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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


  2 / 3146 MEDLINE  
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[PMID]:27770613
[Au] Autor:Shukla-Dave A; Castillo-Martin M; Chen M; Lobo J; Gladoun N; Collazo-Lorduy A; Khan FM; Ponomarev V; Yi Z; Zhang W; Pandolfi PP; Hricak H; Cordon-Cardo C
[Ad] Endereço:Department of Medical Physics, Memorial Sloan Kettering Cancer Center, New York, New York; Department of Radiology, Memorial Sloan Kettering Cancer Center, New York, New York.
[Ti] Título:Ornithine Decarboxylase Is Sufficient for Prostate Tumorigenesis via Androgen Receptor Signaling.
[So] Source:Am J Pathol;186(12):3131-3145, 2016 Dec.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Increased polyamine synthesis is known to play an important role in prostate cancer. We aimed to explore its functional significance in prostate tumor initiation and its link to androgen receptor (AR) signaling. For this purpose, we generated a new cell line derived from normal epithelial prostate cells (RWPE-1) with overexpression of ornithine decarboxylase (ODC) and used it for in vitro and in vivo experiments. We then comprehensively analyzed the expression of the main metabolic enzymes of the polyamine pathway and spermine abundance in 120 well-characterized cases of human prostate cancer and high-grade prostate intraepithelial neoplasia (HGPIN). Herein, we show that the ODC-overexpressing prostate cells underwent malignant transformation, revealing that ODC is sufficient for de novo tumor initiation in 94% of injected mice. This oncogenic capacity was acquired through alteration of critical signaling networks, including AR, EIF2, and mTOR/MAPK. RNA silencing experiments revealed the link between AR signaling and polyamine metabolism. Human prostate cancers consistently demonstrated up-regulation of the main polyamine enzymes analyzed (ODC, polyamine oxidase, and spermine synthase) and reduction of spermine. This phenotype was also dominant in HGPIN, rendering it a new biomarker of malignant transformation. In summary, we report that ODC plays a key role in prostate tumorigenesis and that the polyamine pathway is altered as early as HGPIN.
[Mh] Termos MeSH primário: Ornitina Descarboxilase/metabolismo
Neoplasia Prostática Intraepitelial/enzimologia
Neoplasias da Próstata/enzimologia
Receptores Androgênicos/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Adulto
Idoso
Animais
Carcinogênese
Linhagem Celular
Estudos de Coortes
Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Masculino
Camundongos
Meia-Idade
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Poliaminas/metabolismo
Próstata/enzimologia
Próstata/patologia
Neoplasia Prostática Intraepitelial/etiologia
Neoplasia Prostática Intraepitelial/patologia
Neoplasias da Próstata/etiologia
Neoplasias da Próstata/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polyamines); 0 (Receptors, Androgen); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); EC 4.1.1.17 (Ornithine Decarboxylase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171202
[Lr] Data última revisão:
171202
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE


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[PMID]:28886181
[Au] Autor:Zahedi K; Barone S; Destefano-Shields C; Brooks M; Murray-Stewart T; Dunworth M; Li W; Doherty JR; Hall MA; Smith RD; Cleveland JL; Casero RA; Soleimani M
[Ad] Endereço:Departments of Medicine, University of Cincinnati College of Medicine, Cincinnati, OH, United States of America.
[Ti] Título:Activation of endoplasmic reticulum stress response by enhanced polyamine catabolism is important in the mediation of cisplatin-induced acute kidney injury.
