Mechanisms of conversion of xanthine dehydrogenase to xanthine oxidase in ischemic rat liver and kidney

Mechanisms of conversion of xanthine dehydrogenase to xanthine oxidase in ischemic rat liver and... of superoxide during tissue reperfusion has been implicated as a critical component of postischemic injury in a variety of tissues including intestine, skin, skeletal muscle, brain, heart, lung, kidney, liver. Both (X0) inhibitors enzymatic scavengers of oxygen free radicals limit the extent of postischemic injury. As a result, the enzyme X0 has been proposed as an important source of superoxide in reperfused tissues (11, 14, 17). The involvement of X0 in reperfusion injury depends on its ability to produce superoxide. In vivo, under nor0193-1857/88 $1.50 Copyright ma1conditions, the -utilizing enzyme exists predominantly as a ,dehydrogenase (XD), which utilizes NAD+ rather than oxygen as an electron acceptor produces NADH rather than superoxide (2). To explain the X0-mediated, superoxide-dependent reperfusion injury observed in cat ileum, Granger et al. (11) proposed that the dehydrogenase form of the enzyme was converted to an form during . In vitro, XD can be converted to X0 by a variety of chemical enzymatic treatments. These can be divided into two groups based on their reversibility by the addition of thiol reducing compounds, such as dithiothreitol (DTT). XD can be reversibly converted to X0 by air oxidation (29), enzymatic sulfhydryl oxidation [sulfhydryl glutathione disulfide (GSSG)dependent thiol: http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Gastrointestinal and Liver Physiology The American Physiological Society

Mechanisms of conversion of xanthine dehydrogenase to xanthine oxidase in ischemic rat liver and kidney

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Publisher
The American Physiological Society
Copyright
Copyright © 1988 the American Physiological Society
ISSN
0193-1857
eISSN
1522-1547
Publisher site
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Abstract

of superoxide during tissue reperfusion has been implicated as a critical component of postischemic injury in a variety of tissues including intestine, skin, skeletal muscle, brain, heart, lung, kidney, liver. Both (X0) inhibitors enzymatic scavengers of oxygen free radicals limit the extent of postischemic injury. As a result, the enzyme X0 has been proposed as an important source of superoxide in reperfused tissues (11, 14, 17). The involvement of X0 in reperfusion injury depends on its ability to produce superoxide. In vivo, under nor0193-1857/88 $1.50 Copyright ma1conditions, the -utilizing enzyme exists predominantly as a ,dehydrogenase (XD), which utilizes NAD+ rather than oxygen as an electron acceptor produces NADH rather than superoxide (2). To explain the X0-mediated, superoxide-dependent reperfusion injury observed in cat ileum, Granger et al. (11) proposed that the dehydrogenase form of the enzyme was converted to an form during . In vitro, XD can be converted to X0 by a variety of chemical enzymatic treatments. These can be divided into two groups based on their reversibility by the addition of thiol reducing compounds, such as dithiothreitol (DTT). XD can be reversibly converted to X0 by air oxidation (29), enzymatic sulfhydryl oxidation [sulfhydryl glutathione disulfide (GSSG)dependent thiol:

Journal

AJP - Gastrointestinal and Liver PhysiologyThe American Physiological Society

Published: May 1, 1988

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