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[PMID]:29351321
[Au] Autor:Khan MA; Arif Z; Khan MA; Moinuddin; Alam K
[Ad] Endereço:Department of Biochemistry, J.N. Medical College, Faculty of Medicine, Aligarh Muslim University, Aligarh, Uttar Pradesh, India.
[Ti] Título:Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level.
[So] Source:PLoS One;13(1):e0191014, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hyperglycaemia triggers increased production of methylglyoxal which can cause gross modification in proteins' structure vis-a-vis function though advanced glycation end products (AGEs). The AGEs may initiate vascular and nonvascular pathologies. In this study, we have examined the biochemical and biophysical changes in human IgG under normal and high glucose after introducing methylglyoxal into the assay mixture. This non-enzymatic reaction mainly engaged lysine residues as indicated by TNBS results. The UV results showed hyperchromicity in modified-IgG samples while fluorescence data supported AGEs formation during the course of reaction. Shift in amide I and amide II band position indicated perturbations in secondary structure. Increase carbonyl content and decrease in sulfhydryl suggests that the modification is accompanied by oxidative stress. All modified-IgG samples showed more thermostability than native IgG; the highest Tm was shown by IgG-high glucose-MGO variant. Results of ANS, Congo red and Thioflavin T dyes clearly suggest increase in hydrophobic patches and aggregation, respectively. SEM and TEM images support aggregates generation in modified-IgG samples.
[Mh] Termos MeSH primário: Glucose/química
Imunoglobulina G/química
Aldeído Pirúvico/farmacologia
[Mh] Termos MeSH secundário: Fenômenos Biofísicos
Seres Humanos
Microscopia Eletrônica de Varredura
Microscopia Eletrônica de Transmissão
Estresse Oxidativo
Desnaturação Proteica
Espectrometria de Fluorescência
Espectrofotometria Ultravioleta
Espectroscopia de Infravermelho com Transformada de Fourier
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin G); 722KLD7415 (Pyruvaldehyde); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191014


  2 / 1661 MEDLINE  
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[PMID]:29017767
[Au] Autor:Kwak MK; Ku M; Kang SO
[Ad] Endereço:Laboratory of Biophysics, School of Biological Sciences, Institute of Microbiology, Seoul National University, Seoul 151-742, Republic of Korea. Electronic address: genie6@snu.ac.kr.
[Ti] Título:Inducible NAD(H)-linked methylglyoxal oxidoreductase regulates cellular methylglyoxal and pyruvate through enhanced activities of alcohol dehydrogenase and methylglyoxal-oxidizing enzymes in glutathione-depleted Candida albicans.
[So] Source:Biochim Biophys Acta;1862(1):18-39, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: High methylglyoxal content disrupts cell physiology, but mammals have scavengers to prevent glycolytic and mitochondrial dysfunctions. In yeast, methylglyoxal accumulation triggers methylglyoxal-oxidizing alcohol dehydrogenase (Adh1) activity. While methylglyoxal reductases and glyoxalases have been well studied in prokaryotes and eukaryotes, experimental evidence for methylglyoxal dehydrogenase (Mgd) and other catalytic activities of this enzyme affecting glycolysis and the tricarboxylic acid cycle is lacking. METHODS: A glycine-rich cytoplasmic Mgd protein, designated as Mgd1/Grp2, was isolated from glutathione-depleted Candida albicans. The effects of Mgd1/Grp2 activities on metabolic pathophysiology were investigated using knockout and overexpression mutants. We measured glutathione-(in)dependent metabolite contents and metabolic effects, including viability, oxygen consumption, ADH1 transcripts, and glutathione reductase and α-ketoglutarate dehydrogenase activities in the mutants. Based on the findings, methylglyoxal-oxidizing proteins were monitored to determine effects of MGD1/GRP2 disruption on methylglyoxal-scavenging traits during glutathione deprivation. RESULTS: Methylglyoxal-oxidizing NAD(H)-linked Mgd1/Grp2 was found solely in glutathione auxotrophs, and it catalyzed the reduction of both methylglyoxal and pyruvate. MGD1/GRP2 disruptants showed growth defects, cell-cycle arrest, and methylglyoxal and pyruvate accumulation with mitochondrial impairment, regardless of ADH1 compensation. Other methylglyoxal-oxidizing enzymes were identified as key glycolytic enzymes with enhanced activity and transcription in MGD1/GRP2 disruptants, irrespective of glutathione content. CONCLUSIONS: Failure of methylglyoxal and pyruvate dissimilation by Mgd1/Grp2 deficiency leads to poor glutathione-dependent redox regulation despite compensation by Adh1. GENERAL SIGNIFICANCE: This is the first report that multifunctional Mgd activities contribute to scavenging methylglyoxal and pyruvate to maintain metabolic homeostasis and the redox pool via glycolytic enzymes and Adh1 expression.