[So] Source:PLoS One;12(9):e0184570, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cisplatin-induced nephrotoxicity limits its use in many cancer patients. The expression of enzymes involved in polyamine catabolism, spermidine/spermine N1-acetyltransferase (SSAT) and spermine oxidase (SMOX) increase in the kidneys of mice treated with cisplatin. We hypothesized that enhanced polyamine catabolism contributes to tissue damage in cisplatin acute kidney injury (AKI). Using gene knockout and chemical inhibitors, the role of polyamine catabolism in cisplatin AKI was examined. Deficiency of SSAT, SMOX or neutralization of the toxic products of polyamine degradation, H2O2 and aminopropanal, significantly diminished the severity of cisplatin AKI. In vitro studies demonstrated that the induction of SSAT and elevated polyamine catabolism in cells increases the phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) and enhances the expression of binding immunoglobulin protein BiP/GRP78) and CCAAT-enhancer-binding protein homologous protein (CHOP/GADD153). The increased expression of these endoplasmic reticulum stress response (ERSR) markers was accompanied by the activation of caspase-3. These results suggest that enhanced polyamine degradation in cisplatin AKI may lead to tubular damage through the induction of ERSR and the consequent onset of apoptosis. In support of the above, we show that the ablation of the SSAT or SMOX gene, as well as the neutralization of polyamine catabolism products modulate the onset of ERSR (e.g. lower BiP and CHOP) and apoptosis (e.g. reduced activated caspase-3). These studies indicate that enhanced polyamine catabolism and its toxic products are important mediators of ERSR and critical to the pathogenesis of cisplatin AKI.
[Mh] Termos MeSH primário: Lesão Renal Aguda/induzido quimicamente
Lesão Renal Aguda/metabolismo
Antineoplásicos/efeitos adversos
Cisplatino/efeitos adversos
Estresse do Retículo Endoplasmático
Poliaminas/metabolismo
[Mh] Termos MeSH secundário: Acetiltransferases/metabolismo
Lesão Renal Aguda/patologia
Animais
Apoptose/efeitos dos fármacos
Modelos Animais de Doenças
Testes de Função Renal
Redes e Vias Metabólicas
Camundongos
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Índice de Gravidade de Doença
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Polyamines); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.57 (diamine N-acetyltransferase); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184570


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[PMID]:28644554
[Au] Autor:Miller DV; Ruhlin M; Ray WK; Xu H; White RH
[Ad] Endereço:Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg, VA, USA.
[Ti] Título:N ,N -methylenetetrahydromethanopterin reductase from Methanocaldococcus jannaschii also serves as a methylglyoxal reductase.
[So] Source:FEBS Lett;591(15):2269-2278, 2017 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In Methanocaldococcus jannaschii, methylglyoxal (MG) is required for aromatic amino acid biosynthesis. Previously, the reduction of MG to lactaldehyde in Methanocaldococcus jannaschii cell extracts using either NADPH or F H was demonstrated; however, the enzyme responsible was not identified. Using NADPH as the reductant, the unknown enzyme was purified from cell extracts of Methanocaldococcus jannaschii and determined to be the F -dependent N ,N -methylenetetrahydromethanopterin reductase (Mer). Here, we report that the recombinantly overexpressed Mer is able to use NADPH and MG (K of 1.6 and 1.0 mm, respectively) to produce lactaldehyde. Additionally, Mer does not catalyze the reduction of MG to lactaldehyde in the presence of reduced Fo, the precursor of F .
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Methanocaldococcus/enzimologia
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
[Mh] Termos MeSH secundário: Aldeídos/metabolismo
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Clonagem Molecular
Escherichia coli/genética
Methanocaldococcus/metabolismo
NADP/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Aldeído Pirúvico/metabolismo
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Aldehydes); 0 (Archaeal Proteins); 0 (Recombinant Proteins); 53-59-8 (NADP); 598-35-6 (lactaldehyde); 722KLD7415 (Pyruvaldehyde); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.78 (D-lactaldehyde dehydrogenase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.99.- (methylenetetrahydromethanopterin dehydrogenase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12728


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[PMID]:28485817
[Au] Autor:Feng M; Ma Z; Crudup BF; Davidson VL
[Ad] Endereço:Department of Chemistry, Tougaloo College, MS, USA.
[Ti] Título:Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.
[So] Source:FEBS Lett;591(11):1566-1572, 2017 Jun.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The diheme enzyme MauG catalyzes oxidative post-translational modifications of a protein substrate, precursor protein of methylamine dehydrogenase (preMADH), that binds to the surface of MauG. The high-spin heme iron of MauG is located 40 Å from preMADH. The ferric heme is an equilibrium of five- and six-coordinate states. PreMADH binding increases the proportion of five-coordinate heme three-fold. On reaction of MauG with H O both hemes become Fe . In the absence of preMADH the hemes autoreduce to ferric in a multistep process involving multiple electron and proton transfers. Binding of preMADH in the absence of catalysis alters the mechanism of autoreduction of the ferryl heme. Thus, substrate binding alters the environment in the distal heme pocket of the high-spin heme over very long distance.
