadi, and M. Schramm, Interaction of the beta-adrenergic receptor with Gs following delipidation, Eur. J. Biochem. 176:649 (1988).
A. Achari, D. Scott, P. Barlow et al., Facing up to membranes: structural function relationships in phospholipases, in Cold Spring Harbor Symposia on Quantitive Biology, Vol LII (1987).
C.J.A. Doelman, K. Kramer, H. Timmerman, and A. Bast, Vitamin E and selenium regulate balance between ß-adrenergic and muscarinic responses in rat lungs,FEBS Lett. 233:427 (1988).
R. Anderson, A.J. Theron, and G.J. Ras, Ascorbic acid neutralizes reactive oxidants released by hyperactive phagocytes from cigarette smokers, Lung 166:149 (1988).
H. Wefers, and H. Sies, The protection by ascorbate and glutathione against microsomal lipid peroxidation is dependent on vitamin E, Eur. J. Biochem. 174:353 (1988).
C.G. Ramell, B. Cunliffe, and A.J. Kieboom, Determination of alpha-tocopherol in biological specimens by high-performance liquid chromatography, J. Liq. Chromatogr. 6:1123 (1983).
S.K. Jagota, and H.M. Dani, A new colorimetric technique for the estimation of vitamin C using folin phenol reagent, Anal. Biochem. 127:178 (1982).
O.W. Griffith, Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine, Anal. Biochem. 106:207 (1988).
P. E. Brumby, and V. Massey, Determination of nonheme iron, total iron and copper, J. Biol. Chem. 229:763 (1957).
M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248 (1976).
A. Wendel, Glutathione peroxidase, Methods in Enzymol. 77:325 (1981).
D.J. Worthington, and M.A. Rosemeyer, Human glutathione reductase: purification of the crystalline enzyme from erythrocytes, Eur. J. Biochem. 48:167 (1974).
J.M. McCord, and I. Fridovich, Superoxide dismutase, J. Biol. Chem. 244:6049 (1969).
G.R.M.M. Haenen, and A. Bast, Protection against lipid peroxidation by a microsomal glutathione-dependent labile factor, FEBS Lett. 159:24 (1983).
M.G. Mustafa, and D.F. Tierney, Biochemical and metabolic changes in the lung with oxygen, ozone, and nitrogen dioxide toxicity, Am. Rev. Resp. Dis. 118:1061 (1978).
J.R. Wright, H.D. Colby, and P.R. Miles, Cytosolic factors which affect microsomal lipid peroxidation in lung and liver, Arch. Biochem. Biophys. 206:296 (1981).
J.R. Wright, H.D. Colby, and P.R. Miles, Lipid peroxidation in guinea pig lung microsomes, Biochim. Biophys. Acta 619:374 (1980).
G. Minotti, and S.D. Aust, The requirement for iron (III) in the initiation of lipid peroxidation by iron (II) and hydrogen peroxide, J. Biol. Chem. 262:1098 (1987).
J.M. Braughler, R.L. Chase, and J.F. Pregenzer, Stimulation and inhibition of iron-dependent lipid peroxidation by desferrioxamine, Biochem. Biophys. Res. Comm. 153:933 (1988).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
Doelman, C.J.A., Bast, A. (1990). Pro- and Anti-Oxidant Factors in Rat lung Cytosol. In: Emerit, I., Packer, L., Auclair, C. (eds) Antioxidants in Therapy and Preventive Medicine. Advances in Experimental Medicine and Biology, vol 264. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5730-8_71
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5730-8_71
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5732-2
Online ISBN: 978-1-4684-5730-8
eBook Packages: Springer Book Archive