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Results: 1 to 10 of 12

Publication Record


Clinical Relevance of Biomarkers of Oxidative Stress.
Frijhoff J, Winyard PG, Zarkovic N, Davies SS, Stocker R, Cheng D, Knight AR, Taylor EL, Oettrich J, Ruskovska T, Gasparovic AC, Cuadrado A, Weber D, Poulsen HE, Grune T, Schmidt HH, Ghezzi P
(2015) Antioxid Redox Signal 23: 1144-70
MeSH Terms: Animals, Biomarkers, DNA Damage, Glycation End Products, Advanced, Humans, Lipid Peroxidation, Lipoproteins, LDL, Malondialdehyde, Oxidative Stress, Protein Carbonylation, Reactive Oxygen Species
Show Abstract · Added October 8, 2015
SIGNIFICANCE - Oxidative stress is considered to be an important component of various diseases. A vast number of methods have been developed and used in virtually all diseases to measure the extent and nature of oxidative stress, ranging from oxidation of DNA to proteins, lipids, and free amino acids.
RECENT ADVANCES - An increased understanding of the biology behind diseases and redox biology has led to more specific and sensitive tools to measure oxidative stress markers, which are very diverse and sometimes very low in abundance.
CRITICAL ISSUES - The literature is very heterogeneous. It is often difficult to draw general conclusions on the significance of oxidative stress biomarkers, as only in a limited proportion of diseases have a range of different biomarkers been used, and different biomarkers have been used to study different diseases. In addition, biomarkers are often measured using nonspecific methods, while specific methodologies are often too sophisticated or laborious for routine clinical use.
FUTURE DIRECTIONS - Several markers of oxidative stress still represent a viable biomarker opportunity for clinical use. However, positive findings with currently used biomarkers still need to be validated in larger sample sizes and compared with current clinical standards to establish them as clinical diagnostics. It is important to realize that oxidative stress is a nuanced phenomenon that is difficult to characterize, and one biomarker is not necessarily better than others. The vast diversity in oxidative stress between diseases and conditions has to be taken into account when selecting the most appropriate biomarker.
2 Communities
1 Members
0 Resources
11 MeSH Terms
Genetic variation in GPX1 is associated with GPX1 activity in a comprehensive analysis of genetic variations in selenoenzyme genes and their activity and oxidative stress in humans.
Takata Y, King IB, Lampe JW, Burk RF, Hill KE, Santella RM, Kristal AR, Duggan DJ, Vaughan TL, Peters U
(2012) J Nutr 142: 419-26
MeSH Terms: Aged, Cross-Sectional Studies, Female, Glutathione Peroxidase, Humans, Male, Malondialdehyde, Middle Aged, Oxidative Stress, Phospholipid Hydroperoxide Glutathione Peroxidase, Polymorphism, Single Nucleotide, Protein Carbonylation, Risk Factors, Selenium, Selenoprotein P
Show Abstract · Added September 28, 2015
Previous studies suggest some effects of selenium on risk of several chronic diseases, which may be mediated through a small number of selenoenzymes with antioxidant properties. In this cross-sectional analysis of 195 participants from the Seattle Barrett's Esophagus Study who were free of esophageal cancer at the time of blood draw, we examined whether the number of the minor alleles in 26 tagging single nucleotide polymorphisms (SNP) of five selenoenzyme genes [i.e., glutathione peroxidase 1-4 (GPX1-4) and selenoprotein P (SEPP1)] was associated with activity of GPX1 in white blood cells and GPX3 in plasma, and concentrations of SEPP1 and markers of oxidative stress [malondialdehyde (MDA) and protein carbonyl content] in plasma. At the gene level, associations were observed between overall variation in GPX1 and GPX1 activity (P = 0.02) as well as between overall variation in GPX2 and SEPP1 concentrations (P = 0.03). By individual SNP, two variants in GPX1 (rs8179164 and rs1987628) showed a suggestive association with GPX1 activity (P = 0.10 and 0.08, respectively) and two GPX2 variants (rs4902346 and rs2071566) were associated with SEPP1 concentration (P = 0.004 and 0.002, respectively). Furthermore, two SNP in the SEPP1 gene (rs230813 and rs230819) were associated with MDA concentrations (P = 0.03 and 0.02, respectively). Overall, our study supports the hypothesis that common genetic variants in selenoenzymes affect their activity.