[Mh] Termos MeSH primário: Heme/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
[Mh] Termos MeSH secundário: Catálise
Heme/química
Peróxido de Hidrogênio/química
Peróxido de Hidrogênio/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/química
Paracoccus denitrificans/metabolismo
Ligação Proteica
Rhodobacter sphaeroides/metabolismo
Análise Espectral Raman
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
42VZT0U6YR (Heme); BBX060AN9V (Hydrogen Peroxide); EC 1.4.9.1 (methylamine dehydrogenase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170510
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12666


  6 / 3146 MEDLINE  
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[PMID]:28423064
[Au] Autor:Murray-Stewart T; Ferrari E; Xie Y; Yu F; Marton LJ; Oupicky D; Casero RA
[Ad] Endereço:The Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins University, Baltimore, Maryland, United States of America.
[Ti] Título:Biochemical evaluation of the anticancer potential of the polyamine-based nanocarrier Nano11047.
[So] Source:PLoS One;12(4):e0175917, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Synthesizing polycationic polymers directly from existing drugs overcomes the drug-loading limitations often associated with pharmacologically inert nanocarriers. We recently described nanocarriers formed from a first-generation polyamine analogue, bis(ethyl)norspermine (BENSpm), that could simultaneously target polyamine metabolism while delivering therapeutic nucleic acids. In the current study, we describe the synthesis and evaluation of self-immolative nanocarriers derived from the second-generation polyamine analogue PG-11047. Polyamines are absolutely essential for proliferation and their metabolism is frequently dysregulated in cancer. Through its effects on polyamine metabolism, PG-11047 effectively inhibits tumor growth in cancer cell lines of multiple origins as well as in human tumor mouse xenografts. Promising clinical trials have been completed verifying the safety and tolerance of this rotationally restricted polyamine analogue. We therefore used PG-11047 as the basis for Nano11047, a biodegradable, prodrug nanocarrier capable of targeting polyamine metabolism. Following exposure of lung cancer cell lines to Nano11047, uptake and intracellular degradation into the parent compound PG-11047 was observed. The release of PG-11047 highly induced the polyamine catabolic enzyme activities of spermidine/spermine N1-acetyltransferase (SSAT) and spermine oxidase (SMOX). By contrast, the activity of ornithine decarboxylase (ODC), a rate-limiting enzyme in polyamine biosynthesis and a putative oncogene, was decreased. Consequently, intracellular levels of the natural polyamines were depleted concurrent with tumor cell growth inhibition. This availability of Nano11047 as a novel drug form and potential nucleic acid delivery vector will potentially benefit and encourage future clinical studies.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Portadores de Fármacos
Regulação Neoplásica da Expressão Gênica
Ornitina Descarboxilase/genética
Pró-Fármacos/farmacologia
Espermina/análogos & derivados
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Acetiltransferases/metabolismo
Antineoplásicos/síntese química
Biotransformação
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Nanoestruturas/química
Ornitina Descarboxilase/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Poliaminas/antagonistas & inibidores
Poliaminas/metabolismo
Pró-Fármacos/síntese química
Pró-Fármacos/metabolismo
Mucosa Respiratória/efeitos dos fármacos
Mucosa Respiratória/metabolismo
Mucosa Respiratória/patologia
Espermina/síntese química
Espermina/metabolismo
Espermina/farmacologia
Carga Tumoral/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 ((N(1),N(12))bis(ethyl)-6,7-dehydrospermine); 0 (Antineoplastic Agents); 0 (Drug Carriers); 0 (Polyamines); 0 (Prodrugs); 2FZ7Y3VOQX (Spermine); BBX060AN9V (Hydrogen Peroxide); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.57 (diamine N-acetyltransferase); EC 4.1.1.17 (Ornithine Decarboxylase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170518
[Lr] Data última revisão:
170518
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0175917


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[PMID]:28259896
[Au] Autor:Konno M; Asai A; Kawamoto K; Nishida N; Satoh T; Doki Y; Mori M; Ishii H
[Ad] Endereço:Department of Frontier Science for Cancer and Chemotherapy, Osaka University, Osaka 565-0871, Japan.
