Quantification of reactive carbonyl compounds in icodextrin-based peritoneal dialysis fluids by combined UHPLC-DAD and -MS/MS detection

Gensberger‐Reigl, Sabrina; Huppert, Jochen; Pischetsrieder, Monika

doi:10.1016/j.jpba.2015.10.022

Cited by 12 publications

(16 citation statements)

References 38 publications

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“…Liquid chromatography coupled tandem mass spectrometry (LC–MS/MS) employing internal, preferably isotopically labeled, standards is the method of choice for the quantification of dicarbonyls and several methods have been reported [59,74,89,90]. Alternatively, the use of GC–MS and high-performance liquid chromatography (HPLC) methods has been reported for the detection of MG [91,92].…”

Section: Quantification Of Dicarbonyls and Advanced Glycation End-mentioning

confidence: 99%

Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention

Brings

Fleming

Freichel

et al. 2017

IJMS

167

106

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Advanced glycation end-products (AGEs) are non-enzymatic protein and amino acid adducts as well as DNA adducts which form from dicarbonyls and glucose. AGE formation is enhanced in diabetes and is associated with the development of diabetic complications. In the current review, we discuss mechanisms that lead to enhanced AGE levels in the context of diabetes and diabetic complications. The methylglyoxal-detoxifying glyoxalase system as well as alternative pathways of AGE detoxification are summarized. Therapeutic approaches to interfere with different pathways of AGE formation are presented.

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Section: Quantification Of Dicarbonyls and Advanced Glycation End-mentioning

confidence: 99%

Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention

Brings

Fleming

Freichel

et al. 2017

IJMS

167

106

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show abstract

“…To understand the mechanisms of AGE formation in such in vitro glycation model systems, and to dissect individual pathways of advanced glycation, analysis of peptide products can be complemented by quantification of carbohydrate [ 47 ] and α-dicarbonyl [ 276 ] intermediates. In such cases, analysis of carbohydrates relies on sequential derivatization with methoxyamine hydrochloride (MOA) and N -methyl- N -(trimethylsilyl) trifluoroacetamide (MSTFA), followed with GC-EI-MS relying on well-standardized methods [ 47 ], whereas the α-dicarbonyl patterns are typically addressed by liquid chromatography with ultraviolet detection (LC-UV), LS-MS or LC-MS/MS after derivatization of the α-dicarbonyl moieties with o -phenylenediamine (oPDA) [ 49 , 277 ].…”

Section: Part 2 New Prospectives In Maillard Proteomicsmentioning

confidence: 99%

Maillard Proteomics: Opening New Pages

Soboleva

Schmidt

Vikhnina

et al. 2017

IJMS

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Protein glycation is a ubiquitous non-enzymatic post-translational modification, formed by reaction of protein amino and guanidino groups with carbonyl compounds, presumably reducing sugars and α-dicarbonyls. Resulting advanced glycation end products (AGEs) represent a highly heterogeneous group of compounds, deleterious in mammals due to their pro-inflammatory effect, and impact in pathogenesis of diabetes mellitus, Alzheimer’s disease and ageing. The body of information on the mechanisms and pathways of AGE formation, acquired during the last decades, clearly indicates a certain site-specificity of glycation. It makes characterization of individual glycation sites a critical pre-requisite for understanding in vivo mechanisms of AGE formation and developing adequate nutritional and therapeutic approaches to reduce it in humans. In this context, proteomics is the methodology of choice to address site-specific molecular changes related to protein glycation. Therefore, here we summarize the methods of Maillard proteomics, specifically focusing on the techniques providing comprehensive structural and quantitative characterization of glycated proteome. Further, we address the novel break-through areas, recently established in the field of Maillard research, i.e., in vitro models based on synthetic peptides, site-based diagnostics of metabolism-related diseases (e.g., diabetes mellitus), proteomics of anti-glycative defense, and dynamics of plant glycated proteome during ageing and response to environmental stress.

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“…Such variations in sample processing can lead to an overestimation of MGO con-centration(455). The current state-of-the art technique for the measurement of MGO is ultra-performance liquid chromatography tandem mass spectrometry (UPLC-MS/MS)(189,233,455,506). By using UPLC-MS/MS and controlling sample processing to avoid artificial formation of MGO, typical plasma levels of MGO in healthy individuals have been estimated at~60 -250 nM(233,455,506) and cellular MGO levels have been estimated at~1-5 M MGO(149,436).…”

mentioning

confidence: 99%

Methylglyoxal, a Highly Reactive Dicarbonyl Compound, in Diabetes, Its Vascular Complications, and Other Age-Related Diseases

Schalkwijk

Stehouwer

2020

Physiological Reviews

365

330

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The formation and accumulation of methylglyoxal (MGO), a highly reactive dicarbonyl compound, has been implicated in the pathogenesis of type 2 diabetes, vascular complications of diabetes, and several other age-related chronic inflammatory diseases such as cardiovascular disease, cancer and disorders of the central nervous system. MGO is mainly formed as a byproduct of glycolysis and, under physiological circumstances, detoxified by the glyoxalase system. MGO is the major precursor of non-enzymatic glycation of proteins and DNA, subsequently leading to the formation of advanced glycation endproducts (AGEs). MGO and MGO-derived AGEs can impact on organs and tissues affecting their functions and structure. This review summarizes the mechanisms through which MGO is formed, its detoxification by the glyoxalase system, and its effect on biochemical pathways in relation to the development of diabetes, vascular complications of diabetes and other age-related diseases. Although therapies to treat MGO-associated complications are not yet available for application in clinical practice, several strategies to lower MGO have been developed over the years. We will summarize several new directions to target MGO stress including glyoxalase inducers and MGO scavengers. Diminishing MGO burden can potentially form the basis for new treatment strategies for age-related disorders in which MGO plays a pivotal role.

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Quantification of reactive carbonyl compounds in icodextrin-based peritoneal dialysis fluids by combined UHPLC-DAD and -MS/MS detection

Cited by 12 publications

References 38 publications

Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention

Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention

Maillard Proteomics: Opening New Pages

Methylglyoxal, a Highly Reactive Dicarbonyl Compound, in Diabetes, Its Vascular Complications, and Other Age-Related Diseases

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