Influence of carbonyl stress on rheological alterations of blood materials and decarbonylation effect of glutathione

Abstract

The effects of various toxic carbonyls such as malondialdehyde (MDA), a secondary product of lipid peroxidation, and other aldehydes on rheological parameters and their relationship with aging-associated alterations were studied. Both MDA and glutaraldehyde (Glu) in different concentrations significantly increase viscosity, plastic viscosity and yield stress of human plasma and erythrocyte suspensions. MDA (20 mmol/L) reduces sharply the typical fluorescence of proteins (excitation 280 nm/emission 350 nm), and produces age pigment-like fluorescence with a strong emission peak at 460 nm when excites at 395 nm by only being incubated for some hours. In contrast, Glu decreases merely the fluorescence of proteins without producing age pigment-like fluorescence. These data suggest interestingly that the MDA-induced gradual protein cross linking seems to form from different mechanisms compared to the fast rheological changes of blood materials which may take place either in acute and chronic diseases or during aging. On the other hand, MDA induces various deleterious alterations of erythrocytes whereas glutathione (GSH) inhibits the MDA-related carbonyl stress in a concentration-dependent manner. The results indicate that carbonyl-amino reaction exists in the blood widely and GSH has the ability to interrupt or reverse this reaction in a certain way. It implies that carbonyl stress may be one of the important factors in blood stasis and suggests a theoretical and practical approach in anti-stresses and anti-aging.

Keywords

blood viscosity / carbonyl stress / malondialdehyde / cross linking / decarbonylation effect / glutathione

References

[1] MiyataT.. Alterations of non-enzymatic biochemistry in uremia, diabetes, and atherosclerosis (“carbonyl stress”) [J]. Bull Mem Acad R Med Belg, 2002, 157(3/4): 189-198

[2] RobertsM. J., WondrakG. T., LaureanD. C., JacobsonM. K., JacobsonE. L.. DNA damage by carbonyl stress in human skin cells [J]. Mutat Res, 2003, 522(1/2): 45-56

[3] BaynesJ. W., ThorpS. R.. Glycoxidation and lipoxidation in atherogenesis [J]. Free Radic Biol Med, 2000, 28(12): 1708-1716

[4] HermannE., HelmwardZ.. Methods for determination of aldehydic lipid peroxidation products [J]. Free Radic Biol Med, 1989, 7(2): 197-203

[5] SushilK. J., JeanD. R., GaryJ. L., JohenD.. The effect of malonyldialdehyde on viscosity of normal and sickle red blood cells [J]. Biochem Med Motab Bio, 1990, 44(1): 37-44

[6] KikugawaK., TsukudaK., KurechiT.. Studies on peroxidized lipids. Interaction of malondialdehyde with secondary amine and its relevance to nitrosamine formation [J]. Chem Pharm Bull, 1980, 28(11): 3323-3331

[7] LiuX. B., QinW. H., YinD. Z.. Biochemical relevance between oxidative/carbonyl stress and elevated viscosity of erythrocyte suspensions [J]. Clinical Hemorheology and Microcirculation, 2004, 31(2): 149-156

[8] ShiY. D.. Shortcoming in blood viscosity and how to overcome it by Casson equation [J]. Chinese J Hemorheol, 1998, 8: 4-7

[9] ChungT. W., HoC. P.. Changes in viscosity of low shear rates and viscoelastic properties of oxidative erythrocyte suspensions [J]. Clin Hemorheol Microcirc, 1999, 21(2): 99-103

[10] YinD. Z.. Biochemical basis of lipofuscin, ceroid, and age pigment -like fluorophores [J]. Free Radic Biol Med, 1996, 21(6): 871-888

[11] YinD. Z.. Lipofuscin-like fluorophores can result from reactions between oxidized ascorbic acid and glutamine. Carbonyl-protein cross-linking may represent a common reaction in oxygen radical and glycosylation-related ageing processes [J]. Mech Ageing Dev, 1992, 62(10): 35-46