0 Communities
1 Members
0 Resources
15 MeSH Terms
Glucose autoxidation induces functional damage to proteins via modification of critical arginine residues.
Chetyrkin S, Mathis M, Pedchenko V, Sanchez OA, McDonald WH, Hachey DL, Madu H, Stec D, Hudson B, Voziyan P
(2011) Biochemistry 50: 6102-12
MeSH Terms: Amino Acid Motifs, Animals, Arginine, Collagen Type IV, Diabetes Mellitus, Experimental, Glucose, Glyoxal, Hyperglycemia, Male, Micrococcus, Muramidase, Protein Carbonylation, Protein Structure, Tertiary, Proteins, Pyruvaldehyde, Random Allocation, Rats, Rats, Sprague-Dawley
Show Abstract · Added February 25, 2014
Nonenzymatic modification of proteins in hyperglycemia is a major mechanism causing diabetic complications. These modifications can have pathogenic consequences when they target active site residues, thus affecting protein function. In the present study, we examined the role of glucose autoxidation in functional protein damage using lysozyme and RGD-α3NC1 domain of collagen IV as model proteins in vitro. We demonstrated that glucose autoxidation induced inhibition of lysozyme activity as well as NC1 domain binding to α(V)β(3) integrin receptor via modification of critical arginine residues by reactive carbonyl species (RCS) glyoxal (GO) and methylglyoxal while nonoxidative glucose adduction to the protein did not affect protein function. The role of RCS in protein damage was confirmed using pyridoxamine which blocked glucose autoxidation and RCS production, thus protecting protein function, even in the presence of high concentrations of glucose. Glucose autoxidation may cause protein damage in vivo since increased levels of GO-derived modifications of arginine residues were detected within the assembly interface of collagen IV NC1 domains isolated from renal ECM of diabetic rats. Since arginine residues are frequently present within protein active sites, glucose autoxidation may be a common mechanism contributing to ECM protein functional damage in hyperglycemia and oxidative environment. Our data also point out the pitfalls in functional studies, particularly in cell culture experiments, that involve glucose treatment but do not take into account toxic effects of RCS derived from glucose autoxidation.
1 Communities
7 Members
1 Resources
18 MeSH Terms
Evidence of oxidative stress in relation to feeding type during early life in premature infants.
Friel JK, Diehl-Jones B, Cockell KA, Chiu A, Rabanni R, Davies SS, Roberts LJ
(2011) Pediatr Res 69: 160-4
MeSH Terms: Analysis of Variance, Biomarkers, Bottle Feeding, Breast Feeding, Catalase, F2-Isoprostanes, Female, Gestational Age, Glutathione Peroxidase, Humans, Infant Formula, Infant, Newborn, Infant, Premature, Infant, Very Low Birth Weight, Male, Oxidation-Reduction, Oxidative Stress, Pilot Projects, Protein Carbonylation, Superoxide Dismutase
Show Abstract · Added June 1, 2013
Morbidity in the premature (PT) infant may reflect difficult adaptation to oxygen. We hypothesized that feeding including formula feeding (F) and feeding mother's milk (HM) with added fortifier would affect redox status. Therefore, 65 PT infants (birth weight: 1146 ± 261 g; GA: 29 ± 2.5 wk; mean ± SD) were followed biweekly, once oral feeds were introduced. Feeding groups: F (>75% total feeds) and HM (>75% total feeds) were further subdivided according to human milk fortifier (HMF) content of 0-19, 20-49, and ≥ 50%. Oxidative stress was quantified by F2-isoprostanes (F2-IsoPs) in urine, protein carbonyls, and oxygen radical absorbance capacity (ORAC) in plasma. F2-IsoPs (ng/mg creatinine): 0-2 wk, 125 ± 63; 3-4 wk, 191 ± 171; 5-6 wk, 172 ± 83; 7-8 wk, 211 ± 149; 9-10 wk, 222 ± 121; and >10 wk, 183 ± 67. Protein carbonyls from highest [2.41 ± 0.75 (n = 9)] and lowest [2.25 ± 0.89 (n = 12) pmol/μg protein] isoprostane groups did not differ. ORAC: baseline, 6778 ± 1093; discharge, 6639 ± 735 [full term 4 and 12 M, 9010 ± 600 mg (n = 12) TE]. Highest isoprostane values occurred in infants with >50% of their mother's milk fortified. Further research on HMF is warranted.
