Hemoglobin, oxidative damage

Quercetin and rutin suppressed photosensitized hemolysis of human erythrocytes with ho values equal to 40 p.mol l-1 and 150 jjlmt>I I 1, respectively [139]. Suppression of photohemolysis was accompanied by inhibition of lipid peroxidation. Morin inhibited oxygen radical-mediated damage induced by superoxide or peroxyl radicals to the human cells in the cardiovascular system, erythrocytes, ventricular myocytes, and saphenous vein endothelial cells [140]. Rutin protected against hemoglobin oxidation inside erythrocytes stimulated by prooxidant primaquine [141],... 

Shelf life of an LEH preparation is dependent on the change in particle size and oxidative damage to the lipid and hemoglobin upon storage. LEH tends to... 

Selenium 10-75 meg Protects against oxidative damage to hemoglobin... 

Ribavirin accnmnlates in erythrocytes, resnlting in hemolysis by an nnknown mechanism, perhaps related to oxidative damage to the erythrocyte membrane. Time-dependent and dose-dependent hemolytic anemia (eventnaUy associated with hyperbilirubinemia and a high reticnlocyte connt) is the only major toxic effect associated with oral or intravenons ribavirin and is reversible on withdrawal. There was a fall in hemoglobin concentrations below 10.0 g/dl in 9% of patients with hepatitis C treated with ribavirin and interferon alfa (6,7). 

Oxidative damage to hemoglobin may lead to its precipitation (e.g., by acetaminophen) and present as Heinz bodies that can be detected by morphological evaluation of blood smears. Heinz body is a rounded, often retractile, projection from the surface of the RBC that is due to oxidation and denatur-ation of hemoglobin. Typically, the detection of Heinz bodies associated with hemolytic anemia is believed to be indicative of nonimmune-mediated anemia. In contrast, supportive evidence of the involvement of immune system components in anemic animals could include a positive autoagglutination of blood cells. 

M. Roy, S. Sen, and A. S. Chakraborti, Action of pelargonidin on hyperglycemia and oxidative damage in diabetic rats Implication for glyeation-induced hemoglobin modification. Life Sci, 82 (2008) 1102-1110. 

Angeli, J. R, C. C. Garda, F. Sena, F. P. Freitas, S. Miyamoto et al. 2011. Lipid hydroperoxide-indueed and hemoglobin-enhanced oxidative damage to colon cancer cells. 

Nitrosoarenes are readily formed by the oxidation of primary N-hydroxy arylamines and several mechanisms appear to be involved. These include 1) the metal-catalyzed oxidation/reduction to nitrosoarenes, azoxyarenes and arylamines (144) 2) the 02-dependent, metal-catalyzed oxidation to nitrosoarenes (145) 3) the 02-dependent, hemoglobin-mediated co-oxidation to nitrosoarenes and methe-moglobin (146) and 4) the 0 2-dependent conversion of N-hydroxy arylamines to nitrosoarenes, nitrosophenols and nitroarenes (147,148). Each of these processes can involve intermediate nitroxide radicals, superoxide anion radicals, hydrogen peroxide and hydroxyl radicals, all of which have been observed in model systems (149,151). Although these radicals are electrophilic and have been suggested to result in DNA damage (151,152), a causal relationship has not yet been established. Nitrosoarenes, on the other hand, are readily formed in in vitro metabolic incubations (2,153) and have been shown to react covalently with lipids (154), proteins (28,155) and GSH (17,156-159). Nitrosoarenes are also readily reduced to N-hydroxy arylamines by ascorbic acid (17,160) and by reduced pyridine nucleotides (9,161). 

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