Mini review
Antioxidant systems and erythrocyte life-span in mammals

https://doi.org/10.1016/0305-0491(93)90121-KGet rights and content

Abstract

  • 1.

    1. Erythrocyte antioxidant systems—superoxide dismutase (SOD), catalase (CAT), reduced glutathione (GSH), glutathione peroxidase (GSH-Px), glutathione S-transferase (GST) and glutathione reductase (GR)—were discussed in relation to life-spans in some mammalian species.

  • 2.

    2. The erythrocyte life-span of different mammals was found to be correlated with the levels of SOD, GSH-Px and GSH.

  • 3.

    3. Data reviewed indicates that the erythrocyte life-span of each species is governed by both the oxygen radical formation and the efficiency of intrinsic antioxidant systems.

References (139)

  • R.G. Cutler

    Antioxidants, aging, and longevity

  • R.G. Cutler

    Urate and ascorbate: their possible roles as antioxidants in determining longevity of mammalian species

    Arch. Gerontol. Geriat.

    (1984)
  • M. Das et al.

    Differential inhibition of rat and human glutathione S-transferase isoenzymes by plant phenols

    Biochem. biophys. Res. Commun.

    (1986)
  • K.G. Eckert et al.

    Formation and transport of xenobiotic glutathione-S-conjugates in red cells

    Biochem. Pharmac.

    (1986)
  • A. Fazi et al.

    Cell age-dependent decay of human erythrocytes glutathione S-transferase

    Mech. Ageing Dev.

    (1991)
  • T.M. Fischer et al.

    Selective alternation of erythrocyte deformability by SH-reagents

    Biochim. biophys. Acta

    (1978)
  • L. Flohé et al.

    Kinetics of glutathione peroxidase

    Biochim. biophys. Acta

    (1969)
  • L. Flohe et al.

    Glutathione peroxidase: a selenoenzyme

    FEBS Lett.

    (1973)
  • G. Fornaini et al.

    Regulatory properties of human erythrocyte hexokinase during cell ageing

    Archs Biochem. Biophys.

    (1985)
  • G.F. Gaetani et al.

    Catalase and glutathione peroxidase are equally active in detoxification of hydrogen peroxide in human erythrocytes

    Blood

    (1989)
  • C. Guthenberg et al.

    Glutathione S-transferase (transferase π) from human placenta is identical or closely related to glutathione S-transferase (transferase ϱ) from erythrocytes

    Biochim. biophys. Acta

    (1981)
  • W.H. Habig et al.

    Glutathione S-transferases

  • J.W. Harvey et al.

    Binding of heme by glutathione S-transferase: a possible role of the erythrocyte enzyme

    Blood

    (1982)
  • J.W. Harvey et al.

    Erythrocyte enzyme activities and glutathione levels of the horse, cat, dog and man

    Comp. Biochem. Physiol.

    (1975)
  • R.P. Hebbel et al.

    Phagocytosis of sickle erythrocytes: immunologic and oxidative determinants of hemolytic anemia

    Blood

    (1984)
  • H. Imanishi et al.

    Glutathione-linked enzyme activities in red cell aging

    Clin. chim. Acta

    (1986)
  • S.K. Jain

    The accumulation of malonyldialdehyde, a product of fatty acid peroxidation, can disturb aminophospholipid organization in the membrane bilayer of human erythrocytes

    J. biol. Chem.

    (1984)
  • S.K. Jain

    Evidence for membrane lipid peroxidation during the in vivo aging of human erythrocytes

    Biochim. biophys. Acta

    (1988)
  • M. Kurata et al.

    Differences in levels of erythrocyte glutathione and its metabolizing enzyme activities among primates

    Comp. Biochem. Physiol.

    (1993)
  • P.G. Lankisch et al.

    Reduced glutathione and glutathione reductase—a comparative study of erythrocytes from various species

    Comp. Biochem. Physiol.

    (1973)
  • R.A. Lawrence et al.

    Glutathione peroxidase activity in selenium-deficient rat liver

    Biochem. biophys. Res. Commun.

    (1976)
  • R.A. Lawrence et al.

    Species, tissue and subcellular distribution of non-Se-dependent glutathione peroxidase activity

    J. Nutr.

    (1978)
  • N. Maeda et al.

