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Journal articles on the topic 'Proteins Oxidation'

Author: Grafiati

Published: 4 June 2021

Last updated: 20 February 2023

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1

Pattison, David I., Aldwin Suryo Rahmanto, and Michael J. Davies. "Photo-oxidation of proteins." Photochem. Photobiol. Sci. 11, no. 1 (2012): 38–53. http://dx.doi.org/10.1039/c1pp05164d.

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2

FU, Shanlin, Min-Xin FU, W. John BAYNES, R. Suzanne THORPE, and T. Roger DEAN. "Presence of dopa and amino acid hydroperoxides in proteins modified with advanced glycation end products (AGEs): amino acid oxidation products as a possible source of oxidative stress induced by AGE proteins." Biochemical Journal 330, no. 1 (February 15, 1998): 233–39. http://dx.doi.org/10.1042/bj3300233.

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Glycation and subsequent Maillard or browning reactions of glycated proteins, leading to the formation of advanced glycation end products (AGEs), are involved in the chemical modification of proteins during normal aging and have been implicated in the pathogenesis of diabetic complications. Oxidative conditions accelerate the browning of proteins by glucose, and AGE proteins also induce oxidative stress responses in cells bearing AGE receptors. These observations have led to the hypothesis that glycation-induced pathology results from a cycle of oxidative stress, increased chemical modificatio

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3

Burgoyne, Joseph R., and Philip Eaton. "Contemporary techniques for detecting and identifying proteins susceptible to reversible thiol oxidation." Biochemical Society Transactions 39, no. 5 (September 21, 2011): 1260–67. http://dx.doi.org/10.1042/bst0391260.

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Elevated protein oxidation is a widely reported hallmark of most major diseases. Historically, this ‘oxidative stress’ has been considered causatively detrimental, as the protein oxidation events were interpreted simply as damage. However, recent advances have changed this antiquated view; sensitive methodology for detecting and identifying proteins susceptible to oxidation has revealed a fundamental role for this modification in physiological cell signalling during health. Reversible protein oxidation that is dynamically coupled with cellular reducing systems allows oxidative protein modifica

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4

Pandey, Kanti Bhooshan, Mohd Murtaza Mehdi, Pawan Kumar Maurya, and Syed Ibrahim Rizvi. "Plasma Protein Oxidation and Its Correlation with Antioxidant Potential During Human Aging." Disease Markers 29, no. 1 (2010): 31–36. http://dx.doi.org/10.1155/2010/964630.

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Previous studies have indicated that the main molecular characteristic of aging is the progressive accumulation of oxidative damages in cellular macromolecules. Proteins are one of the main molecular targets of age-related oxidative stress, which have been observed during aging process in cellular systems. Reactive oxygen species (ROS) can lead to oxidation of amino acid side chains, formation of protein-protein cross-linkages, and oxidation of the peptide backbones. In the present study, we report the age-dependent oxidative alterations in biomarkers of plasma protein oxidation: protein carbo

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5

Rogers, K. R., C. J. Morris, and D. R. Blake. "Oxidation of thiol in the vimentin cytoskeleton." Biochemical Journal 275, no. 3 (May 1, 1991): 789–91. http://dx.doi.org/10.1042/bj2750789.

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Sublethal doses of H2O2, which induces oxidative stress, cause substantial alteration to the vimentin cytoskeleton in various cell types. We have used a thiol-blot assay to assess thiol status in individual proteins from cell extracts. Vimentin thiol is oxidized in preference to other cytoskeleton proteins. Immunoblot analysis also demonstrated a loss of reactivity to an anti-vimentin monoclonal antibody under non-reducing conditions, possibly due to thiol-group oxidation. During induced oxidative stress a number of proteins become associated with the cytoskeleton extracts.

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6

Lawal, Remilekun O., Fabrizio Donnarumma, and Kermit K. Murray. "Electrospray Photochemical Oxidation of Proteins." Journal of The American Society for Mass Spectrometry 30, no. 11 (September 5, 2019): 2196–99. http://dx.doi.org/10.1007/s13361-019-02313-4.

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7

Hambly, David M., and Michael L. Gross. "Cold Chemical Oxidation of Proteins." Analytical Chemistry 81, no. 17 (September 2009): 7235–42. http://dx.doi.org/10.1021/ac900855f.

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8

Simpson, Richard J. "Performic Acid Oxidation of Proteins." Cold Spring Harbor Protocols 2007, no. 3 (March 2007): pdb.prot4698. http://dx.doi.org/10.1101/pdb.prot4698.

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9

Luna, Carolina, and Mario Estévez. "Oxidative damage to food and human serum proteins: Radical-mediated oxidation vs. glyco-oxidation." Food Chemistry 267 (November 2018): 111–18. http://dx.doi.org/10.1016/j.foodchem.2017.06.154.

