Nitrotyrosine and Chlorotyrosine: Clinical Significance and Biological Functions in the Vascular System

Mohiuddin, Imran; Chai, Hong; Lin, Peter H.; Lumsden, Alan B.; Yao, Qizhi; Chen, Changyi

doi:10.1016/j.jss.2005.10.008

Cited by 99 publications

(75 citation statements)

References 56 publications

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“…Nitrotyrosine is a very stable altered amino acid (an addition of a nitro group to the benzene ring of tyrosine) that can be found both as a single amino acid and belong to a complete protein in the cell. It has been found in elevated levels in a lot of inflammatory conditions like atherosclerosis, rheumatoid arthritis, influenza, pancratitis, cholecystitis, Diabetes Mellitus, ulcerative colitis and Crohn´s disease (5,(14)(15) and is therefore a good indicator of the radical production. In the present study nitrotyrosine showed elevated levels in both the red streak and in the squamous epithelium taken from the ERD-patients compared to controls.…”

Section: Discussionmentioning

confidence: 99%

Expression of Reactive Oxygen Species in Reflux Disease

Andréasson¹,

Casselbrant²

2011

Gastrointestinal Endoscopy

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Section: Discussionmentioning

confidence: 99%

Expression of Reactive Oxygen Species in Reflux Disease

Andréasson¹,

Casselbrant²

2011

Gastrointestinal Endoscopy

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“…These changes often result in the alteration of function or inhibition of enzyme activities. The protein adducts have been observed in several pathologic conditions [67,68], suggesting their deleterious effects. However, whether these endogenous modifications are produced in a controlled manner, they may also control physiological responses [69,70].…”

Section: Protein Adductsmentioning

confidence: 99%

“…It is important to stress that the presence of proteins containing nitrotyrosine residues, for example, has been a biomarker of damage by reactive species [67,68]. The tyrosine nitration occurs by addition of NO 2 to the ortho position of the phenolic ring of this amino acid.…”

Section: Protein Adductsmentioning

confidence: 99%

“…ONOO À , its protonated form peroxynitrous acid (ONOOH), and its secondary radical product, react with electron-rich groups, such as sulfhydryls, ironsulphur centers, zinc-thiolates and active site sulfhydryl in tyrosine phosphatases [67,68,72,73].…”

Section: Protein Adductsmentioning

confidence: 99%

“…The protein adducts have been observed in several pathologic conditions [67,68], suggesting their deleterious effects. However, whether these endogenous modifications are produced in a controlled manner, they may also control physiological responses [69,70].It is important to stress that the presence of proteins containing nitrotyrosine residues, for example, has been a biomarker of damage by reactive species [67,68]. The tyrosine nitration occurs by addition of NO 2 to the ortho position of the phenolic ring of this amino acid.…”

mentioning

confidence: 99%

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Oxidative Stress: Noxious but Also Vital

Bagatini¹,

Jaques²,

Oliveira³

et al. 2018

Novel Prospects in Oxidative and Nitrosative Stress

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The imbalance between reactive oxygen species (ROS) production and antioxidant defenses determines the condition called oxidative stress. When there is an increase in ROS production or a decrease in the antioxidant defenses, this systemic antioxidant/pro-oxidant imbalance may lead to the accumulation of oxidative damage, which, in turn, may lead to a modification of biomolecules. These consist of reactions resulting in protein adducts, DNA oxidation, and formation of lipid peroxides, which, in turn, reduce the cellular functional capacity and increase the risk of disease development. The body has natural scavenging systems against free radicals and other reactive species. However, sometimes the endogenous antioxidant capacity is exceeded by the production of ROS. When this occurs, exogenous antioxidants exert important function for the human health. These bioactive compounds act preventing and neutralizing the formation of new reactive species and free radical s .I ns o m ec a s e s ,a n increase of ROS can help the host to resolve an infection or even to control the tumor growth. Finally, the levels of ROS can be perceived by signal transduction pathways involving known targets(i.e.,p53,Ras,andNF-κB) and regulate physiopathological events such as the cellular cycle, apoptosis, and inflammation.Keywords: reactive species, cellular oxidation, antioxidant system, health, disease © 2018 The Author(s). Licensee IntechOpen. This chapter is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Cellular respiration and generation of reactive species in the mitochondria: implications in cell viability and agingOxidative phosphorylation is the center of energy metabolism in plants, animals and several microbial life forms [1]. In eukaryotes, this process occurs in mitochondria. The mitochondria is a cytoplasmic organelle surrounded by two membranes, outer and inner membrane, which main function is the production of most of the phosphate compounds necessary for the energetic balance of the cell. In addition, other functions such as the regulation of the body'sheatgeneration [2][3][4] programmed cell death [5][6][7], reactive oxygen species (ROS) generation and cell signaling [8] is also associated with mitochondria. Cellular vitality is directly related to mitochondria, and mitochondrial dysfunctions are frequent causes of accidental cell death [5,[9][10][11], cancer [12, 13], diabetes [14][15][16] and neurodegenerative diseases [17][18][19], among others.The characterization of the respiratory electron chain could be performed in studies using the fractionation of its components by certain detergents that at low concentrations break the interactions between proteins and lipids in the membranes, leaving associations between proteins intact [20]. In electron transport chain, through this process, four protein complexes were found....

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High‐Throughput, Multiplexed Analysis of 3‐Nitrotyrosine in Individual Proteins

Jin

Zangar

2012

CP Toxicology

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Reactive nitrogen species (RNS) and reactive oxygen species (ROS) are derived as a result of inflammation and oxidative stress and can result in protein modifications. As such, these protein modifications are used as biomarkers for inflammation and oxidative stress. In addition, modifications in single-tissue-associated proteins released into blood can provide insight into the tissue localization of the inflammation or oxidative stress. We have developed an enzyme-linked immunosorbent assay antibody microarray platform to analyze the levels of 3-nitrotyrosine in specific proteins in a variety of biological samples, including human plasma and sputum. Selective-capture antibodies are used to immunoprecipitate individual proteins from samples onto isolated spots on the microarray chips. Then, a monoclonal antibody for 3-nitrotyrosine is used to detect the amount of 3-nitrotyrosine on each spot. Our studies suggest that this approach can be used to detect trace amounts of 3-nitrotyrosine in human plasma and sputum. In this paper, we describe our antibody microarray protocol for detecting 3-nitrotyrosine in specific proteins.

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Nitrotyrosine and Chlorotyrosine: Clinical Significance and Biological Functions in the Vascular System

Cited by 99 publications

References 56 publications

Expression of Reactive Oxygen Species in Reflux Disease

Expression of Reactive Oxygen Species in Reflux Disease

Oxidative Stress: Noxious but Also Vital

High‐Throughput, Multiplexed Analysis of 3‐Nitrotyrosine in Individual Proteins

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