[Mh] Termos MeSH primário: Álcool Desidrogenase/metabolismo
Oxirredutases do Álcool/metabolismo
Candida albicans/metabolismo
Proteínas Fúngicas/metabolismo
Glutationa/metabolismo
Aldeído Pirúvico/metabolismo
Ácido Pirúvico/metabolismo
[Mh] Termos MeSH secundário: Álcool Desidrogenase/genética
Oxirredutases do Álcool/genética
Candida albicans/genética
Proteínas Fúngicas/genética
Glutationa/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fungal Proteins); 722KLD7415 (Pyruvaldehyde); 8558G7RUTR (Pyruvic Acid); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 1.1.3.- (glyoxal oxidase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171012
[St] Status:MEDLINE


  3 / 1661 MEDLINE  
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[PMID]:29227084
[Au] Autor:Gudkova OO; Latyshko NV; Shandrenko SG
[Ti] Título:Amine oxidases as important agents of pathological processes of rhabdomyolysis in rats.
[So] Source:Ukr Biochem J;88(1):79-87, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:In this study we have tested an idea on the important role of amine oxidases (semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase) as an additional source of oxidative/carbonyl stress under glycerol-induced rhabdomyolysis, since the enhanced formation of reactive oxygen species and reactive carbonyl species in a variety of tissues is linked to various diseases. In our experiments we used the sensitive fluorescent method devised for estimation of amine oxidases activity in the rat kidney and thymus as targeted organs under rhabdomyolysis. We have found in vivo the multiple rises in activity of semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase (2-4.5 times) in the corresponding cell fractions, whole cells or their lysates at the 3-6th day after glycerol injection. Aberrant antioxidant activities depended on rhabdomyolysis stage and had organ specificity. Additional treatment of animals with metal chelator 'Unithiol' adjusted only the activity of antioxidant enzymes but not amine oxidases in both organs. Furthermore the in vitro experiment showed that Fenton reaction (hydrogen peroxide in the presence of iron) products alone had no effect on semicarbazide-sensitive amine oxidase activity in rat liver cell fraction whereas supplementation with methylglyoxal resulted in its significant 2.5-fold enhancement. Combined action of the both agents had additive effect on semicarbazide-sensitive amine oxidase activity. We can assume that biogenic amine and polyamine catabolism by amine oxidases is upregulated by oxidative and carbonyl stress factors directly under rhabdomyolysis progression, and the increase in catabolic products concentration contributes to tissue damage in glycerol-induced acute renal failure and apoptosis stimulation in thymus.
[Mh] Termos MeSH primário: Amina Oxidase (contendo Cobre)/metabolismo
Monoaminoxidase/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Rabdomiólise/enzimologia
[Mh] Termos MeSH secundário: Animais
Quelantes/farmacologia
Glicerol
Hepatócitos/efeitos dos fármacos
Hepatócitos/enzimologia
Hepatócitos/patologia
Peróxido de Hidrogênio/antagonistas & inibidores
Peróxido de Hidrogênio/farmacologia
Rim/efeitos dos fármacos
Rim/enzimologia
Rim/patologia
Fígado/efeitos dos fármacos
Fígado/enzimologia
Fígado/patologia
Masculino
Especificidade de Órgãos
Oxirredução
Carbonilação Proteica
Aldeído Pirúvico/antagonistas & inibidores
Aldeído Pirúvico/farmacologia
Ratos
Ratos Wistar
Rabdomiólise/induzido quimicamente
Rabdomiólise/tratamento farmacológico
Rabdomiólise/patologia
Semicarbazidas/antagonistas & inibidores
Semicarbazidas/farmacologia
Timo/efeitos dos fármacos
Timo/enzimologia
Timo/patologia
Unitiol/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chelating Agents); 0 (Reactive Oxygen Species); 0 (Semicarbazides); 37QUC23K2X (carbamylhydrazine); 4076-02-2 (Unithiol); 722KLD7415 (Pyruvaldehyde); BBX060AN9V (Hydrogen Peroxide); EC 1.4.3.21 (Amine Oxidase (Copper-Containing)); EC 1.4.3.4 (Monoamine Oxidase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.079


  4 / 1661 MEDLINE  
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[PMID]:27773573
[Au] Autor:Chaudhuri J; Bose N; Gong J; Hall D; Rifkind A; Bhaumik D; Peiris TH; Chamoli M; Le CH; Liu J; Lithgow GJ; Ramanathan A; Xu XZS; Kapahi P
[Ad] Endereço:The Buck Institute for Research on Aging, 8001 Redwood Boulevard, Novato, CA 94945, USA.
