Keto-Aldehydes and Cell Division

Szent‐Györgyi, Albert; Együd, Laszlo G.; McLaughlin, Jane A.

doi:10.1126/science.155.3762.539

Cited by 181 publications

(37 citation statements)

References 13 publications

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“…Methylglyoxal is a potent cytotoxic compound and its cytotoxicity is mediated by the inhibition of protein synthesis and interaction with nucleic acids. It has been shown to inhibit the activity of *Address correspondence to this author at the School of Life Sciences, Jawaharlal Nehru University, New Delhi-110067, India; Tel: 91-11-6704523 Fax: 91-11-26742580; E-mail: neerasarin@rediffmail.com various enzymes of glycolytic pathway under in vitro conditions [5][6][7][8]. It has also been shown to arrest growth in G1 phase of the cell cycle through inhibition of DNA synthesis [9,10].…”

Section: Introductionmentioning

confidence: 99%

GOverexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea

Saxena¹

2011

TOPSJ

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Engineering of salinity tolerance in agronomically important crop plants is required to increase their productivity by enabling them to grow in saline soils, which are otherwise left uncultivated. Since an increase in the enzymes of glyoxalase system has been shown to impart salinity tolerance in the model plant tobacco, we used the glyoxalase II gene for engineering salinity tolerance in an important oil yielding crop, Brassica juncea. The transgenic plants of B. juncea overexpressing the glyoxalase II gene showed higher salinity tolerance as compared to the untransformed control plants as observed by delayed senescence in leaf discs at 400 mM and 800 mM NaCl in T1 generation. The percentage of germination of the T2 transgenic seeds was higher at 150 mM and 200 mM NaCl as compared to the seeds of untransformed plants. This for the first time demonstrates the applicability of utilizing the glyoxalase II gene for enhanced salinity tolerance in an oilseed crop plant B. juncea.

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Section: Introductionmentioning

confidence: 99%

GOverexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea

Saxena¹

2011

TOPSJ

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“…MG was therefore once thought to be an intermediate of glycolysis. However, MG was found to inhibit the growth of various types of cells from microorganisms to mammals (14,15,56). MG exerts its toxicity through modification of macromolecules to diminish their biological activities.…”

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confidence: 99%

Activity of the Yap1 Transcription Factor in Saccharomyces cerevisiae Is Modulated by Methylglyoxal, a Metabolite Derived from Glycolysis

Maeta

Izawa

Okazaki

et al. 2004

Molecular and Cellular Biology

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Methylglyoxal (MG) is synthesized during glycolysis, although it inhibits cell growth in all types of organisms. Hence, it has long been asked why such a toxic metabolite is synthesized in vivo. Glyoxalase I is a major enzyme detoxifying MG. Here we show that the Yap1 transcription factor, which is critical for the oxidativestress response in Saccharomyces cerevisiae, is constitutively concentrated in the nucleus and activates the expression of its target genes in a glyoxalase I-deficient mutant. Yap1 contains six cysteine residues in two cysteine-rich domains (CRDs), i.e., three cysteine residues clustering near the N terminus (n-CRD) and the remaining three cysteine residues near the C terminus (c-CRD). We reveal that any of the three cysteine residues in the c-CRD is sufficient for MG to allow Yap1 to translocate into the nucleus and to activate the expression of its target gene. A Yap1 mutant possessing only one cysteine residue in the c-CRD but no cysteine in the n-CRD and deletion of the basic leucine zipper domain can concentrate in the nucleus with MG treatment. However, substitution of all the cysteine residues in Yap1 abolishes the ability of this transcription factor to concentrate in the nucleus following MG treatment. The redox status of Yap1 is substantially unchanged, and protein(s) interaction with Yap1 through disulfide bond is hardly detected in cells treated with MG. Collectively, neither intermolecular nor intramolecular disulfide bond formation seems to be involved in Yap1 activation by MG. Moreover, we show that nucleocytoplasmic localization of Yap1 closely correlates with growth phase and intracellular MG level. We propose a novel regulatory pathway underlying Yap1 activation by a natural metabolite in the cell.

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“…69 Mais tarde essa proposta foi confirmada ao se utilizar 2,4-difenil-hidrazina, conhecido nucleófilo de aldeídos, em extratos de fígado de rato. 70 Os resultados obtidos corroboraram a proposta de Dakin, Dudley e Neuberg de que aldeídos são ativadores do ciclo das glioxalases. Szent-Györgyi, conhecendo os trabalhos de Schubert 71 e Lohmann, 61 em que se constatou que metilglioxal era capaz de reagir com o grupo sulfídrila de cisteína e que o ciclo era dependente de glutationa reduzida (GSH), propôs que o derivado de glioxal encontrado nos trabalhos anteriores era o metilglioxal, 72 o que foi confirmado posteriormente.…”

Section: Esquema 2 Ciclo Das Glioxalases Gsh: Glutationa Reduzida unclassified

Metilglioxal: uma toxina endógena?

Sartori¹,

Bechara²

2010

Quím. Nova

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IS METHYLGLYOXAL AN ENDOGENOUS TOXIN?Methylglyoxal is a very reactive α-oxoaldehyde putatively produced by glycolysis, cytochrome P 450 -catalyzed acetone oxidation and aminoacetone oxidation. Methylglyoxal has been pointed as a substrate for the glyoxalase system ultimately energy-yielding pyruvate, but methylglyoxal is also a toxicant involved in protein aggregation and DNA modification. Controversial hypothesis on methylglyoxal as an anticancer agent, an energy-yielding glycolysis intermediates, and as a regulator of cell division have also been proposed. Methylglyoxal research focuses now on unveiling its biological properties and on the discovery of drugs capable to inhibit its toxic effects, principally in diabetes.

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Keto-Aldehydes and Cell Division

Cited by 181 publications

References 13 publications

GOverexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea

GOverexpression of the Glyoxalase II Gene Leads to Enhanced Salinity Tolerance in Brassica Juncea

Activity of the Yap1 Transcription Factor in Saccharomyces cerevisiae Is Modulated by Methylglyoxal, a Metabolite Derived from Glycolysis

Metilglioxal: uma toxina endógena?

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