Age-Related Oxidation Reaction in Proteins

Er, Stadtman; Oliver, C; Starke–Reed, Pamela; Rhee, Sang Youl

doi:10.1177/0748233793009001-213

Cited by 22 publications

(8 citation statements)

References 17 publications

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“…As proteins become damaged and release metal ions into the system, where they become redox active, they contribute to radical formation by Fenton chemistry processes. 26,27 Albumin ordinarily provides a firstline defense against these reactions by binding and removing metal ions from the plasma, an ability that appears to be deficient in this patient cohort.…”

Section: Discussionmentioning

confidence: 96%

Alterations in the functional capacity of albumin in patients with decompensated cirrhosis is associated with increased mortality

Schnurr²,

et al. 2009

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Albumin concentration is diminished in patients with liver failure. Albumin infusion improves survival of cirrhotic patients with spontaneous bacterial peritonitis, and it is hypothesized that this may be due in part to its detoxifying capabilities. The aim of this study was to perform detailed quantitative and qualitative assessment of albumin function in patients with cirrhosis. Healthy controls and patients with acute deterioration of cirrhosis requiring hospital admission (n ‫؍‬ 34) were included. Albumin function was assessed using affinity of the fatty acid binding sites using a spin label (16 doxyl-stearate) titration and electron paramagnetic resonance spectroscopy and ischemia-modified albumin (IMA) was measured. Twenty-two patients developed acute-on-chronic liver failure. Twelve were treated with the Molecular Adsorbents Recirculating System (MARS) and 10 with standard medical therapy. For each parameter measured, the patients' albumin had reduced functional ability, which worsened with disease severity. Fifteen patients died, and IMA, expressed as an albumin ratio (IMAR), was significantly higher in nonsurvivors compared with survivors (P < 0.001; area under the receiver operating curve ‫؍‬ A lbumin is the major plasma protein and constitutes around 50% of the cell free protein in healthy individuals. It is produced exclusively in the liver, and therefore its concentration is reduced during hepatic dysfunction. 1 Following the Cochrane meta-analysis describing potential harmfully effect of albumin infusion in critically ill patients, there has been a reexamination of the use of albumin infusions for volume replacement. However, the results of the recently published SAFE study have provided new data confirming the safety of albumin infusion in critically ill patients. 2,3 Liver failure results in multiple organ dysfunction, and mortality rates without liver transplantation remain unacceptably high. 4 However, recovery is associated with complete reversal of multiorgan dysfunction. At present, in patients with cirrhosis, albumin is used mainly to replenish the circulating volume. With increasing severity of cirrhosis, there is a progressive increase in cardiac output, which is associated with a progressive reduction in individual organ blood flow. This peculiar circulatory disturbance is thought to occur as a result of splanchnic

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Section: Discussionmentioning

confidence: 96%

Alterations in the functional capacity of albumin in patients with decompensated cirrhosis is associated with increased mortality

Schnurr²,

et al. 2009

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“…Malate dehydrogenase is located within the mitochondrial matrix in order to connect glycolysis to mitochondrial respiration. The activity of this enzyme is also decreased during aging, which could be related to oxidative modification (Stadtman et al, 1993). The oxidation of the protein, potentially resulting in enzyme dysfunction, could result in alterations in ATP availability, synaptic plasticity, and neuronal recovery owing to its relationship with glutamate regulation.…”

Section: Discussionmentioning

confidence: 99%

Protective effect of D609 against amyloid-beta1–42-induced oxidative modification of neuronal proteins: Redox proteomics study

et al. 2006

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Oxidative stress has been implicated in the pathophysiology of a number of diseases, including neurodegenerative disorders such as Alzheimer's disease (AD), a neurodegenerative disorder associated with cognitive decline and enhanced oxidative stress. Amyloid-beta peptide(1-42) (Abeta(1-42)), one of the main component of senile plaques, can induce in vitro and in vivo oxidative damage to neuronal cells through its ability to produce free radicals. The aim of this study was to investigate the protective effect of the xanthate D609 on Abeta(1-42)-induced protein oxidation by using a redox proteomics approach. D609 was recently found to be a free radical scavenger and antioxidant. In the present study, rat primary neuronal cells were pretreated with 50 microM of D609, followed by incubation with 10 microM Abeta(1-42) for 24 hr. In the cells treated with Abeta(1-42) alone, four proteins that were significantly oxidized were identified: glyceraldehyde-3-phosphate dehydrogenase, pyruvate kinase, malate dehydrogenase, and 14-3-3 zeta. Pretreatment of neuronal cultures with D609 prior to Abeta(1-42) protected all the identified oxidized proteins in the present study against Abeta(1-42)-mediated protein oxidation. Therefore, D609 may ameliorate the Abeta(1-42)-induced oxidative modification. We discuss the implications of these Abeta(1-42)-mediated oxidatively modified proteins for AD pathology and for potential therapeutic intervention in this dementing disorder.

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“…Third, the identity of the gene encoding TPx II with that encoding NKEF, which has been shown to be induced by oxidative stress (5), implies a potential physiologic role for this factor in the protection of cells from death by oxidative damage. Oxidative stress and damage by free radicals have been implicated in several pathologic states including cancer (31,32), several neurodegenerative diseases such as muscular dystrophy (33), Alzheimer's (34, 35) and Parkinson's diseases (36), amyotrophic lateral sclerosis (37), atherosclerosis/ischemic injuries (31,38), and aging (39,40). Interestingly, chromosomal localization of the human TPx II gene demonstrated that it resides on chromosome 13q12 (4).…”

Section: Discussionmentioning

confidence: 99%

Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2

Zhang

Liu

Kang

et al. 1997

Journal of Biological Chemistry

347

177

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Thioredoxin peroxidase (TPx) is a member of a newly discovered family of proteins that are conserved from yeast to mammals and to which natural killer enhancing factor belongs. These proteins are antioxidants that function as peroxidases only when coupled to a sulfhydryl reducing system. The physiological function of TPx in cells is not yet known. Here we demonstrate that when the human TPx II, a member of this family, is stably overexpressed in Molt-4 leukemia cells, it protects from apoptosis induced by serum deprivation, ceramide, or etoposide. TPx II, like Bcl-2, is able to inhibit release of cytochrome c from mitochondria to cytosol, and it inhibits lipid peroxidation in cells. TPx II, unlike Bcl-2, could prevent hydrogen peroxide accumulation in cells, suggesting that it functions upstream of Bcl-2 in the protection from apoptosis and may be implicated as an endogenous regulator of apoptosis.

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Age-Related Oxidation Reaction in Proteins

Cited by 22 publications

References 17 publications

Alterations in the functional capacity of albumin in patients with decompensated cirrhosis is associated with increased mortality

Alterations in the functional capacity of albumin in patients with decompensated cirrhosis is associated with increased mortality

Protective effect of D609 against amyloid-beta1–42-induced oxidative modification of neuronal proteins: Redox proteomics study

Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2

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