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[PMID]:27776915
[Au] Autor:Mendler M; Riedinger C; Schlotterer A; Volk N; Fleming T; Herzig S; Nawroth PP; Morcos M
[Ad] Endereço:Department of Medicine 1 and Clinical Chemistry, University of Heidelberg, Im Neuenheimer Feld 410, 69120 Heidelberg, Germany. Electronic address: michael.mendler@med.uni-heidelberg.de.
[Ti] Título:Reduction in ins-7 gene expression in non-neuronal cells of high glucose exposed Caenorhabditis elegans protects from reactive metabolites, preserves neuronal structure and head motility, and prolongs lifespan.
[So] Source:J Diabetes Complications;31(2):304-310, 2017 Feb.
[Is] ISSN:1873-460X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glucose derived metabolism generates reactive metabolites affecting the neuronal system and lifespan in C. elegans. Here, the role of the insulin homologue ins-7 and its downstream effectors in the generation of high glucose induced neuronal damage and shortening of lifespan was studied. RESULTS: In C. elegans high glucose conditions induced the expression of the insulin homologue ins-7. Abrogating ins-7 under high glucose conditions in non-neuronal cells decreased reactive oxygen species (ROS)-formation and accumulation of methylglyoxal derived advanced glycation endproducts (AGEs), prevented structural neuronal damage and normalised head motility and lifespan. The restoration of lifespan by decreased ins-7 expression was dependent on the concerted action of sod-3 and glod-4 coding for the homologues of iron-manganese superoxide dismutase and glyoxalase 1, respectively. CONCLUSIONS: Under high glucose conditions mitochondria-mediated oxidative stress and glycation are downstream targets of ins-7. This impairs the neuronal system and longevity via a non-neuronal/neuronal crosstalk by affecting sod-3 and glod-4, thus giving further insight into the pathophysiology of diabetic complications.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/antagonistas & inibidores
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Glucose/envenenamento
Lactoilglutationa Liase/metabolismo
Estresse Oxidativo
Hormônios Peptídicos/antagonistas & inibidores
Superóxido Dismutase/metabolismo
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Caenorhabditis elegans/enzimologia
Caenorhabditis elegans/crescimento & desenvolvimento
Proteínas de Caenorhabditis elegans/agonistas
Proteínas de Caenorhabditis elegans/genética
Retroalimentação Fisiológica
Técnicas de Silenciamento de Genes
Técnicas de Inativação de Genes
Produtos Finais de Glicação Avançada/metabolismo
Lactoilglutationa Liase/antagonistas & inibidores
Lactoilglutationa Liase/genética
Longevidade
Mutação
Neuroproteção
Concentração Osmolar
Hormônios Peptídicos/agonistas
Hormônios Peptídicos/genética
Hormônios Peptídicos/metabolismo
Interferência de RNA
Espécies Reativas de Oxigênio/metabolismo
Superóxido Dismutase/antagonistas & inibidores
Superóxido Dismutase/genética
Análise de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Glycation End Products, Advanced); 0 (Ins-7 protein, C elegans); 0 (Peptide Hormones); 0 (Reactive Oxygen Species); EC 1.15.1.1 (Sod-3 protein, C elegans); EC 1.15.1.1 (Superoxide Dismutase); EC 4.4.1.5 (Lactoylglutathione Lyase); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 1091 MEDLINE  
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[PMID]:29324881
[Au] Autor:Yan G; Xiao X; Wang N; Zhang F; Gao G; Xu K; Chen B; Qiao J; Wu X
[Ad] Endereço:Oil Crops Research Institute of the Chinese Academy of Agricultural Sciences, Key Laboratory of Biology and Genetic Improvement of Oil Crops, Ministry of Agriculture, Wuhan, P. R. China.
[Ti] Título:Genome-wide analysis and expression profiles of glyoxalase gene families in Chinese cabbage (Brassica rapa L).