    Alternation of rheological properties of human erythrocytes by crosslinking of membrane proteins

    Biochim. biophys. Acta

    (1983)
  • M. Magnani et al.

    Effect of age on some properties of mice erythrocytes

    Mech. Ageing Dev.

    (1988)
  • B. Mandula et al.

    Synthesis of riboflavin nucleotides by mature human erythrocytes

    Blood

    (1970)
  • J. Maral et al.

    Comparative study of superoxide dismutase, catalase and glutathione peroxidase levels in erythrocytes of different animals

    Biochem. biophys. Res. Commun.

    (1977)
  • C.J. Marcus et al.

    Glutathione transferase from human erythrocytes

  • H.J. Meiselman et al.

    Membrane mechanical properties of ATP-depleted human erythrocytes

    Blood

    (1978)
  • J. Miquel et al.

    Effects of temperature on the life-span, vitality and fine structure of Drosophila melanogaster

    Mech. Ageing Dev.

    (1976)
  • K.D. Munkres et al.

    Genetically determined conidial longevity is positively correlated with superoxide dismutase, catalase, glutathione peroxidase, cytochrome c peroxidase, and ascorbate free radical reductase activities in Neurospora crassa

    Mech. Ageing Dev.

    (1984)
  • J. Murakami et al.

    A contribution of calmodulin to cellular deformability of calcium-loaded human erythrocytes

    Biochim. biophys. Acta

    (1986)
  • T. Ono et al.

    Unique increase of superoxide dismutase level in brains of long living mammals

    Expl Gerontol.

    (1984)
  • S.R. Pfeffer et al.

    Role of peroxidation in erythrocyte aging

    Mech. Ageing Dev.

    (1982)
  • H.J. Powers et al.

    Is red blood cell survival limited by the activity of a critical enzyme?

    J. theor. Biol.

    (1981)
  • A.S. Reddi

    Riboflavin nutritional status and flavoprotein enzymes in streptozotocin-diabetic rats

    Biochim. biophys. Acta

    (1986)
  • G. Rijksen et al.

    Properties of human erythrocyte hexokinase related to cell age

    Clin. chim. Acta

    (1977)
  • M.D. Sass et al.

    Enzyme activity as an indicator of red cell age

    Clin. chim. Acta

    (1964)
  • M. Scarpa et al.

    Generation of superoxide ion in human red blood cell lysates

    J. biol. Chem.

    (1984)
  • N.S. Agar et al.

    Studies on glucose-6-phosphate dehydrogenase, glutathione reductase and regeneration of reduced glutathione in the red blood cells of various mammalian species

    Aust. J. exp. Med. Sci.

    (1974)
  • N.S. Agar et al.

    Certain features of erythrocytes of normal and glutathione-deficient sheep

    Am. J. Vet. Res.

    (1975)
  • Cited by (235)

    • The effects of dietary yeast hydrolysate on growth, hematology, antioxidant enzyme activities and non-specific immunity of juvenile Nile tilapia, Oreochromis niloticus

      2020, Fish and Shellfish Immunology
      Citation Excerpt :

      The current study suggests that the dietary YH could possibly protect fish from possibly invasive organisms. During the aging processes, it was observed that antioxidant enzyme activity is equivocal in response to the accumulation of ROS (Reactive Oxygen Species) [34]. However, if the antioxidant activity mechanisms are unable to control the increased levels of ROS, lipids, proteins, and nucleic acids membranes are injured because of oxidative stress.

    • Omega-3 fatty acids supplementation and oxidative stress parameters: A systematic review and meta-analysis of clinical trials

      2019, Pharmacological Research
      Citation Excerpt :

      When the subgroup analysis was performed based on the health condition of participants, in metabolic and non-metabolic or diabetic and non-diabetic patients, this effect remained significant, while in healthy subjects this effect was not significant. MDA is an end-product created during lipid peroxidation, because of breaking down of omega-6 LCUFAs in cell membrane such as arachidonic acid [55], it’s levels is usually high in pathologic and disease conditions [56]. Therefore, it is logical that supplementation of omega-3 FAs in patients have a greater effect on MDA reduction than on healthy people.

    View all citing articles on Scopus
    View full text