S-nitrosoglutathione inhibits SOD/H2O2-dependent lipid peroxidation

B. Kalyanaraman, Ravinder Jit Singh

Research output: Contribution to journalArticle

Abstract

The peroxidase activity of superoxide dismutase (SOD) has been attributed to the increased lipid peroxidation observed during the reaction between linoleic acid, SOD and H2O2. The copper-bound hydroxyl radical was proposed to abstract an hydrogen atom from linoleate and initiate lipid peroxidation. To better understand the mechanism of SOD/H2O2-catalyzed lipid peroxidation, we have used S-nitrosoglutathione (GSNO) as an antioxidant probe. Addition of H2O2 (1 mM) to an incubation mixture containing egg phosphatidylcholine liposomes (250 μg/ml) and SOD (200 μg/ml) caused an increase in the formation of conjugate diene which was inhibited by the addition of diethylenetriaminepentaacetic acid (DTPA). Addition of GSNO caused a dose-dependent increase in time-lag for conjugate diene formation. Nitric oxide released from GSNO in the presence of SOD and H2O2 was measured by electron spin resonance spectroscopy. We attribute the increase in lipid peroxidation caused by SOD and H2O2 to the copper ions released from SOD that subsequently catalyzes the lipid hydroperoxide-dependent oxidation. The antioxidant activity of GSNO is attributed to the copper ion dependent release of nitric oxide, which acts as a chain breaking antioxidant. We conclude that GSNO can act as a potent antioxidant in biological systems where free copper ions released from metalloproteins catalyze peroxidation of lipid.

Original languageEnglish (US)
JournalFASEB Journal
Volume12
Issue number5
StatePublished - Mar 20 1998

Fingerprint

S-Nitrosoglutathione
Lipid Peroxidation
Superoxide Dismutase
superoxide dismutase
lipid peroxidation
Lipids
Copper
Antioxidants
copper
Linoleic Acid
Ions
ions
antioxidants
nitric oxide
Nitric Oxide
metalloproteins
Metalloproteins
Electron spin resonance spectroscopy
Lipid Peroxides
electron paramagnetic resonance spectroscopy

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

S-nitrosoglutathione inhibits SOD/H2O2-dependent lipid peroxidation. / Kalyanaraman, B.; Singh, Ravinder Jit.

In: FASEB Journal, Vol. 12, No. 5, 20.03.1998.

Research output: Contribution to journalArticle

@article{10f4c785eb2c4a709c6c4912091cac0f,
title = "S-nitrosoglutathione inhibits SOD/H2O2-dependent lipid peroxidation",
abstract = "The peroxidase activity of superoxide dismutase (SOD) has been attributed to the increased lipid peroxidation observed during the reaction between linoleic acid, SOD and H2O2. The copper-bound hydroxyl radical was proposed to abstract an hydrogen atom from linoleate and initiate lipid peroxidation. To better understand the mechanism of SOD/H2O2-catalyzed lipid peroxidation, we have used S-nitrosoglutathione (GSNO) as an antioxidant probe. Addition of H2O2 (1 mM) to an incubation mixture containing egg phosphatidylcholine liposomes (250 μg/ml) and SOD (200 μg/ml) caused an increase in the formation of conjugate diene which was inhibited by the addition of diethylenetriaminepentaacetic acid (DTPA). Addition of GSNO caused a dose-dependent increase in time-lag for conjugate diene formation. Nitric oxide released from GSNO in the presence of SOD and H2O2 was measured by electron spin resonance spectroscopy. We attribute the increase in lipid peroxidation caused by SOD and H2O2 to the copper ions released from SOD that subsequently catalyzes the lipid hydroperoxide-dependent oxidation. The antioxidant activity of GSNO is attributed to the copper ion dependent release of nitric oxide, which acts as a chain breaking antioxidant. We conclude that GSNO can act as a potent antioxidant in biological systems where free copper ions released from metalloproteins catalyze peroxidation of lipid.",
author = "B. Kalyanaraman and Singh, {Ravinder Jit}",
year = "1998",
month = "3",
day = "20",
language = "English (US)",
volume = "12",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "5",

}

TY - JOUR

T1 - S-nitrosoglutathione inhibits SOD/H2O2-dependent lipid peroxidation

AU - Kalyanaraman, B.

AU - Singh, Ravinder Jit

PY - 1998/3/20

Y1 - 1998/3/20

N2 - The peroxidase activity of superoxide dismutase (SOD) has been attributed to the increased lipid peroxidation observed during the reaction between linoleic acid, SOD and H2O2. The copper-bound hydroxyl radical was proposed to abstract an hydrogen atom from linoleate and initiate lipid peroxidation. To better understand the mechanism of SOD/H2O2-catalyzed lipid peroxidation, we have used S-nitrosoglutathione (GSNO) as an antioxidant probe. Addition of H2O2 (1 mM) to an incubation mixture containing egg phosphatidylcholine liposomes (250 μg/ml) and SOD (200 μg/ml) caused an increase in the formation of conjugate diene which was inhibited by the addition of diethylenetriaminepentaacetic acid (DTPA). Addition of GSNO caused a dose-dependent increase in time-lag for conjugate diene formation. Nitric oxide released from GSNO in the presence of SOD and H2O2 was measured by electron spin resonance spectroscopy. We attribute the increase in lipid peroxidation caused by SOD and H2O2 to the copper ions released from SOD that subsequently catalyzes the lipid hydroperoxide-dependent oxidation. The antioxidant activity of GSNO is attributed to the copper ion dependent release of nitric oxide, which acts as a chain breaking antioxidant. We conclude that GSNO can act as a potent antioxidant in biological systems where free copper ions released from metalloproteins catalyze peroxidation of lipid.

AB - The peroxidase activity of superoxide dismutase (SOD) has been attributed to the increased lipid peroxidation observed during the reaction between linoleic acid, SOD and H2O2. The copper-bound hydroxyl radical was proposed to abstract an hydrogen atom from linoleate and initiate lipid peroxidation. To better understand the mechanism of SOD/H2O2-catalyzed lipid peroxidation, we have used S-nitrosoglutathione (GSNO) as an antioxidant probe. Addition of H2O2 (1 mM) to an incubation mixture containing egg phosphatidylcholine liposomes (250 μg/ml) and SOD (200 μg/ml) caused an increase in the formation of conjugate diene which was inhibited by the addition of diethylenetriaminepentaacetic acid (DTPA). Addition of GSNO caused a dose-dependent increase in time-lag for conjugate diene formation. Nitric oxide released from GSNO in the presence of SOD and H2O2 was measured by electron spin resonance spectroscopy. We attribute the increase in lipid peroxidation caused by SOD and H2O2 to the copper ions released from SOD that subsequently catalyzes the lipid hydroperoxide-dependent oxidation. The antioxidant activity of GSNO is attributed to the copper ion dependent release of nitric oxide, which acts as a chain breaking antioxidant. We conclude that GSNO can act as a potent antioxidant in biological systems where free copper ions released from metalloproteins catalyze peroxidation of lipid.

UR - http://www.scopus.com/inward/record.url?scp=33749364103&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749364103&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33749364103

VL - 12

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 5

ER -