Abstract
In recent years, experimental and clinical evidence has determined that the reperfusion of previously ischemic myocardium may lead to accelerated cellular damage. In the past this has been attributed to the disruption of cellular membranes (1, 2) following the endogenous generation of oxygen-free radicals (OFR), but more recently there is increasing evidence that damage to cellular proteins is also involved (3, 4). Attempts to quench the endogenous generation of OFR’s with superoxide dismutase and catalase has met with some success, but the long term results have not shown a major reduction in tissue loss (5, 6). OFR’s, such as superoxide anion or the hydroxyl radical, are highly reactive compounds, but have extremely short half-lives (ie 10−9 seconds). However, much of the observed damage to the myocardium occurs several hours after reperfusion (7). This suggests a role for exogenously generated OFR’s or related oxidizing agents in the late development of myocardial reperfusion injury.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Chien K., Abrams J., Serroni A., Martin J. and Farber J. Accelerated phospolipid degredation and associated membrane dysfunction in irreversible, ischemic liver cell injury. J. Biol. Chem. 253: 4809 - 4817, 1978.
Meerson F., Kagan V., Kozlov Y., Belkina L. and Arkhipenko Y. The role of lipid peroxidation in pathogenesis of ischemic damage and the antioxidant protection of the heart. Basic Res. Cardiol. 77: 465 - 485, 1982.
Davies K. Protein damage and degredation by oxygen radicals. I. General aspects. J. Biol. Chem. 262: 9895 - 9901, 1987.
Hashizume H. and Abiko Y. Rapid changes in myofibrillar proteins after reperfusion of ischemic myocardium in dogs. Basic Res. Cardiol. 83: 250 - 257, 1988.
Gallagher K., Buda A., Pace D., Gerren R. and Shalfer M. Failure of superoxide dismutase and catalase to alter size of infarction in conscious dogs after 3 hours of occlusion followed by reperfusion. Circulation 73: 1065 - 1076, 1986.
Richard V., Murray C., Jennings R. and Reimer K. Therapy to reduce free radicals during early reperfusion does not limit the size of myocardial infarct caused by 90 minutes of ischemia in dogs. Circulation 78: 473 - 480, 1988.
Smith E. HI, Egan J., Bugelski P., Hillegass L., Hill D. and Griswold D. Temporal relation between neutrophil accumulation and myocardial reperfusion injury. Am. J. Physiol. 255: H1060 - H1068, 1988.
Chatelain P., Latour J., Tran D., de Lorgeril M., Dupras G. and Bourassa M. Neutrophil accumulation in experimental myocardial infarcts: relation with extent of injury and effect of reperfusion. Circulation 75: 1083 - 1090, 1987.
Loewe O.G., Murry C., Richard J., Weischedel G., Jennings R. and Reimer K. Myocardial neutrophil accumulation during reperfusion after reversible or irreversible ischemic injury. Am. J. Physiol. 255: H1188 - H1198, 1988.
Mullane K. Myocardial ischemia-reperfusion injury: role of neutrophils and neutrophil derived mediators. In: Human Inflammatory Disease, 1, (edited by G. Marone, L. Lichtenstein, M. Condorelli and A. Fauci ). Decker, Philedelphia, 1988, pp. 143 - 159.
Engler R., Schmid-Schonbein G. and Pavelec R. Leukocyte capillary plugging in myocardial ischemia and reperfusion in the dog. Am. J. Pathol. 111: 98 - 111, 1983.
Klebanoff S. Phagocytic cells: products of oxygen metabolism. In.Inflammation: Basic Principles and Clinical Correlates., (edited by J. Gallin, I. Goldstein andR. Snyderman ). Raven Press, Ltd., New York, 1988, pp. 391 - 444.
Engler R. and Covell J. Granulocytes cause reperfusion ventricular dysfunction after 15-minute ischemia in the dog. Cell Calcium 61: 20 - 28, 1987.
Barroso-Aranda J., Schmid-Schonbein G., Zweifach B. and Engler R. Granulocytes and no-reflow phenomenon in irreversible hemorrhagic shock. Circ. Res. 63: 437 - 447, 1988.
Korthuis R., Grisham M. and Granger D. Leukocyte depletion attenuates vascular injury in postischemic skeletal muscle. Am. J. Physiol. 254: H823 - H827, 1988.
Fliss H., Masika M., Eley D.W. and Korecky B. Oxygen radical mediated protein oxidation in heart. In:Oxygen Radicals in the Pathophysiology of Heart Disease, (edited by P. Singal ). Martinus Nijhoff Publishers, Boston, 1988, pp. 71 - 90.
Vissers M., Day W. and Winterbourne C. Neutrophils adherent to a nonphagocytosable surface (glomerular basement membrane) produce oxidants only at the site of attachment. Blood 66: 161 - 166, 1985.