[So] Source:PLoS One;13(1):e0191159, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The glyoxalase pathway is composed of glyoxalase I (GLYI) and glyoxalase II (GLYII) and is responsible for the detoxification of a cytotoxic metabolite methylglyoxal (MG) into the nontoxic S-D-lactoylglutathione. The two glyoxalase enzymes play a crucial role in stress tolerance in various plant species. Recently, the GLY gene families have well been analyzed in Arabidopsis, rice and soybean, however, little is known about them in Chinese cabbage (Brassica rapa). Here, 16 BrGLYI and 15 BrGLYII genes were identified in the B. rapa genome, and the BrGLYI and BrGLYII proteins were both clustered into five subfamilies. The classifications, chromosomal distributions, gene duplications, exon-intron structures, localizations, conserved motifs and promoter cis-elements were also predicted and analyzed. In addition, the expression pattern of these genes in different tissues and their response to biotic and abiotic stresses were analyzed using publicly available data and a quantitative real-time PCR analysis (RT-qPCR). The results indicated that the expression profiles of BrGLY genes varied among different tissues. Notably, a number of BrGLY genes showed responses to biotic and abiotic stress treatments, including Plasmodiophora brassicae infection and various heavy metal stresses. Taken together, this study identifies BrGLYI and BrGLYII gene families in B. rapa and offers insight into their roles in plant development and stress resistance, especially in heavy metal stress tolerance and pathogen resistance.
[Mh] Termos MeSH primário: Brassica rapa/genética
Perfilação da Expressão Gênica
Lactoilglutationa Liase/genética
[Mh] Termos MeSH secundário: Genes de Plantas
Lactoilglutationa Liase/classificação
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191159


  3 / 1091 MEDLINE  
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[PMID]:29225125
[Au] Autor:Shimada N; Takasawa R; Tanuma SI
[Ad] Endereço:Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
[Ti] Título:Interdependence of GLO I and PKM2 in the Metabolic shift to escape apoptosis in GLO I-dependent cancer cells.
[So] Source:Arch Biochem Biophys;638:1-7, 2018 01 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many cancer cells undergo metabolic reprogramming known as the Warburg effect, which is characterized by a greater dependence on glycolysis for ATP generation, even under normoxic conditions. Glyoxalase I (GLO I) is a rate-limiting enzyme involved in the detoxification of cytotoxic methylglyoxal formed in glycolysis and which is known to be highly expressed in many cancer cells. Thus, specific inhibitors of GLO I are expected to be effective anticancer drugs. We previously discovered a novel GLO I inhibitor named TLSC702. Although the strong inhibitory activity of TLSC702 was observed in the in vitro enzyme assay, higher concentrations were required to induce apoptosis at the cellular level. One of the proposed reasons for this difference is that cancer cells alter the energy metabolism leading them to become more dependent on mitochondrial respiration than glycolysis (Metabolic shift) to avoid apoptosis induction. Thus, we assumed that combination of TLSC702 with shikonin-a specific inhibitor of pyruvate kinase M2 (PKM2) that acts as a driver of TCA cycle by supplying pyruvate and which is known to be specifically expressed in cancer cells-would have anticancer effects. We herein show the anticancer effects of combination treatment with TLSC702 and shikonin, and a possible anticancer mechanism.