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10

Bruckbauer, Steven T., Benjamin B. Minkoff, Michael R. Sussman, and Michael M. Cox. "Proteome Damage Inflicted by Ionizing Radiation: Advancing a Theme in the Research of Miroslav Radman." Cells 10, no. 4 (April 20, 2021): 954. http://dx.doi.org/10.3390/cells10040954.

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Oxidative proteome damage has been implicated as a major contributor to cell death and aging. Protein damage and aging has been a particular theme of the recent research of Miroslav Radman. However, the study of how cellular proteins are damaged by oxidative processes is still in its infancy. Here we examine oxidative changes in the proteomes of four bacterial populations—wild type E. coli, two isolates from E. coli populations evolved for high levels of ionizing radiation (IR) resistance, and D. radiodurans—immediately following exposure to 3000 Gy of ionizing radiation. By a substantial marg

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11

CZAPSKI, Grzegorz A., Diana AVRAM, Dmitri V. SAKHAROV, Karel W. A. WIRTZ, Joanna B. STROSZNAJDER, and Everard H. W. PAP. "Activated neutrophils oxidize extracellular proteins of endothelial cells in culture: effect of nitric oxide donors." Biochemical Journal 365, no. 3 (August 1, 2002): 897–902. http://dx.doi.org/10.1042/bj20011206.

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Protein oxidation of human umbilical-vein endothelial cells (HUVEC) in culture was examined under various conditions of oxidative stress. Extracellular protein (ECP) oxidation was assessed by determining dityrosine bond formation, which is indicated by the covalent coupling of the membrane-impermeable tyramine—fluorescein conjugate (TyrFluo) to HUVEC proteins. The acetylated membrane-permeable form of TyrFluo (acetylTyrFluo) was used for the determination of intracellular protein (ICP) oxidation. Oxidative stress was induced by exposing the HUVEC to PMA-activated human neutrophils, to a horser

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12

Gladstone, Igor M., and Rodney L. Levine. "Oxidation of Proteins in Neonatal Lungs." Pediatrics 93, no. 5 (May 1, 1994): 764–68. http://dx.doi.org/10.1542/peds.93.5.764.

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Objective. To develop a method capable of quantifying the oxidative modification of proteins in pulmonary fluid obtained during routine suctioning of neonates receiving ventilation, thus providing an integrated assessment of antioxidant defenses. Design. Consecutive sample of neonates receiving ventilation. Setting. Neonatal intensive care unit. Patients. Twenty-six neonates receiving ventilation with a gestational age of 24 to 42 weeks, from whom 246 samples were collected and analyzed. Measurements and results. The carbonyl content in the lavage samples was measured by reaction with 2,4-dini

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13

Chen, Chiao-nan, Deborah A. Ferrington, and LaDora V. Thompson. "Carbonic anhydrase III and four-and-a-half LIM protein 1 are preferentially oxidized with muscle unloading." Journal of Applied Physiology 105, no. 5 (November 2008): 1554–61. http://dx.doi.org/10.1152/japplphysiol.90680.2008.

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The identities of proteins that show disuse-related changes in the content of oxidative modification are unknown. Furthermore, it is unknown whether the global accumulation of oxidized proteins is greater in aged animals with muscle disuse. The purposes of this study are 1) to identify the exact proteins that show disuse-related changes in oxidation levels and 2) to test the hypothesis that the global accumulation of oxidized proteins with muscle disuse would be greater in aged animals. Adult and old rats were randomized into four groups: weight bearing and 3, 7, or 14 days of hindlimb unloadi

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Quinlan, Roy A., та Philip J. Hogg. "γ-Crystallin redox–detox in the lens". Journal of Biological Chemistry 293, № 46 (16 листопада 2018): 18010–11. http://dx.doi.org/10.1074/jbc.h118.006240.

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In the vertebrate eye, limiting oxidation of proteins and lipids is key to maintaining lens function and avoiding cataract formation. A study by Serebryany et al. identifies a surprising contributor to the eye's oxidative defense in their demonstration that γD-crystallin (HγD) functions as an oxidoreductase and uses disulfide exchange to initiate aggregation of mutant crystallins that mimic oxidative damage. These insights suggest a mechanism by which a dynamic pool of closely packed proteins might avoid oxidation-driven protein-folding traps, providing new avenues to understand the basis of a

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15

Eaton, P. "Reversible Cysteine-Targeted Oxidation of Proteins during Renal Oxidative Stress." Journal of the American Society of Nephrology 14, no. 90003 (August 1, 2003): 290S—296. http://dx.doi.org/10.1097/01.asn.0000078024.50060.c6.

