Studies of advanced glycation end products and oxidation biomarkers for type 2 diabetes

Chiu, Chung‐Jung; Rabbani, Naila; Rowan, Sheldon; Chang, Min-Lee; Sawyer, Sherilyn; Hu, Frank B.; Willett, Walter C.; Thornalley, Paul J.; Anwar, Attia; Bar, Liliana; Kang, Jae H.; Taylor, Allen

doi:10.1002/biof.1423

Cited by 27 publications

(27 citation statements)

References 40 publications

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“…Glucosepane is the major quantitative crosslink formed in protein glycation, formed from FL residues [42]. It is a marker of glycemic control [43] and the major glycation adduct released from joint proteins during early-stage development of osteoarthritis [41]. Pentosidine is pentose sugar-derived AGE and intense fluorophore.…”

Section: Protein Ageomics and Other Modifications As Reporters Of Metmentioning

confidence: 99%

Reading patterns of proteome damage by glycation, oxidation and nitration: quantitation by stable isotopic dilution analysis LC-MS/MS

Rabbani

Thornalley

2020

Essays in Biochemistry

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Liquid chromatography-tandem mass spectrometry (LC-MS/MS) provides a high sensitivity, high specificity multiplexed method for concurrent detection of adducts formed by protein glycation, oxidation and nitration, also called AGEomics. Combined with stable isotopic dilution analysis, it provides for robust quantitation of protein glycation, oxidation and nitration adduct analytes. It is the reference method for such measurements. LC-MS/MS has been used to measure glycated, oxidized and nitrated amino acids – also called glycation, oxidation and nitration free adducts, with a concurrent quantitation of the amino acid metabolome in physiological fluids. Similar adduct residues in proteins may be quantitated with prior exhaustive enzymatic hydrolysis. It has also been applied to quantitation of other post-translation modifications, such as citrullination and formation of Nε-(γ-glutamyl)lysine crosslink by transglutaminases. Application to cellular and extracellular proteins gives estimates of the steady-state levels of protein modification by glycation, oxidation and nitration, and measurement of the accumulation of glycation, oxidation and nitration adducts in cell culture medium and urinary excretion gives an indication of flux of adduct formation. Measurement of glycation, oxidation and nitration free adducts in plasma and urine provides for estimates of renal clearance of free adducts. Diagnostic potential in clinical studies has been enhanced by the combination of estimates of multiple adducts in optimized diagnostic algorithms by machine learning. Recent applications have been in early-stage detection of metabolic, vascular and renal disease, and arthritis, metabolic control and risk of developing vascular complication in diabetes, and a blood test for autism.

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Section: Protein Ageomics and Other Modifications As Reporters Of Metmentioning

confidence: 99%

Reading patterns of proteome damage by glycation, oxidation and nitration: quantitation by stable isotopic dilution analysis LC-MS/MS

Rabbani

Thornalley

2020

Essays in Biochemistry

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“…We also identified the cross-linking AGE glucosepane as a potential plasma biomarker of AMD [148]. Plasma glucosepane may also be a biomarker of diabetes [149]. The accumulation of AGEs with a high glycemic index diet was not irreversible.…”

Section: New Directions and Approachesmentioning

confidence: 99%

Mechanistic targeting of advanced glycation end-products in age-related diseases

Rowan

Bejarano

Taylor

2018

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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164

125

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Glycative stress, caused by the accumulation of cytotoxic and irreversibly-formed sugar-derived advanced glycation end-products (AGEs), contributes to morbidity associated with aging, age-related diseases, and metabolic diseases. In this review, we summarize pathways leading to formation of AGEs, largely from sugars and glycolytic intermediates, and discuss detoxification of AGE precursors, including the glyoxalase system and DJ-1/Park7 deglycase. Disease pathogenesis downstream of AGE accumulation can be cell autonomous due to aggregation of glycated proteins and impaired protein function, which occurs in ocular cataracts. Extracellular AGEs also activate RAGE signaling, leading to oxidative stress, inflammation, and leukostasis in diabetic complications such as diabetic retinopathy. Pharmaceutical agents have been tested in animal models and clinically to diminish glycative burden. We summarize existing strategies and point out several new directions to diminish glycative stress including: plant-derived polyphenols as AGE inhibitors and glyoxalase inducers; improved dietary patterns, particularly Mediterranean and low glycemic diets; and enhancing proteolytic capacities of the ubiquitin-proteasome and autophagy pathways that are involved in cellular clearing of AGEs.

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“…Improved glycemic markers may emerge from a combination of biomarker responses assessed, particularly by machine learning techniques with data-driven selection of optimum biomarker combinations, and further validation of candidate markers in blood samples collected and stored under conventional routine clinical conditions for ease of clinical translation (e.g., use of machine learning in plasma metabolomics studies to identify metabolite combinations that predict progression to diabetes [ 115 ] and application of an LC-MS/MS assay of AGEs in stored repository blood samples [ 116 ]).…”

Section: Discussionmentioning

confidence: 99%

Potential Markers of Dietary Glycemic Exposures for Sustained Dietary Interventions in Populations without Diabetes

Feskens

Brennan

Dussort

et al. 2020

Advances in Nutrition

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There is considerable interest in dietary and other approaches to maintaining blood glucose concentrations within the normal range and minimizing exposure to postprandial hyperglycemic excursions. The accepted marker to evaluate the sustained maintenance of normal blood glucose concentrations is glycated hemoglobin A1c (HbA1c). However, although this is used in clinical practice to monitor glycemic control in patients with diabetes, it has a number of drawbacks as a marker of efficacy of dietary interventions that might beneficially affect glycemic control in people without diabetes. Other markers that reflect shorter-term glycemic exposures have been studied and proposed, but consensus on the use and relevance of these markers is lacking. We have carried out a systematic search for studies that have tested the responsiveness of 6 possible alternatives to HbA1c as markers of sustained variation in glycemic exposures and thus their potential applicability for use in dietary intervention trials in subjects without diabetes: 1,5-anhydroglucitol (1,5-AG), dicarbonyl stress, fructosamine, glycated albumin (GA), advanced glycated end products (AGEs), and metabolomic profiles. The results suggest that GA may be the most promising for this purpose, but values may be confounded by effects of fat mass. 1,5-AG and fructosamine are probably not sensitive enough to the range of variation in glycemic exposures observed in healthy individuals. Use of measures based on dicarbonyls, AGEs, or metabolomic profiles would require further research into possible specific molecular species of interest. At present, none of the markers considered here is sufficiently validated and sensitive for routine use in substantiating the effects of sustained variation in dietary glycemic exposures in people without diabetes.

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Studies of advanced glycation end products and oxidation biomarkers for type 2 diabetes

Cited by 27 publications

References 40 publications

Reading patterns of proteome damage by glycation, oxidation and nitration: quantitation by stable isotopic dilution analysis LC-MS/MS

Reading patterns of proteome damage by glycation, oxidation and nitration: quantitation by stable isotopic dilution analysis LC-MS/MS

Mechanistic targeting of advanced glycation end-products in age-related diseases

Potential Markers of Dietary Glycemic Exposures for Sustained Dietary Interventions in Populations without Diabetes

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