Nitroxidized-Albumin Advanced Glycation End Product and Rheumatoid Arthritis

Tarannum, Akhlas; Arif, Zarina; Alam, Khursheed; Ahmad, Shafeeque; Uddin, Moin

doi:10.5606/archrheumatol.2019.7285

Cited by 12 publications

(10 citation statements)

References 107 publications

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“…The identified 31 Other glycated proteins, Apo-A1 32 and serotransferrin, 33 were reported to have variable abundance under hyperglycemic, oxidative, and inflammatory circumstances, resulting in deficiencies in key processes involved in anti-apoptotic, antioxidant, and iron metabolism. 9,32,33 In this study, DPs including TTR, serotransferrin, and Apo-A1 were identified by both gel-based and non-gelbased techniques. Our findings showed that TTR, serotransferrin, and Apo-A1 has not been previously studied or reported in terms of glycation and their parallel differential expression in RA.…”

Section: Discussionmentioning

confidence: 90%

“… 31 Other glycated proteins, Apo-A1 32 and serotransferrin, 33 were reported to have variable abundance under hyperglycemic, oxidative, and inflammatory circumstances, resulting in deficiencies in key processes involved in anti-apoptotic, antioxidant, and iron metabolism. 9 , 32 , 33 …”

Section: Discussionmentioning

confidence: 99%

“…7 AGE is a non-degradable product that has been demonstrated to have a variety of roles in disease, including a neo-autoantigen in RA. 8 Several glycated proteins such as albumin, 9 fibrinogen, 10 and globulins 11 have been reported to decrease drug-binding ability in plasma, platelet activation, free radical production, impaired fibrinolysis, immune system modulation and inflammation generation. 12 Traditionally, mass spectrometry (MS) has been used to identify glycation and differential protein expression to establish a risk indicator for disease development.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Transthyretin and Receptor for Advanced Glycation End Product’s Differential Levels Associated with the Pathogenesis of Rheumatoid Arthritis

Monu¹,

Agnihotri²,

Saquib³

et al. 2021

JIR

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Transthyretin and Receptor for Advanced Glycation End Product’s Differential Levels Associated with the Pathogenesis of Rheumatoid Arthritis

Monu¹,

Agnihotri²,

Saquib³

et al. 2021

JIR

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“…Increased levels of GA identified in seropositive RA were found to be more sensitive than ESR and CRP [71]. Recently, autoantibodies identified against nitroxidized-AGE-albumin were reported to predict the onset of RA, and understanding their role in pathophysiological impacts on ROS, oxidative stress development is vital [72]. GA also involves in the increment of oxidative stress and promotes the production of superoxide anions in the mitochondria [73].…”

Section: Vascular Complications and Autoimmune Responsementioning

confidence: 99%

AGE/Non-AGE Glycation: An Important Event in Rheumatoid Arthritis Pathophysiology

Monu,

Agnihotri,

Biswas

2021

Inflammation

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Rheumatoid arthritis (RA) is a chronic inflammatory, autoimmune disease that gradually affects the synovial membrane and joints. Many intrinsic and/or extrinsic factors are crucial in making RA pathology challenging throughout the disease. Substantial enzymatic or non-enzymatic modification of proteins driving inflammation has gained a lot of interest in recent years. Endogenously modified glycated protein influences disease development linked with AGEs/non-AGEs and is reported as a disease marker. In this review, we summarized current knowledge of the differential abundance of glycated proteins by compiling and analyzing a variety of AGE and non-AGE ligands that bind with RAGE to activate multi-faceted inflammatory and oxidative stress pathways that are pathobiologically associated with RA-fibroblast-like synoviocytes (RA-FLS). It is critical to comprehend the connection between oxidative stress and inflammation generation, mediated by glycated protein, which may bind to the receptor RAGE, activate downstream pathways, and impart immunogenicity in RA. It is worth noting that AGEs and non-AGEs ligands play a variety of functions, and their functionality is likely to be more reliant on pathogenic states and severity that may serve as biomarkers for RA. Screening and monitoring of these differentially glycated proteins, as well as their stability in circulation, in combination with established pre-clinical characteristics, may aid or predict the onset of RA.KEY WORDS: rheumatoid arthritis (RA); rheumatoid factors (RF); anti-citrullinated peptide antibodies (ACPAs); advanced glycation end-products (AGEs); glyoxal (GO); methylglyoxal (MGO); N-carboxymethyl lysine (CML); reactive oxygen species (ROS); interleukin (IL).