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16

Zheng, Kai, Diya Ren, Y. John Wang, Wayne Lilyestrom, Thomas Scherer, Justin K. Y. Hong, and Junyan A. Ji. "Monoclonal Antibody Aggregation Associated with Free Radical Induced Oxidation." International Journal of Molecular Sciences 22, no. 8 (April 12, 2021): 3952. http://dx.doi.org/10.3390/ijms22083952.

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Oxidation is an important degradation pathway of protein drugs. The susceptibility to oxidation is a common concern for therapeutic proteins as it may impact product efficacy and patient safety. In this work, we used 2,2′-azobis (2-amidinopropane) dihydrochloride (AAPH) as an oxidative stress reagent to evaluate the oxidation of therapeutic antibodies. In addition to the oxidation of methionine (Met) and tryptophan (Trp) residues, we also observed an increase of protein aggregation. Size-exclusion chromatography and multi-angle light scattering showed that the soluble aggregates induced by AAP

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17

Li, Bowen, Ling Mo, Yuhui Yang, Shuai Zhang, Jingbing Xu, Yueting Ge, Yuncong Xu, Yonghui Shi, and Guowei Le. "Processing milk causes the formation of protein oxidation products which impair spatial learning and memory in rats." RSC Advances 9, no. 39 (2019): 22161–75. http://dx.doi.org/10.1039/c9ra03223a.

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Eating a high protein oxidation diet leads to oxidative stress, leading to spatial learning and memory impairment. Dairy products processing conditions should be regulated to control the oxidation level of proteins, improve eating habits, and avoid damage to human health.

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18

Helander, Linda, Animesh Sharma, Hans E. Krokan, Kristjan Plaetzer, Barbara Krammer, Nicole Tortik, Odrun A. Gederaas, Geir Slupphaug, and Lars Hagen. "Photodynamic treatment with hexyl-aminolevulinate mediates reversible thiol oxidation in core oxidative stress signaling proteins." Molecular BioSystems 12, no. 3 (2016): 796–805. http://dx.doi.org/10.1039/c5mb00744e.

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19

Stadtman, E. R., C. N. Oliver, P. E. Starke-Reed, and S. G. Rhee. "Age-Related Oxidation Reaction in Proteins." Toxicology and Industrial Health 9, no. 1-2 (January 1993): 187–96. http://dx.doi.org/10.1177/0748233793009001-213.

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20

Kim, Geumsoo, Stephen J. Weiss, and Rodney L. Levine. "Methionine oxidation and reduction in proteins." Biochimica et Biophysica Acta (BBA) - General Subjects 1840, no. 2 (February 2014): 901–5. http://dx.doi.org/10.1016/j.bbagen.2013.04.038.

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21

Haman, François, François Péronnet, Glen P. Kenny, Éric Doucet, Denis Massicotte, Carole Lavoie, and Jean-Michel Weber. "Effects of carbohydrate availability on sustained shivering I. Oxidation of plasma glucose, muscle glycogen, and proteins." Journal of Applied Physiology 96, no. 1 (January 2004): 32–40. http://dx.doi.org/10.1152/japplphysiol.00427.2003.

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Carbohydrates (CHO) can play an important thermogenic role during shivering, but the effect of their availability on the use of other oxidative fuels is unclear. Using indirect calorimetry and tracer methods ([U-13C]glucose ingestion), we have determined the specific contributions of plasma glucose, muscle glycogen, proteins, and lipids to total heat production (Ḣprod) in men exposed to cold for 2-h (liquid-conditioned suit perfused with 10°C water). Measurements were made after low-CHO diet and exercise (Lo) and high-CHO diet without exercise (Hi). The size of CHO reserves had no effect on Ḣp

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22

Pietzsch, Jens, Ralf Bergmann, and Steffi Kopprasch. "Analysis of non-protein amino acids as specific markers of low density lipoprotein apolipoprotein B-100 oxidation in human atherosclerotic lesions: the use ofN(O)-ethoxycarbonyl trifluoroethyl ester derivatives and GC-MS1." Spectroscopy 18, no. 2 (2004): 177–83. http://dx.doi.org/10.1155/2004/802375.

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Oxidative modification of proteins can interfere with critical cellular functions, and is widely regarded as a crucial event in the pathogenesis of various diseases ranging from rheumatoid arthritis to atherosclerosis and cancer. In this line, a new GC‒MS methodology usingN(O)‒ethoxycarbonyl trifluoroethyl amino acid esters (ECEE‒F3) for rapid and sensitive determination of 3‒chlorotyrosine, 5‒hydroxy‒2‒aminovaleric acid (HAVA), and 6‒hydroxy‒2‒aminocaproic acid (HACA) in proteins has been developed. 3‒Chlorotyrosine is a highly specific marker of myeloperoxidase catalyzed protein oxidation, w

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23

Raajendiran, Arthe, Christoph Krisp, David P. De Souza, Geraldine Ooi, Paul R. Burton, Renea A. Taylor, Mark P. Molloy, and Matthew J. Watt. "Proteome analysis of human adipocytes identifies depot-specific heterogeneity at metabolic control points." American Journal of Physiology-Endocrinology and Metabolism 320, no. 6 (June 1, 2021): E1068—E1084. http://dx.doi.org/10.1152/ajpendo.00473.2020.