[Mh] Termos MeSH primário: Apoptose
Proteínas de Transporte/metabolismo
Lactoilglutationa Liase/metabolismo
Proteínas de Membrana/metabolismo
Proteínas de Neoplasias/metabolismo
Neoplasias/enzimologia
Piruvato Quinase/metabolismo
Hormônios Tireóideos/metabolismo
[Mh] Termos MeSH secundário: Butiratos/farmacologia
Proteínas de Transporte/antagonistas & inibidores
Proteínas de Transporte/genética
Linhagem Celular Tumoral
Ciclo do Ácido Cítrico/efeitos dos fármacos
Ensaios de Seleção de Medicamentos Antitumorais
Seres Humanos
Lactoilglutationa Liase/antagonistas & inibidores
Lactoilglutationa Liase/genética
Proteínas de Membrana/antagonistas & inibidores
Proteínas de Membrana/genética
Naftoquinonas/farmacologia
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/genética
Neoplasias/tratamento farmacológico
Neoplasias/genética
Neoplasias/patologia
Piruvato Quinase/antagonistas & inibidores
Piruvato Quinase/genética
Ácido Pirúvico/metabolismo
Tiazóis/farmacologia
Hormônios Tireóideos/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (3-(1,3-benzothiazol-2-yl)-4-(4-methoxyphenyl)but-3-enoic acid); 0 (Butyrates); 0 (Carrier Proteins); 0 (Membrane Proteins); 0 (Naphthoquinones); 0 (Neoplasm Proteins); 0 (Thiazoles); 0 (Thyroid Hormones); 0 (thyroid hormone-binding proteins); 3IK6592UBW (shikonin); 8558G7RUTR (Pyruvic Acid); EC 2.7.1.40 (Pyruvate Kinase); EC 4.4.1.5 (GLO1 protein, human); EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171212
[St] Status:MEDLINE


  4 / 1091 MEDLINE  
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[PMID]:28929505
[Au] Autor:Burdelski C; Shihada R; Hinsch A; Angerer A; Göbel C; Friedrich E; Hube-Magg C; Burdak-Rothkamm S; Kluth M; Simon R; Möller-Koop C; Sauter G; Büscheck F; Wittmer C; Clauditz TS; Krech T; Tsourlakis MC; Minner S; Graefen M; Schlomm T; Wilczak W; Jacobsen F
[Ad] Endereço:Institute of Pathology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
[Ti] Título:High-Level Glyoxalase 1 (GLO1) expression is linked to poor prognosis in prostate cancer.
[So] Source:Prostate;77(15):1528-1538, 2017 Nov.
[Is] ISSN:1097-0045
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Glyoxalase 1 (GLO1) is an enzyme involved in removal of toxic byproducts accumulating during glycolysis from the cell. GLO1 is up regulated in many cancer types but its role in prostate cancer is largely unknown. METHODS: Here, we employed GLO1 immunohistochemistry on a tissue microarray including 11 152 tumors and an attached clinical and molecular database. RESULTS: Normal prostate epithelium was negative for GLO1, whereas 2059 (27.3%) of 7552 interpretable cancers showed cytoplasmic GLO1 staining, which was considered weak in 8.8%, moderate in 12.5%, and strong in 6.1% of tumors. Up regulation of GLO1 was significantly linked to high original Gleason grade, advanced pathological tumor stage and positive lymph node status (P < 0.0001 each). Comparison of GLO1 staining with several common genomic alterations of prostate cancers revealed a strong link between GLO1 up regulation and TMPRSS2:ERG fusion (P < 0.0001) and an ERG-independent association with PTEN deletion (P < 0.0001). GLO1 up regulation was strongly linked to early biochemical recurrence in univariate analysis (P < 0.0001) and predicted poor prognosis independent from most (except from nodal stage) established prognostic parameters in multivariate analysis (P ≤ 0.03). CONCLUSIONS: GLO1 upregulation is linked to aggressive prostate cancers characterized by ERG fusion and PTEN deletion. The strong and independent prognostic value makes it a promising candidate for routine diagnostic applications either alone or in combination with other markers.
[Mh] Termos MeSH primário: Lactoilglutationa Liase/biossíntese
Neoplasias da Próstata/enzimologia
[Mh] Termos MeSH secundário: Idoso
Biomarcadores Tumorais/biossíntese
Seres Humanos
Imuno-Histoquímica
Calicreínas/metabolismo
Masculino
Meia-Idade
Recidiva Local de Neoplasia/enzimologia
Prognóstico
Antígeno Prostático Específico/metabolismo
Análise Serial de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); EC 3.4.21.- (Kallikreins); EC 3.4.21.- (kallikrein-related peptidase 3, human); EC 3.4.21.77 (Prostate-Specific Antigen); EC 4.4.1.5 (GLO1 protein, human); EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE
[do] DOI:10.1002/pros.23431


  5 / 1091 MEDLINE  
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[PMID]:28695773
[Au] Autor:Tesarova P; Zima T; Kubena AA; Kalousova M
[Ad] Endereço:1 Department of Oncology, First Faculty of Medicine, Charles University and General University Hospital, Prague, Czech Republic.