[Ti] Título:A Caenorhabditis elegans Model Elucidates a Conserved Role for TRPA1-Nrf Signaling in Reactive α-Dicarbonyl Detoxification.
[So] Source:Curr Biol;26(22):3014-3025, 2016 Nov 21.
[Is] ISSN:1879-0445
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Reactive α-dicarbonyls (α-DCs), like methylglyoxal (MGO), accumulate with age and have been implicated in aging and various age-associated pathologies, such as diabetic complications and neurodegenerative disorders like Alzheimer's and Parkinson's diseases. Evolutionarily conserved glyoxalases are responsible for α-DC detoxification; however, their core biochemical regulation has remained unclear. We have established a Caenorhabditis elegans model, based on an impaired glyoxalase (glod-4/GLO1), to broadly study α-DC-related stress. We show that, in comparison to wild-type (N2, Bristol), glod-4 animals rapidly exhibit several pathogenic phenotypes, including hyperesthesia, neuronal damage, reduced motility, and early mortality. We further demonstrate TRPA-1/TRPA1 as a sensor for α-DCs, conserved between worms and mammals. Moreover, TRPA-1 activates SKN-1/Nrf via calcium-modulated kinase signaling, ultimately regulating the glutathione-dependent (GLO1) and co-factor-independent (DJ1) glyoxalases to detoxify α-DCs. Interestingly, this pathway is in stark contrast to the TRPA-1 activation and the ensuing calcium flux implicated in cold sensation in C. elegans, whereby DAF-16/FOXO gets activated via complementary kinase signaling. Finally, a phenotypic drug screen using C. elegans identified podocarpic acid as a novel activator of TRPA1 that rescues α-DC-induced pathologies in C. elegans and mammalian cells. Our work thus identifies TRPA1 as a bona fide drug target for the amelioration of α-DC stress, which represents a viable option to address aging-related pathologies in diabetes and neurodegenerative diseases.
[Mh] Termos MeSH primário: Envelhecimento
Proteínas de Caenorhabditis elegans/genética
Caenorhabditis elegans/fisiologia
Aldeído Pirúvico/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 722KLD7415 (Pyruvaldehyde)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28743744
[Au] Autor:Nomura W; Maeta K; Inoue Y
[Ad] Endereço:From the Laboratory of Molecular Microbiology, Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
[Ti] Título:Phosphatidylinositol 3,5-bisphosphate is involved in methylglyoxal-induced activation of the Mpk1 mitogen-activated protein kinase cascade in .
[So] Source:J Biol Chem;292(36):15039-15048, 2017 09 08.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methylglyoxal (MG) is a natural metabolite derived from glycolysis, and this 2-oxoaldehyde has been implicated in some diseases including diabetes. However, the physiological significance of MG for cellular functions is yet to be fully elucidated. We previously reported that MG activates the Mpk1 (MAPK) cascade in the yeast To gain further insights into the cellular functions and responses to MG, we herein screened yeast-deletion mutant collections for susceptibility to MG. We found that mutants defective in the synthesis of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P ) are more susceptible to MG. PtdIns(3,5)P levels increased following MG treatment, and vacuolar morphology concomitantly changed to a single swollen shape. MG activated the Pkc1-Mpk1 MAPK cascade in which a small GTPase Rho1 plays a crucial role, and the MG-induced phosphorylation of Mpk1 was impaired in mutants defective in the PtdIns(3,5)P biosynthetic pathway. Of note, heat shock-induced stress also provoked Mpk1 phosphorylation in a Rho1-dependent manner; however, PtdIns(3,5)P was dispensable for the heat shock-stimulated activation of this signaling pathway. Our results suggest that PtdIns(3,5)P is specifically involved in the MG-induced activation of the Mpk1 MAPK cascade and in the cellular adaptation to MG-induced stress.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fosfatos de Fosfatidilinositol/metabolismo
Aldeído Pirúvico/farmacologia
Saccharomyces cerevisiae/efeitos dos fármacos
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Ativação Enzimática/efeitos dos fármacos
Aldeído Pirúvico/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Phosphatidylinositol Phosphates); 0 (phosphatidylinositol 3,5-diphosphate); 722KLD7415 (Pyruvaldehyde); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.791590


  6 / 1661 MEDLINE  
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[PMID]:28461203
[Au] Autor:Wang Y; Kim HJ; Sparrow JR
[Ad] Endereço:Department of Ophthalmology, Columbia University Medical Center, New York, NY 10032, United States.
