Base de dados : MEDLINE
Pesquisa : D02.886.030.230 [Categoria DeCS]
Referências encontradas : 33264 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 3327 ir para página                         

  1 / 33264 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28463568
[Au] Autor:Salinas G; Gao W; Wang Y; Bonilla M; Yu L; Novikov A; Virginio VG; Ferreira HB; Vieites M; Gladyshev VN; Gambino D; Dai S
[Ad] Endereço:1 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .
[Ti] Título:The Enzymatic and Structural Basis for Inhibition of Echinococcus granulosus Thioredoxin Glutathione Reductase by Gold(I).
[So] Source:Antioxid Redox Signal;27(18):1491-1504, 2017 Dec 20.
[Is] ISSN:1557-7716
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIMS: New drugs are needed to treat flatworm infections that cause severe human diseases such as schistosomiasis. The unique flatworm enzyme thioredoxin glutathione reductase (TGR), structurally different from the human enzyme, is a key drug target. Structural studies of the flatworm Echinococcus granulosus TGR, free and complexed with Au -MPO, a novel gold inhibitor, together with inhibition assays were performed. RESULTS: Au -MPO is a potent TGR inhibitor that achieves 75% inhibition at a 1:1 TGR:Au ratio and efficiently kills E. granulosus in vitro. The structures revealed salient insights: (i) unique monomer-monomer interactions, (ii) distinct binding sites for thioredoxin and the glutaredoxin (Grx) domain, (iii) a single glutathione disulfide reduction site in the Grx domain, (iv) rotation of the Grx domain toward the Sec-containing redox active site, and (v) a single gold atom bound to Cys and Cys in the Au -TGR complex. Structural modeling suggests that these residues are involved in the stabilization of the Sec-containing C-terminus. Consistently, Cys→Ser mutations in these residues decreased TGR activities. Mass spectroscopy confirmed these cysteines are the primary binding site. INNOVATION: The identification of a primary site for gold binding and the structural model provide a basis for gold compound optimization through scaffold adjustments. CONCLUSIONS: The structural study revealed that TGR functions are achieved not only through a mobile Sec-containing redox center but also by rotation of the Grx domain and distinct binding sites for Grx domain and thioredoxin. The conserved Cys and Cys residues targeted by gold assist catalysis through stabilization of the Sec-containing redox center. Antioxid. Redox Signal. 27, 1491-1504.
[Mh] Termos MeSH primário: Echinococcus granulosus/enzimologia
Complexos Multienzimáticos/química
Complexos Multienzimáticos/metabolismo
NADH NADPH Oxirredutases/química
NADH NADPH Oxirredutases/metabolismo
Compostos Organoáuricos/farmacologia
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/efeitos dos fármacos
Cisteína/metabolismo
Echinococcus granulosus/química
Echinococcus granulosus/genética
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacocinética
Glutarredoxinas/metabolismo
Proteínas de Helminto/química
Proteínas de Helminto/genética
Proteínas de Helminto/metabolismo
Modelos Moleculares
Complexos Multienzimáticos/genética
Mutação
NADH NADPH Oxirredutases/genética
Compostos Organoáuricos/química
Ligação Proteica
Conformação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Glutaredoxins); 0 (Helminth Proteins); 0 (Multienzyme Complexes); 0 (Organogold Compounds); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.4.- (thioredoxin glutathione reductase); K848JZ4886 (Cysteine)
[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:170503
[St] Status:MEDLINE
[do] DOI:10.1089/ars.2016.6816