[Ti] Título:Polymorphisms of the receptor for advanced glycation end products and glyoxalase I and long-term outcome in patients with breast cancer.
[So] Source:Tumour Biol;39(7):1010428317702902, 2017 Jul.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Receptor for advanced glycation end products and glyoxalase I metabolizing advanced glycation end product precursors may play important role in the pathogenesis and progression of cancer. Potential relation between soluble forms of receptor for advanced glycation end products (sRAGE), receptor for advanced glycation end products, glyoxalase I polymorphisms, and long-term outcome (median follow-up of 10.3 years) was studied in 116 patients with breast cancer. Gly82Ser and 2184 A/G RAGE polymorphisms were related to the mortality due to the breast cancer and -419 A/C glyoxalase I polymorphism was related to the overall mortality of the patients suggesting their role not only in the risk of breast cancer but also in the outcome of patients with breast cancer.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Lactoilglutationa Liase/genética
Receptor para Produtos Finais de Glicação Avançada/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Neoplasias da Mama/mortalidade
Neoplasias da Mama/patologia
Feminino
Seres Humanos
Estimativa de Kaplan-Meier
Meia-Idade
Polimorfismo de Nucleotídeo Único
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptor for Advanced Glycation End Products); EC 4.4.1.5 (GLO1 protein, human); EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170712
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317702902


  6 / 1091 MEDLINE  
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[PMID]:28623132
[Au] Autor:Jang S; Kwon DM; Kwon K; Park C
[Ad] Endereço:Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 291, Daehak-ro, Yuseong-gu, Daejeon 34141, Republic of Korea.
[Ti] Título:Generation and characterization of mouse knockout for glyoxalase 1.
[So] Source:Biochem Biophys Res Commun;490(2):460-465, 2017 Aug 19.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Glyoxalase 1 (Glo1) is the first enzyme involved in glutathione-dependent detoxification of methylglyoxal, eventually generating d-lactate by the second enzyme glyoxalase 2 (Glo2). An accumulation of intracellular glyoxal and methylglyoxal leads to protein malfunction and mutation via formation of the advanced glycation end products (AGEs). Studies on mouse behavior suggest that methylglyoxal has anxiolytic properties. In this report, we generated and characterized a mouse knockout for Glo1. The knockout mice were viable without a pronounced phenotypic defect. Increased level of AGEs in Glo1 knockout mice was detected by immunoblotting with anti-MGH1 in liver homogenate, but not in brain. Alterations in behavior were observed in open field, light-dark transition, and tail suspension test. Open field data indicate increased exploration for novel environment and entry/stay in center zone in Glo1 knockout mice. In addition, increased light-dark transition and immobility was observed in the knockout mice. These data indicate that Glo1 knockout reduces anxiety-like behavior, but increases depression-like behavior.
[Mh] Termos MeSH primário: Ansiedade/genética
Depressão/genética
Lactoilglutationa Liase/genética
[Mh] Termos MeSH secundário: Animais
Ansiedade/metabolismo
Depressão/metabolismo
Deleção de Genes
Glutationa/metabolismo
Produtos Finais de Glicação Avançada/metabolismo
Glioxal/metabolismo
Lactoilglutationa Liase/metabolismo
Fígado/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Aldeído Pirúvico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycation End Products, Advanced); 50NP6JJ975 (Glyoxal); 722KLD7415 (Pyruvaldehyde); EC 4.4.1.5 (Lactoylglutathione Lyase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170618
[St] Status:MEDLINE


  7 / 1091 MEDLINE  
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[PMID]:28409415
[Au] Autor:Mahmud JA; Hasanuzzaman M; Nahar K; Rahman A; Hossain MS; Fujita M
[Ad] Endereço:Laboratory of Plant Stress Responses, Department of Applied Biological Science, Faculty of Agriculture, Kagawa University, Miki-cho, Kita-gun, Kagawa, 761-0795, Japan.
