The role of methylglyoxal metabolism in type-2 diabetes and its complications

Κender, Ζoltan; Torzsa, Péter; Grolmusz, K Vince; Patócs, Attila; Lichthammer, Adrienn; Bálint, Márta Veresné; Rácz, Kàroly; Reismann, Péter

doi:10.1556/oh.2012.29348

Cited by 4 publications

(1 citation statement)

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“…MGO is a major precursor of AGEs, especially CEL, which is capable of binding and modifying a number of proteins (glycoxidation reaction), including bovine serum albumin (BSA), RNase A, collagen, lysozyme and lens crystallins. 2,3 Protein glycation is known to be involved in the pathogenesis of several age-related disorders like diabetes, atherosclerosis, and end-stage renal and neurodegenerative diseases. 4 Inhibitors of AGE formation might follow several mechanisms, such as aldose reductase, antioxidant activity, reactive dicarbonyl trapping, sugar autoxidation inhibition and amino group binding.…”

Section: Introductionmentioning

confidence: 99%

New knowledge on the antiglycoxidative mechanism of chlorogenic acid

et al. 2015

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The role of chlorogenic acid (CGA) in the formation of advanced glycation end-products (AGEs) (glycoxidation reaction) was studied. Model systems composed of bovine serum albumin (BSA) (1 mg mL(-1)) and methylglyoxal (5 mM) under mimicked physiological conditions (pH 7.4, 37 °C) were used to evaluate the antiglycoxidative effect of CGA (10 mM). The stability of CGA under reaction conditions was assayed by HPLC and MALDI-TOF MS. The glycoxidation reaction was estimated by analysis of free amino groups by the OPA assay, spectral analysis of fluorescent AGEs and total AGEs by ELISA, and colour formation by absorbance at 420 nm. Structural changes in protein were evaluated by analysis of phenol bound to the protein backbone using the Folin reaction, UV-Vis spectral analysis and MALDI-TOF-MS, while changes in protein function were measured by determining the antioxidant capacity using the ABTS radical cation decolourisation assay. CGA was isomerised and oxidised under our experimental conditions. Evidence of binding between BSA and multiple CGA and/or its derivative molecules (isomers and oxidation products) was found. CGA inhibited (p < 0.05) the formation of fluorescent and total AGEs at 72 h of reaction by 91.2 and 69.7%, respectively. The binding of phenols to BSA significantly increased (p < 0.001) its antioxidant capacity. Correlations between free amino group content, phenol bound to protein and antioxidant capacity were found. Results indicate that CGA simultaneously inhibits the formation of potentially harmful compounds (AGEs) and promotes the generation of neoantioxidant structures.

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Section: Introductionmentioning

confidence: 99%

New knowledge on the antiglycoxidative mechanism of chlorogenic acid

et al. 2015

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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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