Superoxide Radical Generation, NADPH Oxidase Activity, and Cytochrome P-450 Content of Rat Liver Microsomal Fractions in an Experimental Hyperthyroid State: Relation to Lipid Peroxidation*

Endocrinology ◽  
1985 ◽  
Vol 117 (2) ◽  
pp. 496-501 ◽  
Author(s):  
VIRGINIA FERNANDEZ ◽  
XIMENA BARRIENTOS ◽  
KATINA KIPREOS ◽  
ALFONSO VALENZUELA ◽  
LUIS A. VIDELA
Keyword(s):  
Lipid Peroxidation ◽  
Nadph Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Superoxide Radical ◽  
Nadph Oxidase Activity ◽  
Hyperthyroid State ◽  
Radical Generation ◽  
Cytochrome P 450

scholarly journals NADPH oxidase activity of cytochrome P-450 BM3 and its constituent reductase domain

1995 ◽  
Vol 1231 (3) ◽  
pp. 255-264 ◽  
Author(s):  
Andrew W. Munro ◽  
J.Gordon Lindsay ◽  
John R. Coggins ◽  
Sharon M. Kelly ◽  
Nicholas C. Price
Keyword(s):  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Nadph Oxidase Activity ◽  
Cytochrome P 450 ◽  
Reductase Domain

scholarly journals The action of paraquat and diquat on the respiration of liver cell fractions

1968 ◽  
Vol 109 (5) ◽  
pp. 757-761 ◽  
Author(s):  
J C Gage
Keyword(s):  
Oxygen Uptake ◽  
Nadph Oxidase ◽  
Rat Liver ◽  
Oxidase Activity ◽  
Nadh Oxidase ◽  
Liver Microsomes ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Rat Liver Microsomes ◽  
Nadph Oxidase Activity

1. Paraquat and diquat produce only a slight increase in the oxygen uptake of rat liver mitochondria, and it is likely that they do not penetrate the mitochondrial membrane. 2. In mitochondrial fragments inhibited by antimycin A or by Amytal, both substances stimulate oxygen uptake with NADH or β-hydroxybutyrate as substrate but not with succinate. The NADH dehydrogenase of the respiratory chain appears to be involved, at a site only partially inhibited by Amytal. 3. An NADPH oxidase activity is stimulated in rat liver microsomes by diquat, and to a smaller extent by paraquat; diquat also causes an NADH oxidase activity to develop. The effect is not inhibited by carbon monoxide or p-chloromercuribenzoate, and it is probable that a flavoprotein is involved by a mechanism not requiring thiol groups. 4. One molecule of oxygen can oxidize two molecules of NADPH in the stimulated microsomal system, the hydrogen peroxide produced being broken down by a catalase activity in the microsomes. 5. Diquat can stimulate NADH oxidase and NADPH oxidase activity in the postmicrosomal soluble fraction; the enzyme involved may be DT-diaphorase. 6. The mechanism of these reactions and their significance in relation to the toxicity of the dipyridilium compounds are discussed.

NADPH-oxidase activity and lipid peroxidation in neutrophils from rats fed fat-rich diets

1999 ◽  
Vol 17 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Lucia R. Lopes ◽  
Francisco R. M. Laurindo ◽  
Jorge Mancini-Filho ◽  
Rui Curi ◽  
Paulina Sannomiya
Keyword(s):  
Lipid Peroxidation ◽  
Nadph Oxidase ◽  
Oxidase Activity ◽  
Nadph Oxidase Activity
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