[Ti] Título:γ-aminobutyric acid (GABA) confers chromium stress tolerance in Brassica juncea L. by modulating the antioxidant defense and glyoxalase systems.
[So] Source:Ecotoxicology;26(5):675-690, 2017 Jul.
[Is] ISSN:1573-3017
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chromium (Cr) toxicity is hazardous to the seed germination, growth, and development of plants. γ-aminobutyric acid (GABA) is a non-protein amino acid and is involved in stress tolerance in plants. To investigate the effects of GABA in alleviating Cr toxicity, we treated eight-d-old mustard (Brassica juncea L.) seedlings with Cr (0.15 and 0.3 mM K CrO , 5 days) alone and in combination with GABA (125 µM) in a semi-hydroponic medium. The roots and shoots of the seedlings accumulated Cr in a dose-dependent manner, which led to an increase in oxidative damage [lipid peroxidation; hydrogen peroxide (H O ) content; superoxide (O ) generation; lipoxygenase (LOX) activity], methylglyoxal (MG) content, and disrupted antioxidant defense and glyoxalase systems. Chromium stress also reduced growth, leaf relative water content (RWC), and chlorophyll (chl) content but increased phytochelatin (PC) and proline (Pro) content. Furthermore, supplementing the Cr-treated seedlings with GABA reduced Cr uptake and upregulated the non-enzymatic antioxidants (ascorbate, AsA; glutathione, GSH) and the activities of the enzymatic antioxidants including ascorbate peroxidase (APX), monodehydroascorbate reductase (MDHAR), dehydroascorbate reductase (DHAR), glutathione reductase (GR), glutathione peroxidase (GPX), superoxide dismutase (SOD), catalase (CAT), glyoxalase I (Gly I), and glyoxalase II (Gly II), and finally reduced oxidative damage. Adding GABA also increased leaf RWC and chl content, decreased Pro and PC content, and restored plant growth. These findings shed light on the effect of GABA in improving the physiological mechanisms of mustard seedlings in response to Cr stress.
[Mh] Termos MeSH primário: Adaptação Fisiológica/fisiologia
Cromo/toxicidade
Mostardeira/fisiologia
Poluentes do Solo/toxicidade
Ácido gama-Aminobutírico/metabolismo
[Mh] Termos MeSH secundário: Antioxidantes/metabolismo
Ascorbato Peroxidases/metabolismo
Ácido Ascórbico/metabolismo
Catalase/metabolismo
Clorofila/metabolismo
Glutationa/metabolismo
Glutationa Peroxidase/metabolismo
Glutationa Redutase/metabolismo
Peróxido de Hidrogênio/metabolismo
Lactoilglutationa Liase/metabolismo
Fitoquelatinas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Superóxido Dismutase/metabolismo
Tioléster Hidrolases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Reactive Oxygen Species); 0 (Soil Pollutants); 0R0008Q3JB (Chromium); 1406-65-1 (Chlorophyll); 56-12-2 (gamma-Aminobutyric Acid); 98726-08-0 (Phytochelatins); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.6 (Catalase); EC 1.11.1.9 (Glutathione Peroxidase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.8.1.7 (Glutathione Reductase); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.6 (hydroxyacylglutathione hydrolase); EC 4.4.1.5 (Lactoylglutathione Lyase); GAN16C9B8O (Glutathione); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1007/s10646-017-1800-9


  8 / 1091 MEDLINE  
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[PMID]:28361585
[Au] Autor:Scott GF; Nguyen AQ; Cherry BH; Hollrah RA; Salinas I; Williams AG; Ryou MG; Mallet RT
[Ad] Endereço:1 Institute for Cardiovascular and Metabolic Diseases, University of North Texas Health Science Center, Fort Worth, TX 76107, USA.
[Ti] Título:Featured Article: Pyruvate preserves antiglycation defenses in porcine brain after cardiac arrest.
[So] Source:Exp Biol Med (Maywood);242(10):1095-1103, 2017 May.