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Adipocyte metabolism varies depending on anatomical location and the adipocyte protein composition may orchestrate this heterogeneity. We used SWATH proteomics in patient-matched human upper- (visceral and subcutaneous) and lower-body (glutealfemoral) adipocytes and detected 4,220 proteins and distinguishable regional proteomes. Upper-body adipocyte proteins were associated with glycolysis, de novo lipogenesis, mitochondrial dysfunction, and oxidative stress, whereas lower-body adipocyte proteins were associated with enhanced PPARα activation, fatty acid, and BCAA oxidation, TCA cycle flux, an

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Krisko, Anita, and Miroslav Radman. "Protein damage, ageing and age-related diseases." Open Biology 9, no. 3 (March 2019): 180249. http://dx.doi.org/10.1098/rsob.180249.

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Ageing is considered as a snowballing phenotype of the accumulation of damaged dysfunctional or toxic proteins and silent mutations (polymorphisms) that sensitize relevant proteins to oxidative damage as inborn predispositions to age-related diseases. Ageing is not a disease, but it causes (or shares common cause with) age-related diseases as suggested by similar slopes of age-related increase in the incidence of diseases and death. Studies of robust and more standard species revealed that dysfunctional oxidatively damaged proteins are the root cause of radiation-induced morbidity and mortalit

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Tarrago, Lionel, Sandrine Grosse, David Lemaire, Laetitia Faure, Mathilde Tribout, Marina I. Siponen, Mila Kojadinovic-Sirinelli, David Pignol, Pascal Arnoux, and Monique Sabaty. "Reduction of Protein Bound Methionine Sulfoxide by a Periplasmic Dimethyl Sulfoxide Reductase." Antioxidants 9, no. 7 (July 14, 2020): 616. http://dx.doi.org/10.3390/antiox9070616.

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In proteins, methionine (Met) can be oxidized into Met sulfoxide (MetO). The ubiquitous methionine sulfoxide reductases (Msr) A and B are thiol-oxidoreductases reducing MetO. Reversible Met oxidation has a wide range of consequences, from protection against oxidative stress to fine-tuned regulation of protein functions. Bacteria distinguish themselves by the production of molybdenum-containing enzymes reducing MetO, such as the periplasmic MsrP which protects proteins during acute oxidative stress. The versatile dimethyl sulfoxide (DMSO) reductases were shown to reduce the free amino acid MetO

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Fischer, Manuel, Sebastian Horn, Anouar Belkacemi, Kerstin Kojer, Carmelina Petrungaro, Markus Habich, Muna Ali, et al. "Protein import and oxidative folding in the mitochondrial intermembrane space of intact mammalian cells." Molecular Biology of the Cell 24, no. 14 (July 15, 2013): 2160–70. http://dx.doi.org/10.1091/mbc.e12-12-0862.

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Oxidation of cysteine residues to disulfides drives import of many proteins into the intermembrane space of mitochondria. Recent studies in yeast unraveled the basic principles of mitochondrial protein oxidation, but the kinetics under physiological conditions is unknown. We developed assays to follow protein oxidation in living mammalian cells, which reveal that import and oxidative folding of proteins are kinetically and functionally coupled and depend on the oxidoreductase Mia40, the sulfhydryl oxidase augmenter of liver regeneration (ALR), and the intracellular glutathione pool. Kinetics o

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Starke-Reed, Pamela E., Mark B. Reid, I. Tong Mak, Jay H. Kramer, and William B. Weglicki. "Oxidation of cardiac cellular proteins and enzymes during acute oxidative stress." Free Radical Biology and Medicine 9 (January 1990): 88. http://dx.doi.org/10.1016/0891-5849(90)90482-x.

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Tienson, Heather L., Deepa V. Dabir, Sonya E. Neal, Rachel Loo, Samuel A. Hasson, Pinmanee Boontheung, Sung-Kun Kim, Joseph A. Loo, and Carla M. Koehler. "Reconstitution of the Mia40-Erv1 Oxidative Folding Pathway for the Small Tim Proteins." Molecular Biology of the Cell 20, no. 15 (August 2009): 3481–90. http://dx.doi.org/10.1091/mbc.e08-10-1062.