  2 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28454695
[Au] Autor:Hu TX; Guo X; Wang G; Gao L; He P; Xia Y; Gu H; Ni X
[Ad] Endereço:Department of Physiology, Second Military Medical University, Shanghai, China; No.117 Hospital of PLA, Hangzhou, China.
[Ti] Título:MiR133b is involved in endogenous hydrogen sulfide suppression of sFlt-1 production in human placenta.
[So] Source:Placenta;52:33-40, 2017 Apr.
[Is] ISSN:1532-3102
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Increased production of soluble fms-like tyrosine kinase-1 (sFlt-1) from placenta is one of the major contributors to the development of preeclampsia. Our previous study has shown that hydrogen sulfide (H S) inhibits sFlt-1 release in placenta. In the present study, we sought to investigate whether endogenous H S affects sFlt-1 production and elucidate which H S-producing enzyme is responsible for its effect in placenta. It was found that, besides cystathionine ß-synthase (CBS) and cystathionine γ-lyase (CSE), 3-mercaptopyruvatesulfurtransferase (3-MST) was identified in human placenta and mainly localized in syncytiotrophoblasts. There was no significant difference in expression level of 3-MST among preeclamptic and normal placentas. Treatment of cultured syncytiotrophoblasts with NaHS and l-cysteine suppressed sFlt-1 mRNA expression and caused a decrease in sFlt-1 protein content in culture media of the cells. Transfection of syncytiotrophoblasts with CBS siRNA and CSE siRNA reversed the above effects of l-cysteine. Furthermore, NaHS and l-cysteine treatment decreased the half-life of sFlt-1 mRNA and increased the expression of miR-133b targeting sFlt-1. MiR-133b expression was downregulated in preeclamptic placentas and correlated with the level of CBS and CSE. These results indicate that H S is an important regulatory factor in sFlt-1 production in placenta. Reduced H S generation in placenta contributes to development of preeclampsia by enhancing sFlt-1 production.
[Mh] Termos MeSH primário: Sulfeto de Hidrogênio/metabolismo
MicroRNAs/metabolismo
Placenta/metabolismo
Receptor 1 de Fatores de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Células Cultivadas
Cistationina beta-Sintase/metabolismo
Cistationina gama-Liase/metabolismo
Cisteína/farmacologia
Regulação para Baixo
Feminino
Seres Humanos
Sulfeto de Hidrogênio/farmacologia
Gravidez
Sulfurtransferases/metabolismo
Trofoblastos/efeitos dos fármacos
Trofoblastos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN133 microRNA, human); 0 (MicroRNAs); EC 2.7.10.1 (FLT1 protein, human); EC 2.7.10.1 (Vascular Endothelial Growth Factor Receptor-1); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); EC 4.2.1.22 (Cystathionine beta-Synthase); EC 4.4.1.1 (Cystathionine gamma-Lyase); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE


  3 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28746421
[Au] Autor:Sadowska-Bartosz I; Furmaniak P; Bieszczad-Bedrejczuk E; Bartosz G; Glowacki R
[Ad] Endereço:Department of Analytical Biochemistry, Faculty of Biology and Agriculture, University of Rzeszow, Rzeszów, Poland.
[Ti] Título:Developmental changes in the levels and redox potentials of main hemolymph thiols/disulfides in the Jamaican field cricket Gryllus assimilis.
[So] Source:Acta Biochim Pol;64(3):503-506, 2017.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Main thiols and disulfides were determined in the hemolymph of the Jamaican field cricket Gryllus assimilis at various developmental stages. On the basis of these data, redox potentials of the glutathione, cysteine and homocysteine redox systems were calculated. The concentrations of all thiols studied decreased during development (at a stage of 6 molts) with respect to young crickets, and increased again in adult insects. Redox potentials of the glutathione and cysteine systems increased from values of -131.0±5.6 mV and -86.9±17.1 mV, respectively in young crickets to -58.0±3.6 mV and -36.1±4.2 mV, respectively, at the stage of 6 molts and decreased to values of -110.4±24.8 mV and -66.3±12.2 mV, respectively, in adult insects. Redox potentials of the glutathione and cysteine systems in the hemolymph of young and adult insects were similar to those reported for human plasma.
[Mh] Termos MeSH primário: Dissulfetos/metabolismo
Gryllidae/crescimento & desenvolvimento
Gryllidae/metabolismo
Hemolinfa/metabolismo
Compostos de Sulfidrila/metabolismo
[Mh] Termos MeSH secundário: Animais
Cisteína/metabolismo
Glutationa/metabolismo
Dissulfeto de Glutationa/metabolismo
Homocisteína/metabolismo
Ninfa/crescimento & desenvolvimento
Ninfa/metabolismo
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Disulfides); 0 (Sulfhydryl Compounds); 0LVT1QZ0BA (Homocysteine); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); ULW86O013H (Glutathione Disulfide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2017_1510


