Dicarbonyls (Glyoxal, Methylglyoxal, and 3‐Deoxyglucosone)

Rabbani, Naila; Thornalley, Paul J.

doi:10.1002/9781118424032.ch12

Cited by 21 publications

(21 citation statements)

References 61 publications

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“…1). Other usually minor contributions to MG formation are from the oxidation of acetone-increased in diabetic ketoacidosis-catabolism of threonine, and nonenzymatic degradation of glucose and proteins glycated by glucose (11). MG is a highly potent glycating agent with specific reactivity ;20,000-fold higher than that of glucose.…”

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confidence: 99%

The Critical Role of Methylglyoxal and Glyoxalase 1 in Diabetic Nephropathy

2013

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confidence: 99%

The Critical Role of Methylglyoxal and Glyoxalase 1 in Diabetic Nephropathy

2013

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“…We studied renal failure as an example of severe dicarbonyl stress: plasma MG concentration in healthy subjects is ca. 100 nM and increases 5 -7 fold in renal failure [1,63]. The prevalence of increased GLO1 copy number was higher than spontaneous GLO1 duplication in the human population of ca.…”

Section: Discussionmentioning

confidence: 92%

Reappraisal of putative glyoxalase 1-deficient mouse and dicarbonyl stress on embryonic stem cellsin vitro

Shafie

Xue

Barker

et al. 2016

Biochemical Journal

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Glyoxalase 1 (Glo1) is a cytoplasmic enzyme with a cytoprotective function linked to metabolism of the cytotoxic side product of glycolysis, methylglyoxal (MG). It prevents dicarbonyl stress — the abnormal accumulation of reactive dicarbonyl metabolites, increasing protein and DNA damage. Increased Glo1 expression delays ageing and suppresses carcinogenesis, insulin resistance, cardiovascular disease and vascular complications of diabetes and renal failure. Surprisingly, gene trapping by the International Mouse Knockout Consortium (IMKC) to generate putative Glo1 knockout mice produced a mouse line with the phenotype characterised as normal and healthy. Here, we show that gene trapping mutation was successful, but the presence of Glo1 gene duplication, probably in the embryonic stem cells (ESCs) before gene trapping, maintained wild-type levels of Glo1 expression and activity and sustained the healthy phenotype. In further investigation of the consequences of dicarbonyl stress in ESCs, we found that prolonged exposure of mouse ESCs in culture to high concentrations of MG and/or hypoxia led to low-level increase in Glo1 copy number. In clinical translation, we found a high prevalence of low-level GLO1 copy number increase in renal failure where there is severe dicarbonyl stress. In conclusion, the IMKC Glo1 mutant mouse is not deficient in Glo1 expression through duplication of the Glo1 wild-type allele. Dicarbonyl stress and/or hypoxia induces low-level copy number alternation in ESCs. Similar processes may drive rare GLO1 duplication in health and disease.

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“…28 Oxythiamine was a weak inhibitor of thiamine transporters 29 and potentiated the toxicity of methylglyoxal 30 which is also elevated in renal failure and precursor of AGEs. 31 Oxythiamine was taken up and phosphorylated by all tissues of rats except brain; the formation of OTPP was inversely proportional to TPP content. 32 Correspondingly transketolase activity was inhibited in all rat tissues by oxythiamine administration except the brain, 13 likely through formation of OTPP.…”

Section: Discussionmentioning

confidence: 99%

The uremic toxin oxythiamine causes functional thiamine deficiency in end-stage renal disease by inhibiting transketolase activity

Zhang

Masania

Anwar

et al. 2016

Kidney International

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(2016) The uremic toxin oxythiamine causes functional thiamine deficiency in end-stage renal disease by inhibiting transketolase activity. Kidney International, 90 (2). pp. 396-403. Permanent WRAP URL:http://wrap.warwick.ac.uk/78200 Copyright and reuse:The Warwick Research Archive Portal (WRAP) makes this work by researchers of the University of Warwick available open access under the following conditions. Copyright © and all moral rights to the version of the paper presented here belong to the individual author(s) and/or other copyright owners. To the extent reasonable and practicable the material made available in WRAP has been checked for eligibility before being made available.Copies of full items can be used for personal research or study, educational, or not-for-profit purposes without prior permission or charge. Provided that the authors, title and full bibliographic details are credited, a hyperlink and/or URL is given for the original metadata page and the content is not changed in any way. A note on versions:The version presented here may differ from the published version or, version of record, if you wish to cite this item you are advised to consult the publisher's version. Please see the 'permanent WRAP url' above for details on accessing the published version and note that access may require a subscription.For more information, please contact the WRAP Team at: wrap@warwick.ac.uk

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Dicarbonyls (Glyoxal, Methylglyoxal, and 3‐Deoxyglucosone)

Cited by 21 publications

References 61 publications

The Critical Role of Methylglyoxal and Glyoxalase 1 in Diabetic Nephropathy

The Critical Role of Methylglyoxal and Glyoxalase 1 in Diabetic Nephropathy

Reappraisal of putative glyoxalase 1-deficient mouse and dicarbonyl stress on embryonic stem cellsin vitro

The uremic toxin oxythiamine causes functional thiamine deficiency in end-stage renal disease by inhibiting transketolase activity

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