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Mia40 and Erv1 execute a disulfide relay to import the small Tim proteins into the mitochondrial intermembrane space. Here, we have reconstituted the oxidative folding pathway in vitro with Tim13 as a substrate and determined the midpoint potentials of Mia40 and Tim13. Specifically, Mia40 served as a direct oxidant of Tim13, and Erv1 was required to reoxidize Mia40. During oxidation, four electrons were transferred from Tim13 with the insertion of two disulfide bonds in succession. The extent of Tim13 oxidation was directly dependent on Mia40 concentration and independent of Erv1 concentration

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Irokawa, Hayato, Satoshi Numasaki, Shin Kato, Kenta Iwai, Atsushi Inose-Maruyama, Takumi Ohdate, Gi-Wook Hwang, Takashi Toyama, Toshihiko Watanabe, and Shusuke Kuge. "Comprehensive analyses of the cysteine thiol oxidation of PKM2 reveal the effects of multiple oxidation on cellular oxidative stress response." Biochemical Journal 478, no. 7 (April 16, 2021): 1453–70. http://dx.doi.org/10.1042/bcj20200897.

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Redox regulation of proteins via cysteine residue oxidation is involved in the control of various cellular signal pathways. Pyruvate kinase M2 (PKM2), a rate-limiting enzyme in glycolysis, is critical for the metabolic shift from glycolysis to the pentose phosphate pathway under oxidative stress in cancer cell growth. The PKM2 tetramer is required for optimal pyruvate kinase (PK) activity, whereas the inhibition of inter-subunit interaction of PKM2 induced by Cys358 oxidation has reduced PK activity. In the present study, we identified three oxidation-sensitive cysteine residues (Cys358, Cys42

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Mukthapura, Anita, Avinash Shimogga, Vinodchandran K, Beena Shetty, and Gayathri Rao. "Oxidative Products of Proteins and Antioxidant Potential of Thiols in Gastric Carcinoma Patients." Journal of Medical Biochemistry 29, no. 2 (April 1, 2010): 102–6. http://dx.doi.org/10.2478/v10011-010-0013-z.

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Oxidative Products of Proteins and Antioxidant Potential of Thiols in Gastric Carcinoma PatientsIt has been suggested that oxidative stress defined as a shift in antioxidant/oxidant balance towards oxidants is associated with the pathogenesis of many diseases, including carcinogenesis. Reactive oxygen species can induce carcinogenesis via injury to macromolecules such as DNA, carbohydrates and proteins. Forty primary gastric carcinoma patients and 40 healthy controls were included in the study. Advanced oxidation protein products, total thiols, total protein, albumin in plasma, % hemolysis in

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31

Maleknia, Simin D., and Kevin M. Downard. "Protein Footprinting with Radical Probe Mass Spectrometry- Two Decades of Achievement." Protein & Peptide Letters 26, no. 1 (February 13, 2019): 4–15. http://dx.doi.org/10.2174/0929866526666181128124241.

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Background: Radical Probe Mass Spectrometry (RP-MS) describes a pioneering methodology in structural biology that enables the study of protein structures, their interactions, and dynamics on fast timescales (down to sub-milliseconds). Hydroxyl radicals (•OH) generated directly from water within aqueous solutions induce the oxidation of reactive, solvent accessible amino acid side chains that are then analyzed by mass spectrometry. Introduced in 1998 at the American Society for Mass Spectrometry annual conference, RP-MS was first published on in 1999. Objective: This review article describes de

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Zergeroglu, Murat A., Michael J. McKenzie, R. Andrew Shanely, Darin Van Gammeren, Keith C. DeRuisseau, and Scott K. Powers. "Mechanical ventilation-induced oxidative stress in the diaphragm." Journal of Applied Physiology 95, no. 3 (September 2003): 1116–24. http://dx.doi.org/10.1152/japplphysiol.00824.2002.

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Prolonged mechanical ventilation (MV) results in oxidative damage in the diaphragm; however, it is unclear whether this MV-induced oxidative injury occurs rapidly or develops slowly over time. Furthermore, it is unknown whether both soluble (cytosolic) and insoluble (myofibrillar) proteins are equally susceptible to oxidation during MV. These experiments tested two hypotheses: 1) MV-induced oxidative injury in the diaphragm occurs within the first 6 h after the initiation of MV; and 2) MV is associated with oxidative modification of both soluble and insoluble proteins. Adult Sprague-Dawley rat

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Dick, Jeffrey M. "Average oxidation state of carbon in proteins." Journal of The Royal Society Interface 11, no. 100 (November 6, 2014): 20131095. http://dx.doi.org/10.1098/rsif.2013.1095.

