Elsevier

Neuroscience Letters

Volume 405, Issues 1–2, 11 September 2006, Pages 89-93
Neuroscience Letters

Protective effect of melatonin and pinoline on nitric oxide-induced lipid and protein peroxidation in rat brain homogenates

https://doi.org/10.1016/j.neulet.2006.06.031Get rights and content

Abstract

Nitric oxide (NO) is a physiological neurotransmitter, a mediator of the excitatory neurotransmitter glutamate pathways that regulates several neuroendocrine functions, but excessive NO is toxic by itself and it interacts with superoxide radical (O2) to form the peroxynitrite anion (ONOO). Using rat brain homogenates, we investigated the effects of melatonin and pinoline in preventing the level of lipid peroxidation (LPO) and carbonyl contents in proteins induced by nitric oxide (NO) which was released by the addition of sodium nitroprusside (SNP). Lipid and protein peroxidation were estimated by quantifying malondialdehyde (MDA) and 4-hydroxyalkenal (4-HDA) concentrations and carbonyl contents, respectively. SNP increased MDA + 4-HDA and carbonyl contents production in brain homogenates in a time and concentration dependent manner. Both, melatonin and pinoline reduced NO-induced LPO and carbonyl contents in a dose-dependent manner in concentrations from 0.03 to 3 mM and 1 to 300 μM, respectively. Under the in vitro conditions of this experiment, both antioxidants were more efficient in limiting SNP protein oxidation than lipid damage.

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Acknowledgements

This work was supported in par by the University of Zaragoza (Grant No. IBE2004B-BIO-02), the Gobierno de Aragón (Aging and Oxidative Stress Physiology, Grant No. B40) and by FIS from Instituto de Salud Carlos III (Grant No. G03/137).

References (37)

  • R.J. Reiter et al.

    Pharmacological actions of melatonin in oxygen radical pathophysiology

    Life Sci.

    (1997)
  • D.X. Tan et al.

    A novel melatonin metabolite, cyclic 3-hydroxymelatonin: a biomarker of in vivo hydroxyl radical generation

    Biochem. Biophys. Res. Commun.

    (1998)
  • D. Acuña-Castroviejo et al.

    Cell protective role of melatonin in the brain

    J. Pineal Res.

    (1995)
  • J.S. Beckman et al.

    Kinetics of superoxide dismutase—an iron catalyzed nitration of phenolics by peroxynitrite

    Arch. Biochem. Biophys.

    (1992)
  • J.C. Callaway et al.

    The Pictet-Spengler reaction and biogenic tryptamines: formation of tetrahydro-β-carbolines at physiological pH

    J. Heterocyclic Chem.

    (1994)
  • E. Camacho et al.

    Inhibition of nNOS activity in rat brain by synthetic kynurenines: structure-activity dependence

    J. Med. Chem.

    (2002)
  • J.P. Crow et al.

    Sensitivity of the zinc-thiolate mioety of yeast alcohol dehydrogenase to hypochorite and peroxynitrite

    Biochemistry

    (1995)
  • V.L. Dawson et al.

    Nitric oxide mediates glutamate neurotoxicity in primary cortical cultures

    Proc. Natl. Acad. Sci. U.S.A.

    (1991)
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