1 Communities
1 Members
0 Resources
20 MeSH Terms
Low ascorbic acid and increased oxidative stress in gulo(-/-) mice during development.
Harrison FE, Meredith ME, Dawes SM, Saskowski JL, May JM
(2010) Brain Res 1349: 143-52
MeSH Terms: Animals, Animals, Newborn, Ascorbic Acid, Brain, Embryo, Mammalian, F2-Isoprostanes, Female, Gene Expression Regulation, Developmental, Glial Fibrillary Acidic Protein, Glutathione, L-Gulonolactone Oxidase, Liver, Male, Malondialdehyde, Mice, Mice, Knockout, Oxidative Stress, Protein Carbonylation
Show Abstract · Added December 10, 2013
Vitamin C (ascorbic acid, AA) depletion during prenatal and postnatal development can lead to oxidative stress in the developing brain and other organs. Such damage may lead to irreversible effects on later brain function. We studied the relationship between AA deficiency and oxidative stress during development in gulonolactone oxidase (gulo) knockout mice that are unable to synthesize their own ascorbic acid. Heterozygous gulo(+/-) mice can synthesize AA and typically have similar tissue levels to wild-type mice. Gulo(+/-) dams were mated with gulo(+/-) males to provide offspring of each possible genotype. Overall, embryonic day 20 (E20) and postnatal day 1 (P1) pups were protected against oxidative stress by sufficient AA transfer during pregnancy. On postnatal day 10 (P10) AA levels were dramatically lower in liver and cerebellum in gulo(-/-) mice and malondialdehyde (MDA) levels were significantly increased. In postnatal day 18 pups (P18) AA levels decreased further in gulo(-/-) mice and oxidative stress was observed in the accompanying elevations in MDA in liver, and F(2)-isoprostanes in cortex. Further, total glutathione levels were higher in gulo(-/-) mice in cortex, cerebellum and liver, indicating that a compensatory antioxidant system was activated. These data show a direct relationship between AA level and oxidative stress in the gulo(-/-) mice. They reinforce the critical role of ascorbic acid in preventing oxidative stress in the developing brain in animals that, like humans, cannot synthesize their own AA.
Copyright 2010 Elsevier B.V. All rights reserved.
0 Communities
2 Members
0 Resources
18 MeSH Terms
Antioxidant supplementation had positive effects in old rat muscle, but through better oxidative status in other organs.
Mosoni L, Balage M, Vazeille E, Combaret L, Morand C, Zagol-Ikapitte I, Boutaud O, Marzani B, Papet I, Dardevet D
(2010) Nutrition 26: 1157-62
MeSH Terms: Aging, Animals, Antioxidants, Cathepsins, Dietary Supplements, Glutathione, Liver, Male, Muscle, Skeletal, Myocardium, Myofibrils, Oxidation-Reduction, Oxidative Stress, Peptide Hydrolases, Protein Carbonylation, Rats, Rats, Wistar, Spleen, Superoxide Dismutase, Thiobarbituric Acid Reactive Substances
Show Abstract · Added March 27, 2014
OBJECTIVE - Aged muscle is characterized by a defect in the ability of leucine to stimulate protein synthesis. We showed previously that antioxidant supplementation improved the anabolic response to leucine of old muscle and reduced inflammation. The aim of the present study was to determine if the positive effects observed in muscle could be related to an improvement of local muscle oxidative status.
METHODS - Two groups of 20-mo-old male Wistar rats were supplemented or not with rutin, vitamin E, vitamin A, zinc, and selenium during 7 wk. We measured body weight, food intake, oxidative status in muscle and other tissues, gastrocnemius muscle proteolytic activities, and liver glutathione metabolism.
RESULTS - Antioxidant supplementation had no effect on muscle antioxidant capacity, superoxide dismutase activities, and myofibrillar protein carbonyl content and induced an increase in muscle cathepsin activities. In other tissues, antioxidant supplementation increased liver glutathione (reduced plus oxidized glutathione) content, reduced oxidative damage in the liver and spleen (as measured by γ-keto-aldehyde content), and reduced heart thiobarbituric acid-reactive substances.
CONCLUSION - Our results showed that the positive effects of antioxidant supplementation observed previously on the anabolic response to leucine of old muscle were not directly related to an improvement of in situ muscle oxidative status. It could result from reduced systemic inflammation/oxidative stress. The dialog between muscle and other organs should be studied more thoroughly, especially during aging.