[Ti] Título:Quercetin and cyanidin-3-glucoside protect against photooxidation and photodegradation of A2E in retinal pigment epithelial cells.
[So] Source:Exp Eye Res;160:45-55, 2017 07.
[Is] ISSN:1096-0007
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:A family of photoreactive retinaldehyde-derived molecules accumulate in retinal pigment epithelial cells with age; this accumulation is implicated in some retinal diseases. One of these compounds is the diretinal fluorophore A2E. Here we compared polyphenols for their ability to suppress the photooxidation and photodegradation of A2E. In cells that had accumulated A2E and were irradiated with short-wavelength light, quercetin, cyanidin-3-glucoside, ferulic acid and chlorogenic acid diminished cellular levels of reactive oxygen species, but only quercetin and cyanidin-3-glucoside promoted cell viability. By chromatographic quantitation, quercetin and cyanidin-3-glucoside reduced the consumption of A2E by photooxidation in both cell- and cell-free assays. With ultra-high performance liquid chromatography-mass spectrometry, quercetin and cyanidin-3-glucoside also inhibited the formation of photooxidized-A2E species. While photodegradation of A2E is known to result in the release of reactive carbonyls, we demonstrated that quercetin and cyanidin-3-glucoside decreased the formation of methylglyoxal adducts in the cells, and reduced the expression of mRNA encoding receptor for advanced glycation end products. These polyphenols also protected glutathione from reaction with photooxidized A2E. In rod outer segments incubated with all-trans-retinal to generate bisretinoid, followed by irradiation, quercetin and cyanidin-3-glucoside reduced release of the lipid peroxidation product 4-hydroxynonenal. In conclusion, quercetin and cyanidin-3-glucoside can guard against photooxidative processes in retina.
[Mh] Termos MeSH primário: Antocianinas/farmacologia
Glucosídeos/farmacologia
Degeneração Macular/prevenção & controle
Fotólise/efeitos dos fármacos
Quercetina/farmacologia
Epitélio Pigmentado da Retina/metabolismo
[Mh] Termos MeSH secundário: Antioxidantes/farmacologia
Células Cultivadas
Cromatografia Líquida de Alta Pressão
Seres Humanos
Degeneração Macular/metabolismo
Degeneração Macular/patologia
Espectrometria de Massas
Aldeído Pirúvico/metabolismo
Receptor para Produtos Finais de Glicação Avançada/metabolismo
Epitélio Pigmentado da Retina/efeitos dos fármacos
Epitélio Pigmentado da Retina/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Anthocyanins); 0 (Antioxidants); 0 (Glucosides); 0 (Receptor for Advanced Glycation End Products); 7084-24-4 (cyanidin 3-O-glucoside); 722KLD7415 (Pyruvaldehyde); 9IKM0I5T1E (Quercetin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171211
[Lr] Data última revisão:
171211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  7 / 1661 MEDLINE  
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[PMID]:28919305
[Au] Autor:Suh KS; Chon S; Jung WW; Choi EM
[Ad] Endereço:Dept. of Endocrinology & Metabolism, School of Medicine, Kyung Hee University, Seoul, 02447, Republic of Korea.
[Ti] Título:Magnolol protects pancreatic ß-cells against methylglyoxal-induced cellular dysfunction.
