Impact of Anti-Peroxynitrite-Damaged-Thymidine- Monophosphate Antibodies on Disease Activity in Patients with Systemic Lupus Erythematosus

Alghasham, Abdullah; Salloom, Abdulaziz A M Al; Alghamadi, Ahmed S S; Rasheed, Zafar

doi:10.1080/15257770.2014.958235

Cited by 5 publications

(3 citation statements)

References 39 publications

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“…Direct binding enzyme-linked immunosorbent assay (ELISA) was performed on flat bottom 96-well Nunc-ImmunoTM MicroWell polystyrene immunoplates (catalog # P8616, Sigma-Aldrich, St. Louis, MO., USA). 29 - 33 …”

Section: Methodsmentioning

confidence: 99%

Recognition of oxidized albumin and thyroid antigens by psoriasis autoantibodies

Al‐Shobaili

Ahmed

Rasheed

2015

SMJ

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Objectives:To investigate the role of reactive-oxygen-species (ROS) induced epitopes on human-serum-albumin (HSA) and thyroid antigens in psoriasis autoimmunity.Methods:This study was performed in the College of Medicine, Qassim University, Buraidah, Saudi Arabia between May 2014 and February 2015. The study was designed to explore the role of ROS-induced epitopes in psoriasis autoimmunity. Singlet-oxygen (or ROS)-induced epitopes on protein (ROS-epitopes-albumin) was characterized by in-vitro and in-vivo. Thyroid antigens were prepared from rabbit thyroid, and thyroglobulin was isolated from thyroid extract. Immunocross-reactions of protein-A purified anti-ROS-epitopes-HSA-immunoglobulin G (IgGs) with thyroid antigen, thyroglobulin, and their oxidized forms were determined. Binding characteristics of autoantibodies in chronic plaque psoriasis patients (n=26) against ROS-epitopes-HSA and also with native and oxidized thyroid antigens were screened, and the results were compared with age-matched controls (n=22).Results:The anti-ROS-epitopes-HSA-IgGs showed cross-reactions with thyroid antigen, thyroglobulin and with their oxidized forms. High degree of specific binding by psoriasis IgGs to ROS-epitopes-HSA, ROS-thyroid antigen and ROS-thyroglobulin was observed. Immunoglobulin G from normal-human-controls showed negligible binding with all tested antigens. Moreover, sera from psoriasis patients had higher levels of carbonyl contents compared with control sera.Conclusion:Structural alterations in albumin, thyroid antigens by ROS, generate unique neo-epitopes that might be one of the factors for the induction of autoantibodies in psoriasis.

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Section: Methodsmentioning

confidence: 99%

Recognition of oxidized albumin and thyroid antigens by psoriasis autoantibodies

Al‐Shobaili

Ahmed

Rasheed

2015

SMJ

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“…In addition, NO interacts with ROS to generate peroxynitrite (ONOO-). This ROS further decreases the bioavailability of NO, and impairs endothelium-dependent relaxation and enhances vasoconstriction and proinflammation [74, 90, 91].…”

Section: Molecular Phenotypes In the Aging Arterial Wallmentioning

confidence: 99%

Proinflammatory Arterial Stiffness Syndrome: A Signature of Large Arterial Aging

Wang

Monticone

McGraw³

2018

J Vasc Res

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Age-associated structural and functional remodeling of the arterial wall produces a productive environment for the initiation and progression of hypertension and atherosclerosis. Chronic aging stress induces low-grade proinflammatory signaling and causes cellular proinflammation in arterial walls, which triggers the structural phenotypic shifts characterized by endothelial dysfunction, diffuse intimal-medial thickening, and arterial stiffening. Microscopically, aged arteries exhibit an increase in arterial cell senescence, proliferation, invasion, matrix deposition, elastin fragmentation, calcification, and amyloidosis. These characteristic cellular and matrix alterations not only develop with aging but can also be induced in young animals under experimental proinflammatory stimulation. Interestingly, these changes can also be attenuated in old animals by reducing low-grade inflammatory signaling. Thus, mitigating age-associated proinflammation and arterial phenotype shifts is a potential approach to retard arterial aging and prevent the epidemic of hypertension and atherosclerosis in the elderly.

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“…Peroxynitrite is produced in humans in response to various internal and external stressors, including toxins, UV light, and stressors, in different pathological scenarios [11]. It is widely accepted that the harmful effects of nitric oxide primarily arise from peroxynitrite, which has high reactivity and reacts readily with different biomolecules like proteins, lipids, and nucleic acids [12][13][14]. Apart from causing oxidative harm to biomolecules, peroxynitrite also triggers several cell-signaling pathways leading to oxidative injury and cell death through necrosis or apoptosis [15,16].…”

Section: Introductionmentioning

confidence: 99%

Apigenin Provides Structural Protection to Human Fibrinogen against Nitrosative Stress: Biochemical and Molecular Insights

Farhana,

Alsrhani,

Khan

et al. 2024

Biomolecules

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Background: Peroxynitrite (ONOO−) is an oxidant linked with several human pathologies. Apigenin, a natural flavonoid known for its health benefits, remains unexplored in relation to ONOO− effects. This study investigated the potential of apigenin to structurally protect fibrinogen, an essential blood clotting factor, from ONOO−-induced damage. Methods: Multi-approach analyses were carried out where fibrinogen was exposed to ONOO− generation while testing the efficacy of apigenin. The role of apigenin against ONOO−-induced modifications in fibrinogen was investigated using UV spectroscopy, tryptophan or tyrosine fluorescence, protein hydrophobicity, carbonylation, and electrophoretic analyses. Results: The findings demonstrate that apigenin significantly inhibits ONOO−-induced oxidative damage in fibrinogen. ONOO− caused reduced UV absorption, which was reversed by apigenin treatment. Moreover, ONOO− diminished tryptophan and tyrosine fluorescence, which was effectively restored by apigenin treatment. Apigenin also reduced the hydrophobicity of ONOO−-damaged fibrinogen. Moreover, apigenin exhibited protective effects against ONOO−-induced protein carbonylation. SDS-PAGE analyses revealed that ONOO−treatment eliminated bands corresponding to fibrinogen polypeptide chains Aα and γ, while apigenin preserved these changes. Conclusions: This study highlights, for the first time, the role of apigenin in structural protection of human fibrinogen against peroxynitrite-induced nitrosative damage. Our data indicate that apigenin offers structural protection to all three polypeptide chains (Aα, Bβ, and γ) of human fibrinogen. Specifically, apigenin prevents the dislocation or breakdown of the amino acids tryptophan, tyrosine, lysine, arginine, proline, and threonine and also prevents the exposure of hydrophobic sites in fibrinogen induced by ONOO−.

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Impact of Anti-Peroxynitrite-Damaged-Thymidine- Monophosphate Antibodies on Disease Activity in Patients with Systemic Lupus Erythematosus

Cited by 5 publications

References 39 publications

Recognition of oxidized albumin and thyroid antigens by psoriasis autoantibodies

Recognition of oxidized albumin and thyroid antigens by psoriasis autoantibodies

Proinflammatory Arterial Stiffness Syndrome: A Signature of Large Arterial Aging

Apigenin Provides Structural Protection to Human Fibrinogen against Nitrosative Stress: Biochemical and Molecular Insights

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