Copyright © 2010 Elsevier Inc. All rights reserved.
0 Communities
1 Members
0 Resources
20 MeSH Terms
Studies on biomarkers for oxidative stress in patients with chronic myeloid leukemia.
Singh RK, Tripathi AK, Tripathi P, Singh S, Singh R, Ahmad R
(2009) Hematol Oncol Stem Cell Ther 2: 285-8
MeSH Terms: Adult, Biomarkers, Tumor, Female, Humans, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Lipid Peroxides, Male, Middle Aged, Oxidative Stress, Protein Carbonylation, Thiobarbituric Acid Reactive Substances, Young Adult
Show Abstract · Added July 12, 2013
BACKGROUND - Chronic myeloid leukemia (CML) is a myeloproliferative disorder with a unique genetic rearrangement, the Philadelphia chromosome. High reactive oxygen species (ROS) levels favor oxidative stress, which could play a vital role in normal processes and various pathophysiologies including neoplasm. Biomarkers of oxidative stress are measured as products of oxidized proteins and lipids. Plasma levels of protein carbonyl (PC), thiobarbituric acid reactive substances (TBARS) and total lipid hydroperoxide (LOOH) were used as biomarkers of oxidative stress in the past. The aim of this study was to evaluate the products of protein oxidation and lipid peroxidation in plasma as biomarkers of oxidative stress in CML patients.
PATIENTS AND METHODS - The study included 40 CML patients and 20 age- and sex-matched healthy volunteers. Of 40 CML patients, 28 were in chronic phase (CML-CP) and 12 in accelerated phase (CML-AP). Plasma levels of PC, TBARS and LOOH as biomarkers of oxidative stress were evaluated by spectrophotometric methods.
RESULTS - There were significant differences (P < .05) in plasma levels of PC, TBARS and LOOH in CML, CML-CP and CML-AP patients as compared to controls.
CONCLUSION - PC, TBARS and LOOH might reflect oxidative stress in CML patients and might be used as biomarkers in such patients.
0 Communities
1 Members
0 Resources
12 MeSH Terms
N,N-diethyldithiocarbamate promotes oxidative stress prior to myelin structural changes and increases myelin copper content.
Viquez OM, Lai B, Ahn JH, Does MD, Valentine HL, Valentine WM
(2009) Toxicol Appl Pharmacol 239: 71-9
MeSH Terms: Animals, Blotting, Western, Brain, Copper, Ditiocarb, Glutathione Transferase, Heme Oxygenase (Decyclizing), Isoenzymes, Lipid Peroxidation, Male, Microscopy, Fluorescence, Myelin Sheath, Oxidative Stress, Proteasome Endopeptidase Complex, Protein Carbonylation, Rats, Rats, Sprague-Dawley, Sciatic Nerve, Spinal Cord, Superoxide Dismutase, Superoxide Dismutase-1
Show Abstract · Added May 27, 2014
Dithiocarbamates are a commercially important class of compounds that can produce peripheral neuropathy in humans and experimental animals. Previous studies have supported a requirement for copper accumulation and enhanced lipid peroxidation in dithiocarbamate-mediated myelinopathy. The study presented here extends previous investigations in two areas. Firstly, although total copper levels have been shown to increase within the nerve it has not been determined whether copper is increased within the myelin compartment, the primary site of lesion development. Therefore, the distribution of copper in sciatic nerve was characterized using synchrotron X-ray fluorescence microscopy to determine whether the neurotoxic dithiocarbamate, N,N-diethyldithiocarbamate, increases copper levels in myelin. Secondly, because lipid peroxidation is an ongoing process in normal nerve and the levels of lipid peroxidation products produced by dithiocarbamate exposure demonstrated an unusual cumulative dose response in previous studies the biological impact of dithiocarbamate-mediated lipid peroxidation was evaluated. Experiments were performed to determine whether dithiocarbamate-mediated lipid peroxidation products elicit an antioxidant response through measuring the protein expression levels of three enzymes, superoxide dismutase 1, heme oxygenase 1, and glutathione transferase alpha, that are linked to the antioxidant response element promoter. To establish the potential of oxidative injury to contribute to myelin injury the temporal relationship of the antioxidant response to myelin injury was determined. Myelin structure in peripheral nerve was assessed using multi-exponential transverse relaxation measurements (MET(2)) as a function of exposure duration, and the temporal relationship of protein expression changes relative to the onset of changes in myelin integrity were determined. Initial assessments were also performed to explore the potential contribution of dithiocarbamate-mediated inhibition of proteasome function and inhibition of cuproenzyme activity to neurotoxicity, and also to assess the potential of dithiocarbamates to promote oxidative stress and injury within the central nervous system. These evaluations were performed using an established model for dithiocarbamate-mediated demyelination in the rat utilizing sciatic nerve, spinal cord and brain samples obtained from rats exposed to N,N-diethyldithiocarbamate (DEDC) by intra-abdominal pumps for periods of 2, 4, and 8 weeks and from non exposed controls. The data supported the ability of DEDC to increase copper within myelin and to enhance oxidative stress prior to structural changes detectable by MET(2). Evidence was also obtained that the excess copper produced by DEDC in the central nervous system is redox active and promotes oxidative injury.