[So] Source:Chem Biol Interact;277:101-109, 2017 Nov 01.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Chronic hyperglycemia aggravates insulin resistance, in part due to increased formation of advanced glycation end-products (AGEs). Methylglyoxal (MG), a major precursor of AGEs, accumulates abnormally in various tissues and organs and participates in oxidative damage. We investigated the insulinotropic benefits of magnolol, a hydroxylated biphenyl compound isolated from Magnolia officinalis, in pancreatic ß-cells exposed to MG in vitro. When exposed to cytotoxic levels of MG for 48 h, RIN-m5F ß-cells exhibited a significant loss of viability and impaired insulin secretion, whereas pretreatment with magnolol protected against MG-induced cell death and decreased insulin secretion. Moreover, magnolol increased the expression of genes involved in ß-cell survival and function, including Ins2 and PDX1. Furthermore, magnolol increased the levels of AMPK phosphorylation, SIRT1, and PGC1α in RIN-5F ß-cells. In addition, magnolol increased the activity of glyoxalase I and decreased the levels of MG-modified protein adducts, which suggests that magnolol protects against MG-induced protein glycation. Taken together, the results indicate the potential application of magnolol as an intervention against MG-induced hyperglycemia.
[Mh] Termos MeSH primário: Compostos de Bifenilo/farmacologia
Citoproteção/efeitos dos fármacos
Células Secretoras de Insulina/efeitos dos fármacos
Lignanas/farmacologia
Substâncias Protetoras/farmacologia
Aldeído Pirúvico/metabolismo
[Mh] Termos MeSH secundário: Animais
Compostos de Bifenilo/química
Compostos de Bifenilo/isolamento & purificação
Morte Celular/efeitos dos fármacos
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Insulina/metabolismo
Células Secretoras de Insulina/citologia
Células Secretoras de Insulina/metabolismo
Lignanas/química
Lignanas/isolamento & purificação
Magnolia/química
Substâncias Protetoras/química
Substâncias Protetoras/isolamento & purificação
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biphenyl Compounds); 0 (Insulin); 0 (Lignans); 0 (Protective Agents); 001E35HGVF (magnolol); 722KLD7415 (Pyruvaldehyde)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE


  8 / 1661 MEDLINE  
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[PMID]:28918740
[Au] Autor:Sudnitsyna MV; Gusev NB
[Ad] Endereço:Lomonosov Moscow State University, Faculty of Biology, Moscow, 119991, Russia. NBGusev@mail.ru.
[Ti] Título:Methylglyoxal and Small Heat Shock Proteins.
[So] Source:Biochemistry (Mosc);82(7):751-759, 2017 Jul.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Methylglyoxal is a highly reactive dicarbonyl compound formed during glucose metabolism and able to modify phospholipids, nucleic acids, and proteins belonging to the so-called dicarbonyl proteome. Small heat shock proteins participating in protection of the cell against different unfavorable conditions can be modified by methylglyoxal. The probability of methylglyoxal modification is increased in the case of distortion of glucose metabolism (diabetes), in the case of utilization of glycolysis as the main source of energy (malignancy), and/or at low rate of modified protein turnover. We have analyzed data on modification of small heat shock protein HspB1 in different tumors and under distortion of carbohydrate metabolism. Data on the effect of methylglyoxal modification on stability, chaperone-like activity, and antiapoptotic activity of HspB1 were analyzed. We discuss data on methylglyoxal modifications of lens α-crystallins. The mutual dependence and mutual effects of methylglyoxal modification and other posttranslational modifications of lens crystallins are analyzed. We conclude that although there is no doubt that the small heat shock proteins undergo methylglyoxal modification, the physiological significance of this process remains enigmatic, and new experimental approaches should be developed for understanding how this type of modification affects functioning of small heat shock proteins in the cell.
[Mh] Termos MeSH primário: Proteínas de Choque Térmico Pequenas/metabolismo
Aldeído Pirúvico/química
[Mh] Termos MeSH secundário: Proteínas de Choque Térmico HSP20/química
Proteínas de Choque Térmico HSP20/metabolismo
Proteínas de Choque Térmico HSP27/química
Proteínas de Choque Térmico HSP27/metabolismo
Proteínas de Choque Térmico Pequenas/química
Seres Humanos
Cristalino/química
Cristalino/metabolismo
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (HSP20 Heat-Shock Proteins); 0 (HSP27 Heat-Shock Proteins); 0 (HSPB1 protein, human); 0 (HSPB6 protein, human); 0 (Heat-Shock Proteins, Small); 722KLD7415 (Pyruvaldehyde)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170919
[St] Status:MEDLINE
[do] DOI:10.1134/S000629791707001X


  9 / 1661 MEDLINE  
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[PMID]:28834691
[Au] Autor:Vistoli G; Colzani M; Mazzolari A; Gilardoni E; Rivaletto C; Carini M; Aldini G
[Ad] Endereço:Department of Pharmaceutical Sciences, Università degli Studi di Milano, via Mangiagalli 25, 20133, Milan, Italy.