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“…[ 7–9 ] Additionally, AGEs promote a robust inflammatory response by triggering the release of proinflammatory cytokines, including interleukin‐1 (IL‐1), IL‐6, and tumor necrosis factors (TNFs). [ 10–12 ] Furthermore, AGEs induce the expression of a disintegrin‐like and metallopeptidase with thrombospondin type motif‐4 (ADAMTS‐4) and ADAMTS‐5, which is mediated by sex‐determining region Y‐box‐related high‐mobility group‐box‐4 (Sox4). ADAMTS‐4 and ADAMTS‐5 target aggrecan for degradation and play a major role in cartilage destruction in OA.…”

Section: Introductionmentioning

confidence: 99%

Azilsartan prevented AGE‐induced inflammatory response and degradation of aggrecan in human chondrocytes through inhibition of Sox4

Lei

et al. 2021

J Biochem & Molecular Tox

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Advanced glycation end products (AGEs)‐induced inflammation and degradation of aggrecan in human chondrocytes play an important role in the progression and development of osteoarthritis (OA). Azilsartan, an angiotensin II receptor antagonist, has been licensed for the treatment of high blood pressure. However, the effects of Azilsartan in OA and AGEs‐induced damages in chondrocytes have not been previously reported. The injured chondrocytes model was established by incubating with 5 μmol/L AGEs. 3‐(4,5‐Dimethylthiazol‐2‐yl)‐2,5‐diphenyltetrazolium bromide was used to evaluate the cell viability of treated SW1353 cells. The gene expression levels of interleukin‐1α (IL‐1α), tumor necrosis factor‐β (TNF‐β), IL‐6, a disintegrin‐like and metallopeptidase with thrombospondin type motif‐4 (ADAMTS‐4), ADAMTS‐5, Aggrecan, and Sox‐4 were evaluated using quantitative real‐time polymerase chain reaction and their protein levels were determined using enzyme‐linked immunosorbent assay or Western blot analysis. Mitogen‐activated protein kinase p38 pathway was surveyed using phosp‐p38 level and its specific inhibitor SB203580 was employed to block the p38 pathway. The overexpression of Sox4 plasmid was transfected into SW1353 cells to assess its regulation on ADAMTS‐4 and ADAMTS‐5. Azilsartan reduced AGEs‐induced production of proinflammatory cytokines, such as IL‐1α, TNF‐β, and IL‐6. Azilsartan prevented AGEs‐induced expressions of ADAMTS‐4 and ADAMTS‐5 as well as the reduction of aggrecan. Mechanistically, AGEs treatment increased the expression of Sox4 in a dose‐dependent manner. AGE treatment increased the level of phosphorylated p38. However, treatment with the p38 inhibitor SB203580 inhibited AGEs‐induced expression of Sox4, suggesting that AGEs‐induced expression of Sox4 is mediated by p38. Furthermore, Azilsartan suppressed AGEs‐induced phosphorylation of p38 and expression of Sox4. Finally, the overexpression of Sox4 abolished the inhibitory effects of Azilsartan against the expressions of ADAMTS‐4 and ADAMTS‐5. Azilsartan treatment prevented AGEs‐induced inflammatory response and degradation of aggrecan through inhibition of Sox4.

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Nitroxidized-Albumin Advanced Glycation End Product and Rheumatoid Arthritis

Cited by 12 publications

References 107 publications

Transthyretin and Receptor for Advanced Glycation End Product’s Differential Levels Associated with the Pathogenesis of Rheumatoid Arthritis

Transthyretin and Receptor for Advanced Glycation End Product’s Differential Levels Associated with the Pathogenesis of Rheumatoid Arthritis

AGE/Non-AGE Glycation: An Important Event in Rheumatoid Arthritis Pathophysiology

Azilsartan prevented AGE‐induced inflammatory response and degradation of aggrecan in human chondrocytes through inhibition of Sox4

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