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The formal oxidation state of carbon atoms in organic molecules depends on the covalent structure. In proteins, the average oxidation state of carbon ( Z C ) can be calculated as an elemental ratio from the chemical formula. To investigate oxidation–reduction (redox) patterns, groups of proteins from different subcellular locations and phylogenetic groups were selected for comparison. Extracellular proteins of yeast have a relatively high oxidation state of carbon, corresponding with oxidizing conditions outside of the cell. However, an inverse relationship between Z C and redox potential occu

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Zhu, Xueshen, Zhenghao Ma, Xinyu Zhang, Xuefang Huang, Junya Liu, and Xinbo Zhuang. "Effect of Malondialdehyde-Induced Oxidation Modification on Physicochemical Changes and Gel Characteristics of Duck Myofibrillar Proteins." Gels 8, no. 10 (October 6, 2022): 633. http://dx.doi.org/10.3390/gels8100633.

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This paper focuses on the effect of malondialdehyde-induced oxidative modification (MiOM) on the gel properties of duck myofibrillar proteins (DMPs). DMPs were first prepared and treated with oxidative modification at different concentrations of malondialdehyde (0, 0.5, 2.5, 5.0, and 10.0 mmol/L). The physicochemical changes (carbonyl content and free thiol content) and gel properties (gel whiteness, gel strength, water holding capacity, rheological properties, and microstructural properties) were then investigated. The results showed that the content of protein carbonyl content increased with

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Márquez-Lázaro, Johana, Darío Méndez-Cuadro, and Erika Rodríguez-Cavallo. "Residues of Fluoroquinolone Antibiotics Induce Carbonylation and Reduce In Vitro Digestion of Sarcoplasmic and Myofibrillar Beef Proteins." Foods 9, no. 2 (February 11, 2020): 170. http://dx.doi.org/10.3390/foods9020170.

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Although the impact of oxidation on human health has been of growing interest, the oxidation of proteins, major component of meat, has received little attention. This paper describes the in vitro effect of five fluoroquinolones (FQs) on carbonylation of sarcoplasmic and myofibrillar proteins of beef when found at concentrations close to the maximum residue limit (MRL). Samples were treated individually with the FQs, determining in each protein fraction the carbonyl index, protein content and oxidized proteins identification, using 2,4-dinitrophenyhydrazine (DNPH) alkaline assay, Western blot a

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Perry, G., D. A. Zelasko, L. M. Sayre, and M. A. Smith. "Oxidative Damage to Axonal Cytoskeletal Proteins." Microscopy and Microanalysis 3, S2 (August 1997): 43–44. http://dx.doi.org/10.1017/s1431927600007108.

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Proteins of the axonal cytoskeleton, particularly neurofilament and microtubule-associated protein τ, should be particularly sensitive to the effects of oxidative modification due to their high content of lysine, an amino acid that is particularly susceptible to direct oxidization as well as adduction by carbonyls produced from lipid and sugar oxidation. To understand the susceptibility of the cytoskeleton to oxidative modification and whether such modification is related to the physiological function of the cytoskeleton, we undertook a cytological analysis of motor neurons isolated from mouse

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Nlelsen, Henrik K., J. Löliger, and R. F. Hurrell. "Reactions of proteins with oxidizing lipids." British Journal of Nutrition 53, no. 1 (January 1985): 61–73. http://dx.doi.org/10.1079/bjn19850011.

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1. The reactions between protein-bound amino acids and oxidizing lipid were investigated in a whey protein-methyl linolenate (C18.3)–water model system. The extent of fat oxidation was followed by measuring oxygen uptake, hydroperoxide formation and hydrocarbon (ethane and pentane) formation.2. Significant losses occurred with lysine (up to 71 %), tryptophan (up to 31 %) and histidine (up to 57%). Methionine was extensively oxidized to its sulphoxide but less than 2% was further oxidized to the sulphone. No other amino acids were affected.3. Increasing storage temperature (20°, 37°, 55°) resul

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Choromańska, Barbara, Piotr Myśliwiec, Tomasz Kozłowski, Magdalena Łuba, Piotr Wojskowicz, Jacek Dadan, Hanna Myśliwiec, et al. "Antioxidant Barrier and Oxidative Damage to Proteins, Lipids, and DNA/RNA in Adrenal Tumor Patients." Oxidative Medicine and Cellular Longevity 2021 (June 22, 2021): 1–19. http://dx.doi.org/10.1155/2021/5543531.

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This study is the first to assess redox balance, glutathione metabolism, and oxidative damage to RNA/DNA, proteins, and lipids in the plasma/serum and urine of patients with adrenal masses. The study included 70 patients with adrenal tumors divided into three subgroups: incidentaloma ( n = 30 ), pheochromocytoma ( n = 20 ), and Cushing’s/Conn’s adenoma ( n = 20 ), as well as 60 healthy controls. Blood and urine samples were collected before elective endoscopic adrenalectomy. Antioxidant defense capacity was significantly decreased (serum/plasma: superoxide dismutase (SOD), catalase (CAT) and r

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Yan, Liang-Jun. "Protein Redox Modification as a Cellular Defense Mechanism against Tissue Ischemic Injury." Oxidative Medicine and Cellular Longevity 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/343154.