[Is] ISSN:1535-3699
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cardiac arrest (CA) and cardiocerebral resuscitation (CCR)-induced ischemia-reperfusion imposes oxidative and carbonyl stress that injures the brain. The ischemic shift to anaerobic glycolysis, combined with oxyradical inactivation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), provokes excessive formation of the powerful glycating agent, methylglyoxal. The glyoxalase (GLO) system, comprising the enzymes glyoxalase 1 (GLO1) and GLO2, utilizes reduced glutathione (GSH) supplied by glutathione reductase (GR) to detoxify methylglyoxal resulting in reduced protein glycation. Pyruvate, a natural antioxidant that augments GSH redox status, could sustain the GLO system in the face of ischemia-reperfusion. This study assessed the impact of CA-CCR on the cerebral GLO system and pyruvate's ability to preserve this neuroprotective system following CA. Domestic swine were subjected to 10 min CA, 4 min closed-chest CCR, defibrillation and 4 h recovery, or to a non-CA sham protocol. Sodium pyruvate or NaCl control was infused (0.1 mmol/kg/min, intravenous) throughout CCR and the first 60 min recovery. Protein glycation, GLO1 content, and activities of GLO1, GR, and GAPDH were analyzed in frontal cortex biopsied at 4 h recovery. CA-CCR produced marked protein glycation which was attenuated by pyruvate treatment. GLO1, GR, and GAPDH activities fell by 86, 55, and 30%, respectively, after CA-CCR with NaCl infusion. Pyruvate prevented inactivation of all three enzymes. CA-CCR sharply lowered GLO1 monomer content with commensurate formation of higher molecular weight immunoreactivity; pyruvate preserved GLO1 monomers. Thus, ischemia-reperfusion imposed by CA-CCR disabled the brain's antiglycation defenses. Pyruvate preserved these enzyme systems that protect the brain from glycation stress. Impact statement Recent studies have demonstrated a pivotal role of protein glycation in brain injury. Methylglyoxal, a by-product of glycolysis and a powerful glycating agent in brain, is detoxified by the glutathione-catalyzed glyoxalase (GLO) system, but the impact of cardiac arrest (CA) and cardiocerebral resuscitation (CCR) on the brain's antiglycation defenses is unknown. This study in a swine model of CA and CCR demonstrated for the first time that the intense cerebral ischemia-reperfusion imposed by CA-resuscitation disabled glyoxalase-1 and glutathione reductase (GR), the source of glutathione for methylglyoxal detoxification. Moreover, intravenous administration of pyruvate, a redox-active intermediary metabolite and antioxidant in brain, prevented inactivation of glyoxalase-1 and GR and blunted protein glycation in cerebral cortex. These findings in a large mammal are first evidence of GLO inactivation and the resultant cerebral protein glycation after CA-resuscitation, and identify novel actions of pyruvate to minimize protein glycation in postischemic brain.
[Mh] Termos MeSH primário: Encéfalo/patologia
Parada Cardíaca/terapia
Fármacos Neuroprotetores/administração & dosagem
Aldeído Pirúvico/toxicidade
Ácido Pirúvico/administração & dosagem
Traumatismo por Reperfusão/prevenção & controle
Ressuscitação/efeitos adversos
[Mh] Termos MeSH secundário: Animais
Córtex Cerebral/patologia
Modelos Animais de Doenças
Glutationa Redutase/análise
Gliceraldeído-3-Fosfato Desidrogenase (Fosforiladora)/análise
Glicosilação
Lactoilglutationa Liase/análise
Estresse Oxidativo
Suínos
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neuroprotective Agents); 722KLD7415 (Pyruvaldehyde); 8558G7RUTR (Pyruvic Acid); EC 1.2.1.12 (Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)); EC 1.8.1.7 (Glutathione Reductase); EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE
[do] DOI:10.1177/1535370217703353


  9 / 1091 MEDLINE  
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[PMID]:28358304
[Au] Autor:Kaur C; Sharma S; Hasan MR; Pareek A; Singla-Pareek SL; Sopory SK
[Ad] Endereço:Stress Physiology and Molecular Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University, New Delhi 110067, India. charanpreet06@gmail.com.