0 Communities
2 Members
0 Resources
21 MeSH Terms
Regulation of matrix synthesis, remodeling and accumulation in glomerulosclerosis.
Pozzi A, Voziyan PA, Hudson BG, Zent R
(2009) Curr Pharm Des 15: 1318-33
MeSH Terms: Animals, Extracellular Matrix, Glomerulosclerosis, Focal Segmental, Glycation End Products, Advanced, Homeostasis, Humans, Integrins, Intercellular Signaling Peptides and Proteins, Kidney Glomerulus, Oxidative Stress, Protein Carbonylation, Transcription Factors
Show Abstract · Added February 24, 2014
After injury the body normally undergoes a repair process, however when this event becomes deregulated the pathological condition of fibrosis occurs. There are many similarities with respect to the fundamental mechanisms that regulate sclerosis in different organ systems. In this review we utilize the pathological entity of glomerulosclerosis in the kidney to highlight some of the general paradigms whereby extracellular matrix (ECM) is deposited in greater quantities than it is degraded. Our review discusses how genetic and structural abnormalities of specific ECM components can result in fibrosis. In addition, we outline how some key growth factors, integrins and oxidative stress play a role in the development of glomerulosclerosis.
1 Communities
4 Members
1 Resources
12 MeSH Terms
Global analysis of protein damage by the lipid electrophile 4-hydroxy-2-nonenal.
Codreanu SG, Zhang B, Sobecki SM, Billheimer DD, Liebler DC
(2009) Mol Cell Proteomics 8: 670-80
MeSH Terms: Aldehydes, Biotin, Biotinylation, Cell Extracts, Cell Line, Tumor, Chromatography, Liquid, Humans, Hydrazines, Immunoblotting, Lipid Peroxidation, Lipids, Mass Spectrometry, Neoplasm Proteins, Peptides, Protein Carbonylation, Reproducibility of Results
Show Abstract · Added August 2, 2013
Lipid peroxidation yields a variety of electrophiles, which are thought to contribute to the molecular pathogenesis of diseases involving oxidative stress, yet little is known of the scope of protein damage caused by lipid electrophiles. We identified protein targets of the prototypical lipid electrophile 4-hydroxy-2-nonenal (HNE) in RKO cells treated with 50 or 100 mum HNE. HNE Michael adducts were biotinylated by reaction with biotinamidohexanoic acid hydrazide, captured with streptavidin, and the captured proteins were resolved by one dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis, digested with trypsin, and identified by liquid chromatography-tandem mass spectrometry. Of the 1500+ proteins identified, 417 displayed a statistically significant increase in adduction with increasing HNE exposure concentration. We further identified 18 biotin hydrazide-modified, HNE-adducted peptides by specific capture using anti-biotin antibody and analysis by high resolution liquid chromatography-tandem mass spectrometry. A subset of the identified HNE targets were validated with a streptavidin capture and immunoblotting approach, which enabled detection of adducts at HNE exposures as low as 1 mum. Protein interaction network analysis indicated several subsystems impacted by endogenous electrophiles in oxidative stress, including the 26 S proteasomal and chaperonin containing TCP-1 (CCT) systems involved in protein-folding and degradation, as well as the COP9 signalosome, translation initiation complex, and a large network of ribonucleoproteins. Global analyses of protein lipid electrophile adducts provide a systems-level perspective on the mechanisms of diseases involving oxidative stress.
0 Communities
3 Members
0 Resources
16 MeSH Terms