  4 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29317652
[Au] Autor:Santos-Barriopedro I; Bosch-Presegué L; Marazuela-Duque A; de la Torre C; Colomer C; Vazquez BN; Fuhrmann T; Martínez-Pastor B; Lu W; Braun T; Bober E; Jenuwein T; Serrano L; Esteller M; Chen Z; Barceló-Batllori S; Mostoslavsky R; Espinosa L; Vaquero A
[Ad] Endereço:Chromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Bellvitge Biomedical Research Institute (IDIBELL), Av. Gran Via de l'Hospitalet 199-203, 08908, L'Hospitalet de Llobregat (Barcelona), Spain.
[Ti] Título:SIRT6-dependent cysteine monoubiquitination in the PRE-SET domain of Suv39h1 regulates the NF-κB pathway.
[So] Source:Nat Commun;9(1):101, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sirtuins are NAD -dependent deacetylases that facilitate cellular stress response. They include SirT6, which protects genome stability and regulates metabolic homeostasis through gene silencing, and whose loss induces an accelerated aging phenotype directly linked to hyperactivation of the NF-κB pathway. Here we show that SirT6 binds to the H3K9me3-specific histone methyltransferase Suv39h1 and induces monoubiquitination of conserved cysteines in the PRE-SET domain of Suv39h1. Following activation of NF-κB signaling Suv39h1 is released from the IκBα locus, subsequently repressing the NF-κB pathway. We propose that SirT6 attenuates the NF-κB pathway through IκBα upregulation via cysteine monoubiquitination and chromatin eviction of Suv39h1. We suggest a mechanism based on SirT6-mediated enhancement of a negative feedback loop that restricts the NF-κB pathway.
[Mh] Termos MeSH primário: Cisteína/metabolismo
Metiltransferases/metabolismo
NF-kappa B/metabolismo
Domínios PR-SET
Proteínas Repressoras/metabolismo
Sirtuínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Cultivadas
Cromatina/metabolismo
Cisteína/genética
Células HCT116
Células HEK293
Células HeLa
Seres Humanos
Metiltransferases/genética
Camundongos
Inibidor de NF-kappaB alfa/metabolismo
Células NIH 3T3
Ligação Proteica
Proteínas Repressoras/genética
Transdução de Sinais
Sirtuínas/genética
Ubiquitinação
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Chromatin); 0 (NF-kappa B); 0 (Repressor Proteins); 139874-52-5 (NF-KappaB Inhibitor alpha); EC 2.1.1. (SUV39H1 protein, human); EC 2.1.1.- (Methyltransferases); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins); K848JZ4886 (Cysteine)
[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:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02586-x


  5 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29301400
[Au] Autor:Clark AC; Deed RC
[Ad] Endereço:School of Agricultural and Wine Sciences, Charles Sturt University , Locked Bag 588, Wagga Wagga, New South Wales 2678, Australia.
[Ti] Título:The Chemical Reaction of Glutathione and trans-2-Hexenal in Grape Juice Media To Form Wine Aroma Precursors: The Impact of pH, Temperature, and Sulfur Dioxide.
[So] Source:J Agric Food Chem;66(5):1214-1221, 2018 Feb 07.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aldehyde 3-S-glutathionylhexanal is an intermediate which is produced during the formation of the wine aroma precursor 3-S-glutathionylhexanol, after the reaction of glutathione with trans-2-hexenal. This study was conducted to assess whether the chemical, as opposed to the enzymatic, production of 3-S-glutathionylhexanal could occur at a significant rate in grape juice. LC-MS/MS was used in low- and high-resolution modes, in combination with functional group derivatization, to identify and quantitate products. In comparison to cysteine, glutathione was found to induce less cyclized products on reaction with trans-2-alkanals and the glutathione-derived products were more reactive to hydrogen sulfite. The zero-order rates for 3-S-glutathionylhexanal formation in model grape juice were 1.08 ± 0.08 and 0.45 ± 0.05 mg/(L·day) glutathione equivalents at 25 and 13 °C, respectively, and the reaction rate increased 3-fold by increasing the pH from 3.2 to 3.8. 3-S-Glutathionylhexanal was detected in all five white grape juices examined. The concentration of the aldehyde could be increased by up to 10-fold after being released from hydrogen sulfite, demonstrating a potentially novel source for the production of varietal thiol aroma compounds in wine.
[Mh] Termos MeSH primário: Aldeídos/síntese química
Glutationa/química
Dióxido de Enxofre/química
Vitis/química
[Mh] Termos MeSH secundário: Aldeídos/química
Cisteína/química
Frutas/química
Sucos de Frutas e Vegetais
Concentração de Íons de Hidrogênio
Cinética
Olfato
Temperatura Ambiente
Vinho
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aldehydes); 0UZA3422Q4 (Sulfur Dioxide); 505-57-7 (2-hexenal); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine)
[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:180106
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b04991