[Ti] Título:Characteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.
[So] Source:Int J Mol Sci;18(4), 2017 Mar 30.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The glyoxalase system is the ubiquitous pathway for the detoxification of methylglyoxal (MG) in the biological systems. It comprises two enzymes, glyoxalase I (GLYI) and glyoxalase II (GLYII), which act sequentially to convert MG into d-lactate, thereby helping living systems get rid of this otherwise cytotoxic byproduct of metabolism. In addition, a glutathione-independent GLYIII enzyme activity also exists in the biological systems that can directly convert MG to d-lactate. Humans and possess a single copy of (encoding either the Ni- or Zn-dependent form) and genes, which through MG detoxification provide protection against various pathological and disease conditions. By contrast, the plant genome possesses multiple and genes with a role in abiotic stress tolerance. Plants possess both Ni - and Zn -dependent forms of GLYI, and studies on plant glyoxalases reveal the various unique features of these enzymes distinguishing them from prokaryotic and other eukaryotic glyoxalases. Through this review, we provide an overview of the plant glyoxalase family along with a comparative analysis of glyoxalases across various species, highlighting similarities as well as differences in the biochemical, molecular, and physiological properties of these enzymes. We believe that the evolution of multiple glyoxalases isoforms in plants is an important component of their robust defense strategies.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Lactoilglutationa Liase/metabolismo
Proteínas de Plantas/metabolismo
Plantas/enzimologia
Tioléster Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/química
Aldeído Oxirredutases/genética
Animais
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Evolução Molecular
Lactoilglutationa Liase/química
Lactoilglutationa Liase/genética
Proteínas de Plantas/química
Proteínas de Plantas/genética
Plantas/genética
Tioléster Hidrolases/química
Tioléster Hidrolases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Plant Proteins); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.- (glyoxalase III); EC 3.1.2.- (Thiolester Hydrolases); EC 3.1.2.6 (hydroxyacylglutathione hydrolase); EC 4.4.1.5 (Lactoylglutathione Lyase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170507
[Lr] Data última revisão:
170507
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE


  10 / 1091 MEDLINE  
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[PMID]:28320998
[Au] Autor:Jin T; Zhai J; Liu X; Yue Y; Huang M; Li Z; Ni C; Deng Q; Sang Y; Yao Z; Zhang H; Hu X; Zheng ZB
[Ad] Endereço:Antibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Insititute of Antibiotics, Chengdu University.
[Ti] Título:Design, Synthesis and Biological Evaluation of Potent Human Glyoxalase I Inhibitors.
[So] Source:Chem Pharm Bull (Tokyo);65(5):455-460, 2017 May 01.
[Is] ISSN:1347-5223
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Several glutathione derivatives bearing the S-(N-aryl-N-hydroxycarbamoyl) or S-(C-aryl-N-hydroxycarbamoyl) moieties (10, 10', 13-15) were synthesized, characterized, and their human glyoxalase I (hGLO1) inhibitory activity was evaluated. Compound 10 was proved to be the effective hGLO1 inhibitor with a K value of 1.0 nM and the inhibition effect of compound 10 on hGLO1 was nearly ten-fold higher than that of the strongest inhibitor 2 (K =10.0 nM) which has been reported in the field of glutathione-type hGLO1 inhibitors. Its diethyl ester prodrug 10' was able to penetrate cell membrane and had good inhibitory effect on the growth of NCI-H522 cell xenograft tumor model.
[Mh] Termos MeSH primário: Desenho de Drogas
Ésteres/síntese química
Glutationa/síntese química
Lactoilglutationa Liase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Bioensaio
Linhagem Celular Tumoral
Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Ésteres/química
Ésteres/farmacologia
Glutationa/química
Glutationa/farmacologia
Seres Humanos
Camundongos
Modelos Biológicos
Estrutura Molecular
Carga Tumoral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Esters); EC 4.4.1.5 (Lactoylglutathione Lyase); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170627
[Lr] Data última revisão:
170627
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1248/cpb.c16-00800



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