[Ti] Título:The one-carbon metabolism pathway highlights therapeutic targets for gastrointestinal cancer (Review).
[So] Source:Int J Oncol;50(4):1057-1063, 2017 Apr.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:After the initial use of anti-folates for treatment of malignancies, folate metabolism has emerged as a rational diagnostic and therapeutic target in gastrointestinal cancer. The one-carbon metabolic pathway, which comprises three critical reactions (i.e., folate and methionine cycles), underlies this effect in conjunction with the trans-sulfuration pathway. Understanding of the one-carbon metabolism pathway has served to unravel the link between the causes and effects of cancer phenotypes leading to several seminal discoveries such as that of diadenosine tri-phosphate hydrolase, microRNAs, 5-FU and, more recently, trifluridine. In the folate cycle, glycine and serine fuel the mitochondrial enzymes SHMT2, MTHFD2 and ALDH1L2, which play critical roles in the cancer survival and proliferation presumably through purine production. In the methionine cycle, S-adenocyl methionine serves hydrocarbons and polyamines that are critical for the epigenetic controls. The trans-sulfuration pathway is a critical component in the synthesis of glutathione, which is involved in the production of reactive oxygen species in cancer stem cells. Therefore, characterization of one-carbon metabolism is indispensable to the development of precision medicine in the context of cancer diagnostics and therapeutics. In the present study, we review the historical issues associated with one-carbon metabolism and highlight the recent advances in cancer research.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Ácido Fólico/metabolismo
Neoplasias Gastrointestinais/metabolismo
Redes e Vias Metabólicas/efeitos dos fármacos
Metionina/metabolismo
Mitocôndrias/metabolismo
Terapia de Alvo Molecular/métodos
[Mh] Termos MeSH secundário: Aminoidrolases/metabolismo
Fluoruracila/metabolismo
Antagonistas do Ácido Fólico/uso terapêutico
Neoplasias Gastrointestinais/tratamento farmacológico
Glicina Hidroximetiltransferase/metabolismo
Seres Humanos
Metaboloma
Metilenotetra-Hidrofolato Desidrogenase (NADP)/metabolismo
MicroRNAs/metabolismo
Mitocôndrias/enzimologia
Complexos Multienzimáticos/metabolismo
Nucleosídeos/uso terapêutico
Nucleotídeos/uso terapêutico
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Purinas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Serina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Folic Acid Antagonists); 0 (MicroRNAs); 0 (Multienzyme Complexes); 0 (Nucleosides); 0 (Nucleotides); 0 (Purines); 0 (Reactive Oxygen Species); 0 (methylene tetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase); 452VLY9402 (Serine); 935E97BOY8 (Folic Acid); AE28F7PNPL (Methionine); EC 1.5.- (ALDH1L2 protein, human); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.1.5 (Methylenetetrahydrofolate Dehydrogenase (NADP)); EC 2.1.2.1 (Glycine Hydroxymethyltransferase); EC 2.1.2.1 (SHMT protein, human); EC 3.5.4.- (Aminohydrolases); U3P01618RT (Fluorouracil); W60KTZ3IZY (purine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170717
[Lr] Data última revisão:
170717
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170306
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3885


  8 / 3146 MEDLINE  
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[PMID]:28205250
[Au] Autor:Okai M; Lee WC; Guan LJ; Ohshiro T; Izumi Y; Tanokura M
[Ad] Endereço:Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.
[Ti] Título:Crystal structure of dibenzothiophene sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B.
[So] Source:Proteins;85(6):1171-1177, 2017 Jun.