  6 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28743765
[Au] Autor:Kurmanbayeva A; Bekturova A; Srivastava S; Soltabayeva A; Asatryan A; Ventura Y; Khan MS; Salazar O; Fedoroff N; Sagi M
[Ad] Endereço:Plant Stress Laboratory, French Associates Institute for Agriculture and Biotechnology of Drylands, Blaustein Institutes for Desert Research, Ben-Gurion University of the Negev, 84990, Israel.
[Ti] Título:Higher Novel L-Cys Degradation Activity Results in Lower Organic-S and Biomass in than the Related Saltwort, .
[So] Source:Plant Physiol;175(1):272-289, 2017 Sep.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:and are almost identical halophytes whose edible succulent shoots hold promise for commercial production in saline water. Enhanced sulfur nutrition may be beneficial to crops naturally grown on high sulfate. However, little is known about sulfate nutrition in halophytes. Here we show that (ecotype RN) exhibits a significant increase in biomass and organic-S accumulation in response to supplemental sulfate, whereas (ecotype VM) does not, instead exhibiting increased sulfate accumulation. We investigated the role of two pathways on organic-S and biomass accumulation in and : the sulfate reductive pathway that generates Cys and l-Cys desulfhydrase that degrades Cys to H S, NH , and pyruvate. The major function of -acetyl-Ser-(thiol) lyase (OAS-TL; EC 2.5.1.47) is the formation of l-Cys, but our study shows that the OAS-TL A and OAS-TL B of both halophytes are enzymes that also degrade l-Cys to H S. This activity was significantly higher in than in , especially upon sulfate supplementation. The activity of the sulfate reductive pathway key enzyme, adenosine 5'-phosphosulfate reductase (APR, EC 1.8.99.2), was significantly higher in than in These results suggest that the low organic-S level in is the result of high l-Cys degradation rate by OAS-TLs, whereas the greater organic-S and biomass accumulation in is the result of higher APR activity and low l-Cys degradation rate, resulting in higher net Cys biosynthesis. These results present an initial road map for halophyte growers to attain better growth rates and nutritional value of and .
[Mh] Termos MeSH primário: Amaranthaceae/metabolismo
Chenopodiaceae/metabolismo
Cisteína/metabolismo
Proteínas de Plantas/metabolismo
Salsola/metabolismo
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Amaranthaceae/efeitos dos fármacos
Biomassa
Chenopodiaceae/efeitos dos fármacos
Cisteína Sintase/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Salinidade
Salsola/efeitos dos fármacos
Plantas Tolerantes a Sal
Sódio/farmacologia
Sulfatos/farmacologia
Compostos de Sulfidrila/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Sulfates); 0 (Sulfhydryl Compounds); 70FD1KFU70 (Sulfur); 9NEZ333N27 (Sodium); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.99.2 (adenylylsulfate reductase); EC 2.5.1.47 (Cysteine Synthase); K848JZ4886 (Cysteine)
[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:170727
[St] Status:MEDLINE
[do] DOI:10.1104/pp.17.00780