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Protein oxidative or redox modifications induced by reactive oxygen species (ROS) or reactive nitrogen species (RNS) not only can impair protein function, but also can regulate and expand protein function under a variety of stressful conditions. Protein oxidative modifications can generally be classified into two categories: irreversible oxidation and reversible oxidation. While irreversible oxidation usually leads to protein aggregation and degradation, reversible oxidation that usually occurs on protein cysteine residues can often serve as an “on and off” switch that regulates protein functi

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Ngo, Vy, Nadun C. Karunatilleke, Anne Brickenden, Wing-Yiu Choy, and Martin L. Duennwald. "Oxidative Stress-Induced Misfolding and Inclusion Formation of Nrf2 and Keap1." Antioxidants 11, no. 2 (January 27, 2022): 243. http://dx.doi.org/10.3390/antiox11020243.

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Cells that experience high levels of oxidative stress respond by inducing antioxidant proteins through activation of the protein transcription factor nuclear factor erythroid 2-related factor 2 (Nrf2). Nrf2 is negatively regulated by the E3 ubiquitin ligase Kelch-like ECH-associated protein 1 (Keap1), which binds to Nrf2 to facilitate its ubiquitination and ensuing proteasomal degradation under basal conditions. Here, we studied protein folding and misfolding in Nrf2 and Keap1 in yeast, mammalian cells, and purified proteins under oxidative stress conditions. Both Nrf2 and Keap1 are susceptibl

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Ortegón Salas, Clara, Katharina Schneider, Christopher Horst Lillig, and Manuela Gellert. "Signal-regulated oxidation of proteins via MICAL." Biochemical Society Transactions 48, no. 2 (March 27, 2020): 613–20. http://dx.doi.org/10.1042/bst20190866.

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Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificit

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Stadtman, E. R., and C. N. Oliver. "Metal-catalyzed oxidation of proteins. Physiological consequences." Journal of Biological Chemistry 266, no. 4 (February 1991): 2005–8. http://dx.doi.org/10.1016/s0021-9258(18)52199-2.

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Nacak, B., H. S. Kavuşan та M. Serdaroğlu. "Effect of α-tocopherol, rosemary extract and their combination on lipid and protein oxidation in beef sausages". IOP Conference Series: Earth and Environmental Science 854, № 1 (1 жовтня 2021): 012062. http://dx.doi.org/10.1088/1755-1315/854/1/012062.

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Abstract This study focuses on the oxidative changes in lipids and proteins of beef sausages with incorporated a-tocopherol, rosemary extract or their combination during 3 months’ storage at 4°C. For this purpose, sausages were formulated with no antioxidant (Control, C), 200 ppm a-tocopherol (T), 200 ppm rosemary extract (R), and 100 ppm a-tocopherol + 100 ppm rosemary extract (TR). To observe oxidative changes in lipids; peroxide value, thiobarbituric acid reactive substances (TBARS), and total oxidation value (TOTOX), in proteins; sulfhydryl and carbonyl contents were measured. Use of antio

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Sumner, Edward R., Anupama Shanmuganathan, Theodora C. Sideri, Sylvia A. Willetts, John E. Houghton, and Simon V. Avery. "Oxidative protein damage causes chromium toxicity in yeast." Microbiology 151, no. 6 (June 1, 2005): 1939–48. http://dx.doi.org/10.1099/mic.0.27945-0.

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Oxidative damage in microbial cells occurs during exposure to the toxic metal chromium, but it is not certain whether such oxidation accounts for the toxicity of Cr. Here, a Saccharomyces cerevisiae sod1Δ mutant (defective for the Cu,Zn-superoxide dismutase) was found to be hypersensitive to Cr(VI) toxicity under aerobic conditions, but this phenotype was suppressed under anaerobic conditions. Studies with cells expressing a Sod1p variant (Sod1H46C) showed that the superoxide dismutase activity rather than the metal-binding function of Sod1p was required for Cr resistance. To help identify the

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Alvarado, Gerardo, Attila Tóth, Éva Csősz, Gergő Kalló, Katalin Dankó, Zoltán Csernátony, Ann Smith, et al. "Heme-Induced Oxidation of Cysteine Groups of Myofilament Proteins Leads to Contractile Dysfunction of Permeabilized Human Skeletal Muscle Fibres." International Journal of Molecular Sciences 21, no. 21 (October 31, 2020): 8172. http://dx.doi.org/10.3390/ijms21218172.