[Is] ISSN:1097-0134
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The dibenzothiophene (DBT) sulfone monooxygenase BdsA from Bacillus subtilis WU-S2B catalyzes the conversion of DBT sulfone to 2'-hydroxybiphenyl 2-sulfinate. We report the crystal structures of BdsA at a resolution of 2.80 Å. BdsA exists as a homotetramer with a dimer-of-dimers configuration in the crystal, and the interaction between E288 and R296 in BdsA is important for tetramer formation. A structural comparison with homologous proteins shows that the orientation and location of the α9-α12 helices in BdsA are closer to those of the closed form than those of the open form in the EDTA monooxygenase EmoA. Proteins 2017; 85:1171-1177. © 2017 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Bacillus subtilis/química
Proteínas de Bactérias/química
Compostos de Bifenilo/química
Oxigenases/química
Subunidades Proteicas/química
Tiofenos/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arginina/química
Arginina/metabolismo
Bacillus subtilis/enzimologia
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Compostos de Bifenilo/metabolismo
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Ácido Glutâmico/química
Ácido Glutâmico/metabolismo
Modelos Moleculares
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/química
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Oxigenases/genética
Oxigenases/metabolismo
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia Estrutural de Proteína
Especificidade por Substrato
Tiofenos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Biphenyl Compounds); 0 (Protein Subunits); 0 (Recombinant Proteins); 0 (Thiophenes); 1013-23-6 (dibenzothiophene 5-oxide); 3KX376GY7L (Glutamic Acid); 94ZLA3W45F (Arginine); D343Z75HT8 (2-phenylphenol); EC 1.13.- (Oxygenases); EC 1.14.99.- (dibenzothiophene sulfone monooxygenase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.7.- (EDTA monooxygenase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1002/prot.25267


  9 / 3146 MEDLINE  
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[PMID]:28135604
[Au] Autor:Gémes K; Mellidou Ι; Karamanoli K; Beris D; Park KY; Matsi T; Haralampidis K; Constantinidou HI; Roubelakis-Angelakis KA
[Ad] Endereço:Department of Biology, University of Crete, Voutes University Campus, 70013 Heraklion, Greece; Biological Research Centre, Hungarian Academy of Sciences, H-6726 Szeged, Temesvari krt. 62, Hungary.
[Ti] Título:Deregulation of apoplastic polyamine oxidase affects development and salt response of tobacco plants.
[So] Source:J Plant Physiol;211:1-12, 2017 Apr.
[Is] ISSN:1618-1328
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Polyamine (PA) homeostasis is associated with plant development, growth and responses to biotic/abiotic stresses. Apoplastic PA oxidase (PAO) catalyzes the oxidation of PAs contributing to cellular homeostasis of reactive oxygen species (ROS) and PAs. In tobacco, PAs decrease with plant age, while apoplastic PAO activity increases. Our previous results with young transgenic tobacco plants with enhanced/reduced apoplastic PAO activity (S-ZmPAO/AS-ZmPAO, respectively) established the importance of apoplastic PAO in controlling tolerance to short-term salt stress. However, it remains unclear if the apoplastic PAO pathway is important for salt tolerance at later stages of plant development. In this work, we examined whether apoplastic PAO controls also plant development and tolerance of adult plants during long-term salt stress. The AS-ZmPAO plants contained higher Ca during salt stress, showing also reduced chlorophyll content index (CCI), leaf area and biomass but taller phenotype compared to the wild-type plants during salt. On the contrary, the S-ZmPAO had more leaves with slightly greater size compared to the AS-ZmPAO and higher antioxidant genes/enzyme activities. Accumulation of proline in the roots was evident at prolonged stress and correlated negatively with PAO deregulation as did the transcripts of genes mediating ethylene biosynthesis. In contrast to the strong effect of apoplastic PAO to salt tolerance in young plants described previously, the effect it exerts at later stages of development is rather moderate. However, the different phenotypes observed in plants deregulating PAO reinforce the view that apoplastic PAO exerts multifaceted roles on plant growth and stress responses. Our data suggest that deregulation of the apoplastic PAO can be further examined as a potential approach to breed plants with enhanced/reduced tolerance to abiotic stress with minimal associated trade-offs.
