Blood Superoxide Dismutase, Catalase and Glutathione Peroxidase Activities in Familial and Sporadic Amyotrophic Lateral Sclerosis

Przedborski, Serge; Donaldson, David M.; Murphy, Peregrine L.; Hirsch, Oscar; Lange, Dale J.; Naini, A.; McKenna‐Yasek, Diane; Brown, Robert H.

doi:10.1006/neur.1996.0008

Cited by 51 publications

(22 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We measured blood-glutathione peroxidase (9.59 -+ 0.49 pmol/min/ gm Hb), SOD (28,920 2 1,218 units/gm Hb), and catalase (309.8 ? 15.3 k/gm Hb) activities in 24 normal volunteers; these values did not differ from those measured in 17 age-matched sporadic ALS patients [31]. Based on these values and on normal blood Hb concentrations, we estimated that glutathione peroxidase activity is 1.34 t 0.07 pmollminigm brain tissue.…”

Section: Discussionmentioning

confidence: 95%

Brain superoxide dismutase, catalase, and glutathione peroxidase activities in amyotrophic lateral sclerosis

Przedborski

Donaldson

Jakowec

et al. 1996

Annals of Neurology

View full text Add to dashboard Cite

Amyotrophic lateral sclerosis is a fatal paralytic disorder of unknown cause. Recent evidence implicated the role of free radicals in the death of motor neurons in this disease. To investigate this hypothesis further, we measured the activity of the main free radical scavenging enzymes copper/zinc superoxide dismutase, manganese superoxide dismutase, catalase, and glutathione peroxidase in postmortem brain samples from 9 patients with sporadic amyotrophic lateral sclerosis and from 9 control subjects. We examined samples from the precentral gyrus of the cerebral cortex, a region affected in amyotrophic lateral sclerosis, and from the cerebellar cortex, a region not affected. The two groups did not differ in age or postmortem delay. In the precentral gyrus from amyotrophic lateral sclerosis samples, glutathione peroxidase activity as measured by spectrophotometric assay (13.8 +/- 2.6 nmol/min/mg protein [mean +/- standard error of mean]) was reduced significantly compared to the activity in the precentral gyrus from control samples (22.7 +/- 0.5 nmol/min/mg protein). In contrast, glutathione peroxidase activity was not significantly altered in the cerebellar cortex from amyotrophic lateral sclerosis patients compared to controls. Copper/zinc superoxide dismutase, manganese superoxide dismutase (corrected or not corrected for citrate synthase), and catalase were not significantly altered in the precentral gyrus or cerebellar cortex in the patient samples. This study indicated that glutathione peroxidase activity is reduced in a brain region affected in amyotrophic lateral sclerosis, thus suggesting that free radicals may be implicated in the pathogenesis of the disease.

show abstract

Section: Discussionmentioning

confidence: 95%

Brain superoxide dismutase, catalase, and glutathione peroxidase activities in amyotrophic lateral sclerosis

Przedborski

Donaldson

Jakowec

et al. 1996

Annals of Neurology

View full text Add to dashboard Cite

show abstract

“…The healthy population was younger than ALS and PD populations. Previous studies emphasized that age impacts on both MDA and thiols [48][49][50]. We performed a multivariate analysis and age-matched patients subgroup analysis in order to examine the influence of demographic parameters on the results.…”

Section: Discussionmentioning

confidence: 99%

The Role of Oxidative Stress in Amyotrophic Lateral Sclerosis and Parkinson’s Disease

et al. 2010

View full text Add to dashboard Cite

We examined oxidative stress markers of 31 patients suffering from ALS, 24 patients suffering from PD and 30 healthy subjects were included. We determined the plasma levels of lipid peroxidation (malondialdehyde, MDA), of protein oxidative lesions (plasma glutathione, carbonyls and thiols) and the activity of antioxidant enzymes i.e. erythrocyte Cu,Zn-Superoxide dismutase (SOD), Glutathione peroxidase (GSH-Px) and catalase. MDA and thiols were significantly different in both neurodegenerative diseases versus control population. A trend for an enhancement of oxidized glutathione was noted in ALS patients. Univariate analysis showed that SOD activity was significantly decreased in ALS and GSH-Px activity was decreased in PD. After adjusting for demographic parameters and enzyme cofactors, we could emphasize a compensatory increase of SOD activity in PD. Different antioxidant systems were not involved in the same way in ALS and PD, suggesting that oxidative stress may be a cause rather than a consequence of the neuronal death.

show abstract

“…With respect to other neurodegenerative disorders, the substantia nigra in PD patients can reveal a 40% reduction in GSH levels compared with control levels (Jenner et al, 1992). Similarly in ALS, perturbations to GPx activity (Przedborski et al, 1996) and GSH receptors (Lanius et al, 1993) are indicative of altered GSH metabolism. In vitro studies have also shown neuronal GSH depletion by the CJD-associated PrP106-126 toxic peptide .…”

Section: Discussionmentioning

confidence: 99%

Exacerbation of Copper Toxicity in Primary Neuronal Cultures Depleted of Cellular Glutathione

White

Bush

Beyreuther

et al. 1999

Journal of Neurochemistry

View full text Add to dashboard Cite

Perturbations to glutathione (GSH) metabolism may play an important role in neurodegenerative disorders such as Alzheimer's, Parkinson's, and prion diseases. A primary function of GSH is to prevent the toxic interaction between free radicals and reactive transition metals such as copper (Cu). Due to the potential role of Cu in neurodegeneration, we examined the effect of GSH depletion on Cu toxicity in murine primary neuronal cultures. Depletion of cellular GSH with L-buthionine-[S,R]-sulfoximine resulted in a dramatic potentiation of Cu toxicity in neurons without effect on iron (Fe) toxicity. Similarly, inhibition of glutathione reductase (GR) activity with 1,3-bis(2-chloroethyl)-l -nitrosurea also increased Cu toxicity in neurons. To determine if the Alzheimer's amyloid-p (Ap) peptide can affect neuronal resistance to transition metal toxicity, we exposed cultures to nontoxic concentrations of Ap25-35 in the presence or absence of Cu or Fe. Ap25-35 pretreatment was found to deplete neuronal GSH and increase GR activity, confirming the ability of Ap to perturb neuronal GSH homeostasis.Ap25-35 pretreatment potently increased Cu toxicity but had no effect on Fe toxicity. These studies demonstrate an important role for neuronal GSH homeostasis in selective protection against Cu toxicity, a finding with widespread implications for neurodegenerative disorders.

show abstract

Blood Superoxide Dismutase, Catalase and Glutathione Peroxidase Activities in Familial and Sporadic Amyotrophic Lateral Sclerosis

Cited by 51 publications

References 0 publications

Brain superoxide dismutase, catalase, and glutathione peroxidase activities in amyotrophic lateral sclerosis

Brain superoxide dismutase, catalase, and glutathione peroxidase activities in amyotrophic lateral sclerosis

The Role of Oxidative Stress in Amyotrophic Lateral Sclerosis and Parkinson’s Disease

Exacerbation of Copper Toxicity in Primary Neuronal Cultures Depleted of Cellular Glutathione

Contact Info

Product

Resources

About