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Heme released from red blood cells targets a number of cell components including the cytoskeleton. The purpose of the present study was to determine the impact of free heme (20–300 µM) on human skeletal muscle fibres made available during orthopedic surgery. Isometric force production and oxidative protein modifications were monitored in permeabilized skeletal muscle fibre segments. A single heme exposure (20 µM) to muscle fibres decreased Ca2+-activated maximal (active) force (Fo) by about 50% and evoked an approximately 3-fold increase in Ca2+-independent (passive) force (Fpassive). Oxidatio

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Kiffin, Roberta, Christopher Christian, Erwin Knecht, and Ana Maria Cuervo. "Activation of Chaperone-mediated Autophagy during Oxidative Stress." Molecular Biology of the Cell 15, no. 11 (November 2004): 4829–40. http://dx.doi.org/10.1091/mbc.e04-06-0477.

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Oxidatively damaged proteins accumulate with age in almost all cell types and tissues. The activity of chaperone-mediated autophagy (CMA), a selective pathway for the degradation of cytosolic proteins in lysosomes, decreases with age. We have analyzed the possible participation of CMA in the removal of oxidized proteins in rat liver and cultured mouse fibroblasts. Added to the fact that CMA substrates, when oxidized, are more efficiently internalized into lysosomes, we have found a constitutive activation of CMA during oxidative stress. Oxidation-induced activation of CMA correlates with highe

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Hopps, Eugenia, and Gregorio Caimi. "Protein Oxidation in Metabolic Syndrome." Clinical & Investigative Medicine 36, no. 1 (February 1, 2013): 1. http://dx.doi.org/10.25011/cim.v36i1.19399.

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Purpose: Oxidative stress plays a pivotal role in the pathogenesis of the metabolic syndrome and in the progression of its complications. Carbonylated proteins are a stable marker of severe oxidative stress because damage to the protein structure is irreversible and may cause an inhibition of their enzymatic activity or an increased susceptibility to proteolysis. There are few data regarding protein oxidation in metabolic syndrome, although elevated levels of carbonyl groups are often detected in subjects with obesity, diabetes mellitus, hypertension or dyslipidemia, well-known components of t

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Umstead, Todd M., Willard M. Freeman, Vernon M. Chinchilli, and David S. Phelps. "Age-related changes in the expression and oxidation of bronchoalveolar lavage proteins in the rat." American Journal of Physiology-Lung Cellular and Molecular Physiology 296, no. 1 (January 2009): L14—L29. http://dx.doi.org/10.1152/ajplung.90366.2008.

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The incidence and severity of many lung diseases change with age. Some diseases, such as pneumonia, occur with increased frequency in children and the elderly. Proteins obtained by bronchoalveolar lavage (BAL) serve as the first line of defense against inhaled toxins and pathogens. Age-related changes in BAL protein expression and oxidative modification were examined in juvenile (1 mo), young adult (2 mo), and aged (18 mo) F344 rats using two-dimensional difference gel electrophoresis (2D-DIGE), matrix-assisted laser desorption ionization-time of flight/time of flight (MALDI-ToF/ToF) tandem ma

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Shaw, C. S., C. Swinton, M. G. Morales-Scholz, N. McRae, T. Erftemeyer, A. Aldous, R. M. Murphy, and K. F. Howlett. "Impact of exercise training status on the fiber type-specific abundance of proteins regulating intramuscular lipid metabolism." Journal of Applied Physiology 128, no. 2 (February 1, 2020): 379–89. http://dx.doi.org/10.1152/japplphysiol.00797.2019.

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Endurance training enhances the capacity for fat oxidation during exercise due to increased utilization of intramuscular lipid (IMCL). This study quantitatively investigated the impact of exercise training status on muscle fiber type-specific abundance of regulatory proteins involved in IMCL utilization. Endurance-trained [ n = 7 subjects, peak oxygen consumption (V̇o2peak) 62.6 ± 4.1 (SD) mL·min−1·kg−1] and non-endurance-trained ( n = 8 subjects, V̇o2peak 44.9 ± 5.3 mL·min−1·kg−1) young men completed an incremental exercise test to determine maximal fat oxidation (MFO) and maximal oxygen upta

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Gebicki, J. M., J. Du, J. Collins, and H. Tweeddale. "Peroxidation of proteins and lipids in suspensions of liposomes, in blood serum, and in mouse myeloma cells." Acta Biochimica Polonica 47, no. 4 (December 31, 2000): 901–11. http://dx.doi.org/10.18388/abp.2000_3945.

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There is growing evidence that proteins are early targets of reactive oxygen species, and that the altered proteins can in turn damage other biomolecules. In this study, we measured the effects of proteins on the oxidation of liposome phospholipid membranes, and the formation of protein hydroperoxides in serum and in cultured cells exposed to radiation-generated hydroxyl free radicals. Lysozyme, which did not affect liposome stability, gave 50% protection when present at 0.3 mg/ml, and virtually completely prevented lipid oxidation at 10 mg/ml. When human blood serum was irradiated, lipids wer

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