A New Role of Phosphoglucose Isomerase. Involvement of the Glycolytic Enzyme in Aldehyde Metabolism

Dmitriev, L F; Dugin, S. F.

doi:10.1007/s10541-005-0255-4

Cited by 13 publications

(8 citation statements)

References 14 publications

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“…The key product of lipid peroxidation is malondialdehyde. A study reported that malondialdehyde might relate to the formation of MG (Agadjanyan, Dmitriev, & Dugin, ). Taken together, the increase in renal MG might be attributed to lipid peroxidation, and subsequently evoke oxidative stress in Pb‐induced renal injury.…”

Section: Discussionmentioning

confidence: 99%

Accumulation of methylglyoxal and d‐lactate in Pb‐induced nephrotoxicity in rats

Huang

Tsai

et al. 2016

Biomedical Chromatography

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Lead (Pb) is an environmental pollutant associated with several diseases, such as nephrotoxicity. Methylglyoxal (MG) is a reactive dicarbonyl compound formed during glycolysis and reported to increase in kidney damage. Metformin is used as an MG scavenger in the clinic. In this study, we investigated the mechanism of Pb-induced renal injury and the effect of metformin on Pb-induced nephrotoxicity. Eighteen Wistar rats were randomly divided into three groups: control, Pb, and Pb + metformin groups. Pb (250 ppm) was administered in drinking water, and 50 mg/kg of metformin was co-administered orally. After 28 days, the levels of MG and its metabolite d-lactate in urine, serum and renal tissues were examined. The elevation of renal MG (56.86 ± 17.47 vs 36.40 ± 5.69, p < 0.01) and urinary d-lactate (0.68 ± 0.28 vs 0.32 ± 0.13, p < 0.01) was observed in Pb-exposed rats compared with those in control rats. After co-treatment with metformin, these phenomena were attenuated. In the present study, it was demonstrated for the first time that urinary d-lactate might serve as the candidate marker for Pb-induced nephrotoxicity in the clinic, and metformin might be a new therapeutic candidate for Pb poisoning.

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Section: Discussionmentioning

confidence: 99%

Accumulation of methylglyoxal and d‐lactate in Pb‐induced nephrotoxicity in rats

Huang

Tsai

et al. 2016

Biomedical Chromatography

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“…Early studies showed that a probable biochemical route for MDA metabolism involves its oxidation by mitochondrial aldehyde dehydrogenase followed by decarboxylation to produce acetaldehyde, which is oxidized by aldehyde dehydrogenase to acetate and further to CO 2 and H 2 O (Figure 3) [49, 101, 102]. On the other hand, phosphoglucose isomerase is probably responsible for metabolizing cytoplasmic MDA to methylglyoxal (MG) and further to D-lactate by enzymes of the glyoxalase system by using GSH as a cofactor [103]. A portion of MDA is excreted in the urine as various enaminals (RNH-CH–CH-CHO) such as N-epsilon-(2-propenal)lysine, or N-2-(propenal) serine [49].…”

Section: Lipids Damage By Reactive Oxygen Speciesmentioning

confidence: 99%

Lipid Peroxidation: Production, Metabolism, and Signaling Mechanisms of Malondialdehyde and 4-Hydroxy-2-Nonenal

Ayala

Muñoz

Argüelles

2014

Oxidative Medicine and Cellular Longevity

4,498

3,003

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Lipid peroxidation can be described generally as a process under which oxidants such as free radicals attack lipids containing carbon-carbon double bond(s), especially polyunsaturated fatty acids (PUFAs). Over the last four decades, an extensive body of literature regarding lipid peroxidation has shown its important role in cell biology and human health. Since the early 1970s, the total published research articles on the topic of lipid peroxidation was 98 (1970–1974) and has been increasing at almost 135-fold, by up to 13165 in last 4 years (2010–2013). New discoveries about the involvement in cellular physiology and pathology, as well as the control of lipid peroxidation, continue to emerge every day. Given the enormity of this field, this review focuses on biochemical concepts of lipid peroxidation, production, metabolism, and signaling mechanisms of two main omega-6 fatty acids lipid peroxidation products: malondialdehyde (MDA) and, in particular, 4-hydroxy-2-nonenal (4-HNE), summarizing not only its physiological and protective function as signaling molecule stimulating gene expression and cell survival, but also its cytotoxic role inhibiting gene expression and promoting cell death. Finally, overviews of in vivo mammalian model systems used to study the lipid peroxidation process, and common pathological processes linked to MDA and 4-HNE are shown.

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“…1 Methylglyoxal is a physiological substrate, derived from glycolysis, via degradation of triose phosphate intermediates, lipid peroxidation, threonine degradation, fragmentation of glycated proteins 2 and enzymatic isomerization from malondialdehyde (MDA). 3 As a highly reactive metabolite, MG has a strong ability to cross-link with protein amino groups to form stable products called advanced glycation end products (AGEs) and to attack guanine residues of DNA leading to DNA glycation. 4 The cytotoxicity of MG is due to its mutagenic and antiproliferative properties and to its ability to trigger apoptosis, 5,6 apparently via oxidative signalling.…”

Section: Introductionmentioning

confidence: 99%

Alteration of glyoxalases gene expression in response to testosterone in LNCaP and PC3 human prostate cancer cells

Antognelli

Buono²,

Baldracchini³

et al. 2007

Cancer Biology & Therapy

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Glyoxalase system, a ubiquitous detoxification pathway protecting against cellular damage caused by potent cytotoxic metabolites, is involved in the regulation of cellular growth. Aberrations in the expression of glyoxalase genes in several human cancers have been reported. Recently, we described a possible regulatory effect by estrogens on glyoxalase genes in human breast cancer cell lines. This result, along with those ones regarding changes in glyoxalases activity and expression in other human hormoneregulated cancers, such as prostate cancer, has prompted us to investigate whether also androgens, whose functional role in prostate cancer pathogenesis is well known, could modulate glyoxalases gene expression. Therefore, we treated LNCaP androgen-responsive and PC3 androgen-independent human prostate cancer cell lines with testosterone at the concentrations of 1 nM and 100 nM. After a two days treatment, glyoxalases mRNA levels as well as cell proliferation were evaluated by real-time RT-PCR analysis and [ 3 H]thymidine incorporation, respectively. Results pointed out that testosterone affects the expression of glyoxalase system genes and cell proliferation in a different manner in the two cell lines. The possibility that modulation of glyoxalase genes expression by testosterone is due to glyoxalases-mediated intracellular response mechanisms to the androgen-induced oxidative stress or to the presence of androgen response elements (ARE) in glyoxalase promoters are discussed. Knowledge regarding the regulation of glyoxalases by testosterone may provide insights into the importance of these enzymes in human prostate carcinomas in vivo.

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A New Role of Phosphoglucose Isomerase. Involvement of the Glycolytic Enzyme in Aldehyde Metabolism

Cited by 13 publications

References 14 publications

Accumulation of methylglyoxal and d‐lactate in Pb‐induced nephrotoxicity in rats

Accumulation of methylglyoxal and d‐lactate in Pb‐induced nephrotoxicity in rats

Lipid Peroxidation: Production, Metabolism, and Signaling Mechanisms of Malondialdehyde and 4-Hydroxy-2-Nonenal

Alteration of glyoxalases gene expression in response to testosterone in LNCaP and PC3 human prostate cancer cells

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