[Ti] Título:Quenching activity of carnosine derivatives towards reactive carbonyl species: Focus on α-(methylglyoxal) and ß-(malondialdehyde) dicarbonyls.
[So] Source:Biochem Biophys Res Commun;492(3):487-492, 2017 Oct 21.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The study combines HPLC-based with MS-based competitive analyses to evaluate the quenching activity of a set of carnosine derivatives towards methylglyoxal (MGO) and malondialdehyde (MDA) chosen as representative of α- and ß-dicarbonyls, respectively. The obtained results underline that these derivatives are moderately reactive towards MDA with which they form the corresponding N-propenal adduct via Michael addition. In contrast they proved a rather poor quenching activity towards MGO with which they can condense to give MOLD-like adducts through a concerted mechanism involving more quenchers molecules. Even though both quenching mechanisms involve the amino group in its neutral form, in silico studies revealed that the reported reactivity values depend on different stereo-electronic parameters which are reflected in the different observed quenching mechanism. Finally, the MGO quenching reactivity and the unselective (and unwanted) pyridoxal quenching are found to be influenced by the same parameters thus rationalizing the known difficulty in the design of potent and selective quenchers towards ß-dicarbonyls.
[Mh] Termos MeSH primário: Carnosina/química
Malondialdeído/química
Aldeído Pirúvico/química
[Mh] Termos MeSH secundário: Cromatografia Líquida de Alta Pressão
Espectrometria de Massas
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
4Y8F71G49Q (Malondialdehyde); 722KLD7415 (Pyruvaldehyde); 8HO6PVN24W (Carnosine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE


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[PMID]:28820963
[Au] Autor:Salomón T; Sibbersen C; Hansen J; Britz D; Svart MV; Voss TS; Møller N; Gregersen N; Jørgensen KA; Palmfeldt J; Poulsen TB; Johannsen M
[Ad] Endereço:Department of Forensic Medicine, Aarhus University, Aarhus 8200, Denmark.
[Ti] Título:Ketone Body Acetoacetate Buffers Methylglyoxal via a Non-enzymatic Conversion during Diabetic and Dietary Ketosis.
[So] Source:Cell Chem Biol;24(8):935-943.e7, 2017 Aug 17.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The α-oxoaldehyde methylglyoxal is a ubiquitous and highly reactive metabolite known to be involved in aging- and diabetes-related diseases. If not detoxified by the endogenous glyoxalase system, it exerts its detrimental effects primarily by reacting with biopolymers such as DNA and proteins. We now demonstrate that during ketosis, another metabolic route is operative via direct non-enzymatic aldol reaction between methylglyoxal and the ketone body acetoacetate, leading to 3-hydroxyhexane-2,5-dione. This novel metabolite is present at a concentration of 10%-20% of the methylglyoxal level in the blood of insulin-starved patients. By employing a metabolite-alkyne-tagging strategy it is clarified that 3-hydroxyhexane-2,5-dione is further metabolized to non-glycating species in human blood. The discovery represents a new direction within non-enzymatic metabolism and within the use of alkyne-tagging for metabolism studies and it revitalizes acetoacetate as a competent endogenous carbon nucleophile.
[Mh] Termos MeSH primário: Acetoacetatos/química
Corpos Cetônicos/química
Aldeído Pirúvico/sangue
[Mh] Termos MeSH secundário: Acetoacetatos/metabolismo
Alquinos/química
Sequência de Aminoácidos
Cromatografia Líquida de Alta Pressão
Diabetes Mellitus/metabolismo
Diabetes Mellitus/patologia
Hexanonas/análise
Hexanonas/sangue
Hexanonas/metabolismo
Seres Humanos
Corpos Cetônicos/metabolismo
Espectrometria de Massas
Aldeído Pirúvico/análise
Aldeído Pirúvico/metabolismo
Albumina Sérica/química
Albumina Sérica/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetoacetates); 0 (Alkynes); 0 (Hexanones); 0 (Ketone Bodies); 0 (Serum Albumin); 4ZI204Y1MC (acetoacetic acid); 722KLD7415 (Pyruvaldehyde)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE



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