[Mh] Termos MeSH primário: Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Cloreto de Sódio/farmacologia
Tabaco/crescimento & desenvolvimento
Tabaco/fisiologia
Zea mays/enzimologia
[Mh] Termos MeSH secundário: Ascorbato Peroxidases/metabolismo
Biomassa
Vias Biossintéticas/efeitos dos fármacos
Vias Biossintéticas/genética
Catalase/metabolismo
Eletrólitos/metabolismo
Etilenos/biossíntese
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Genes de Plantas
Homeostase/efeitos dos fármacos
Íons
Fenóis/análise
Fenótipo
Fotossíntese/efeitos dos fármacos
Folhas de Planta/efeitos dos fármacos
Folhas de Planta/metabolismo
Raízes de Plantas/efeitos dos fármacos
Raízes de Plantas/metabolismo
Plantas Geneticamente Modificadas
Prolina/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Estresse Fisiológico/efeitos dos fármacos
Estresse Fisiológico/genética
Superóxido Dismutase/metabolismo
Tabaco/efeitos dos fármacos
Tabaco/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Electrolytes); 0 (Ethylenes); 0 (Ions); 0 (Phenols); 0 (RNA, Messenger); 0 (Reactive Oxygen Species); 451W47IQ8X (Sodium Chloride); 91GW059KN7 (ethylene); 9DLQ4CIU6V (Proline); EC 1.11.1.11 (Ascorbate Peroxidases); EC 1.11.1.6 (Catalase); EC 1.15.1.1 (Superoxide Dismutase); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE


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[PMID]:28082202
[Au] Autor:Smirnova OA; Keinanen TA; Ivanova ON; Hyvonen MT; Khomutov AR; Kochetkov SN; Bartosch B; Ivanov AV
[Ad] Endereço:Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
[Ti] Título:Hepatitis C virus alters metabolism of biogenic polyamines by affecting expression of key enzymes of their metabolism.
[So] Source:Biochem Biophys Res Commun;483(2):904-909, 2017 Feb 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Chronic infection with hepatitis C virus (HCV) induces liver fibrosis and cancer. In particular metabolic alterations and associated oxidative stress induced by the virus play a key role in disease progression. Albeit the pivotal role of biogenic polyamines spermine and spermidine in the regulation of liver metabolism and function and cellular control of redox homeostasis, their role in the viral life cycle has not been studied so far. Here we show that in cell lines expressing two viral proteins, capsid and the non-structural protein 5A, expression of the two key enzymes of polyamine biosynthesis and degradation, respectively, ornithine decarboxylase (ODC) and spermidine/spermine-N1-acetyl transferase (SSAT), increases transiently. In addition, both HCV core and NS5A induce sustained expression of spermine oxidase (SMO), an enzyme that catalyzes conversion of spermine into spermidine. Human hepatoma Huh7 cells harboring a full-length HCV replicon exhibited suppressed ODC and SSAT levels and elevated levels of SMO leading to decreased intracellular concentrations of spermine and spermidine. Thus, role of HCV-driven alterations of polyamine metabolism in virus replication and development of HCV-associated liver pathologies should be explored in future.
[Mh] Termos MeSH primário: Poliaminas Biogênicas/metabolismo
Hepacivirus/fisiologia
Hepacivirus/patogenicidade
[Mh] Termos MeSH secundário: Acetiltransferases/genética
Acetiltransferases/metabolismo
Linhagem Celular
Regulação Enzimológica da Expressão Gênica
Hepacivirus/genética
Interações Hospedeiro-Patógeno/genética
Interações Hospedeiro-Patógeno/fisiologia
Seres Humanos
Ornitina Descarboxilase/genética
Ornitina Descarboxilase/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/genética
Oxirredutases atuantes sobre Doadores de Grupo CH-NH/metabolismo
Espermidina/metabolismo
Espermina/metabolismo
Proteínas do Core Viral/fisiologia
Proteínas não Estruturais Virais/fisiologia
Replicação Viral/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biogenic Polyamines); 0 (NS-5 protein, hepatitis C virus); 0 (Viral Core Proteins); 0 (Viral Nonstructural Proteins); 2FZ7Y3VOQX (Spermine); EC 1.5.- (Oxidoreductases Acting on CH-NH Group Donors); EC 1.5.3.- (polyamine oxidase); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.57 (diamine N-acetyltransferase); EC 4.1.1.17 (Ornithine Decarboxylase); U87FK77H25 (Spermidine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE



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