Eley D.W., Korecky B. and Fliss H. Dithiothreitol restores contractile function to oxidant-injured cardiac muscle. Am. J. Physiol. 257: H1321 - H1325, 1989.
Mirabelli F., Salis A., Marinoni V., Finardi G., Bellomo G., Thor H. and Orrenius S. Menadione-induced bleb formation in hepatocytes is associated with the oxidation of thiol groups in actin. Arc. Biochem. Biophys. 264: 261 - 269, 1988
Scherer N. and Deamer D. Oxidation of thiols in the Ca2+-ATPase of sarcoplasmic reticulum microsomes. Biochim. Biophys. Acta 862: 309 - 317, 1986.
Reeves J., Bailey C. and Hale C. Redox modification of sodium-calcium exchange activity in cardiac sarcolemmal vesicles. J. Biol. Chem. 261: 4948 - 4955, 1986.
Sedlak J. and Lindsay R. Estimation of total, protein bound, and nonprotein sulfhydryl groups in tissue with Ellman’s reagent. Anal. Biochem. 25: 192 - 205, 1968.
Bishop J., Squier T., Bigelow D. and Inesi G. (Iodoacetamido)fluorescein labels a pair of proximal cysteines on the Ca2+-ATPase of sarcoplasmic reticulum. Biochem. J 262: 4748 - 4754, 1988.
Nicotera P., Moore M., Mirabrelli F., Bellomo G. and Orrenius S. Inhibition of hepatocyte plasma membrane Ca2+ ATase activity by menadione metabolism and its restoration by thiols. FEBS Letters 181: 149 - 153, 1985.
Kawakita M. and Yamashita T. Reactive sulfhydryl groups of sarcoplasmic reticulum ATPase. III. Identification of cysteine residues whose modification with N-ethylmaleimide leads to loss of the Ca2+ transporting activity. J. Biochem. 102: 103 - 109, 1987.
Kako K., Kato M., Matsuoka T. and Mustapha A. Depression of membranebound Na+-K+-ATPase activity induced by free radicals and by ischemia of kidney. Am. J. Physiol. 254: C330 - C337, 1988.
Chaussepied P., Mornet D., Audemard E., Derancourt J. and Kassab R. Abolition of the ATPase activities of skeletal myosin subfragment-s by a new selective proteolitic cleavage within the 50 kilodalton heavy chain segment. Biochem 25: 1134 - 1140, 1986.
Audemard E., Bertrand R., Bonet A., Chaussepied P. and Mornet D. Pathway for the communication between ATPase and actin sites in myosin. J. Muscle Res. Cell Motil. 9: 197 - 218, 1988.
Wagner P. and Giniger E. Hydrolysis of ATP and reversible binding of F-actin by heavy myosin chain free of all light chain. Nature 292: 560 - 561, 1981.
Kasprazak A.A., Chaussepied P. and Morales M.F. Location of a contact site between actin and myosin in the three-dimensional structure of the acto-S 1 complex. Biochem 28: 9230 - 9238, 1989.
Walker M. and Trinick J. Visualization of domains in native and nucleotide-trapped myosin heads by negative staining. J. Musc. Res. Cell. Motil. 9: 359 - 366, 1988.
Tada M., Bailin G., Barany K. and Barany M. Biochem 8: 4842 - 4850, 1969.
Pfister M., Schaub M., Watterson J., Knecht M. and Waser P. Radioactive labeling and location of specific thiol groups in myosin from fast, slow, and cardiac muscle. Biochim. Biophys. Acta 410: 193 - 209, 1975.
Wells J. and Yount R. Active site trapping of nucleotides by crosslinking two sulfhydryls in myosin subfragment 1. Proc. Natl. Acad. Sci. USA 76: 4966–4970, 1979.
Eisenberg E. and Greene L. The relation of muscle biochemistry to muscle physiology. Ann. Rev. Physiology 42: 293 - 309, 1980.
Collins J. and Elzinga M. The primary structure of actin from rabbit skeletal muscle. J. Biol. Chem. 250: 5915 - 5920, 1975.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1990 Kluwer Academic Publishers
About this chapter
Cite this chapter
Eley, D.W., Fliss, H., Korecky, B. (1990). Oxidation of Myofibrillar Thiols: A Mechanism of Contractile Dysfunction Reversible by Dithiothreitol. In: Korecky, B., Dhalla, N.S. (eds) Subcellular Basis of Contractile Failure. Developments in Cardiovascular Medicine, vol 116. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1513-1_18
Download citation
DOI: https://doi.org/10.1007/978-1-4613-1513-1_18
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4612-8813-8
Online ISBN: 978-1-4613-1513-1
eBook Packages: Springer Book Archive