  7 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29223921
[Au] Autor:Zhou B; Ye J; Yang N; Chen L; Zhuo Z; Mao L; Liu Q; Lan G; Ning J; Ge G; Yang L; Shen Y; Wang S; Zhang W
[Ad] Endereço:School of Traditional Chinese Medicine, Guangdong Pharmaceutical University, Guangzhou, China.
[Ti] Título:Metabolism and pharmacokinetics of alantolactone and isoalantolactone in rats: Thiol conjugation as a potential metabolic pathway.
[So] Source:J Chromatogr B Analyt Technol Biomed Life Sci;1072:370-378, 2018 Jan 01.
[Is] ISSN:1873-376X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Alantolactone (AL) and isoalantolactone (IAL), two major active sesquiterpene lactones isolated from Radix Inulae extract, have a wide range of pharmacological activities. The predominant metabolic pathway of AL and IAL observed was glutathione (GSH) conjugation in vitro, which could occur in the absence of metabolic enzymes. Non-enzymatic conjugation with cysteine (Cys) couldalso be observed. Four metabolites (AL-GSH, AL-Cys, IAL-GSH, IAL-Cys) were subsequently isolated and confirmed by nuclear magnetic resonance (NMR). The results indicated that the thiol of GSH or Cys can be reacted with the exomethylene carbon atoms of α, ß-unsaturated carbonyl of AL and IAL. After intravenous administration in rats, AL and IAL were extensively metabolized, and the exposure, as measured by area under the concentration-time curve (AUC), for AL-GSH, AL-Cys, IAL-GSH, and IAL-Cys was approximately 1.54-, 0.96-, 1.50-, and 0.91-fold that of the parent drug, respectively. The AUC ratio of metabolites to parent compounds of oral administration was 3.66-, 9.19-, 12.97-, and 9.92-fold that of the parent drug for the above metabolites, respectively. The bioavailability of AL-total (AL, AL-GSH, AL-Cys) and IAL-total (IAL, IAL-GSH, IAL-Cys) was, respectively, 8.39% and 13.07%, which was 3.62- and 6.95- fold that of AL (2.32%) and IAL (1.88%), respectively. The oral exposure will be underestimated if the parent drugs are tested alone. These findings provide useful information for preclinical safety evaluation, and for predicting AL and IAL metabolism in humans.
[Mh] Termos MeSH primário: Lactonas
Sesquiterpenos de Eudesmano
Sesquiterpenos
Compostos de Sulfidrila/metabolismo
[Mh] Termos MeSH secundário: Animais
Cromatografia Líquida
Cisteína/metabolismo
Glutationa/metabolismo
Seres Humanos
Lactonas/análise
Lactonas/química
Lactonas/metabolismo
Lactonas/farmacocinética
Masculino
Microssomos Hepáticos/metabolismo
Ratos
Ratos Sprague-Dawley
Sesquiterpenos/análise
Sesquiterpenos/química
Sesquiterpenos/metabolismo
Sesquiterpenos/farmacocinética
Sesquiterpenos de Eudesmano/análise
Sesquiterpenos de Eudesmano/química
Sesquiterpenos de Eudesmano/metabolismo
Sesquiterpenos de Eudesmano/farmacocinética
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lactones); 0 (Sesquiterpenes); 0 (Sesquiterpenes, Eudesmane); 0 (Sulfhydryl Compounds); BYH07P620U (isoalantolactone); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); M7GSN5Q1M6 (alantolactone)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE


  8 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28462529
[Au] Autor:Dixon SJ
[Ad] Endereço:Department of Biology, Stanford University, Stanford, CA, USA.
[Ti] Título:Ferroptosis: bug or feature?
[So] Source:Immunol Rev;277(1):150-157, 2017 05.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ferroptosis is an iron-dependent, oxidative form of non-apoptotic cell death. This form of cell death does not share morphological, biochemical, or genetic similarities with classic necrosis, necroptosis, parthanatos, or other forms of non-apoptotic cell death. Ferroptosis can be triggered by depleting the cell of the amino acid cysteine, or by inhibiting the phospholipid hydroperoxidase glutathione peroxidase 4 (GPX4). Why certain stimuli trigger ferroptosis instead of another form of cell death, and whether this process could be adaptive in vivo, are two major unanswered questions concerning this process. Emerging evidence and consideration of related non-apoptotic pathways suggest that ferroptosis could be an adaptive process, albeit one regulated and executed in a manner very different from apoptosis and other forms of cell death.
[Mh] Termos MeSH primário: Morte Celular
Glutationa Peroxidase/metabolismo
Ferro/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Cisteína/metabolismo
Seres Humanos
Necrose
Oxirredução
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Reactive Oxygen Species); E1UOL152H7 (Iron); EC 1.11.1.12 (phospholipid-hydroperoxide glutathione peroxidase); EC 1.11.1.9 (Glutathione Peroxidase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12533


  9 / 33264 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29331374
[Au] Autor:Nagahara N; Koike S; Nirasawa T; Kimura H; Ogasawara Y
[Ad] Endereço:Isotope Research Center, Nippon Medical School, Japan. Electronic address: noriyuki@nms.ac.jp.
[Ti] Título:Alternative pathway of H S and polysulfides production from sulfurated catalytic-cysteine of reaction intermediates of 3-mercaptopyruvate sulfurtransferase.
[So] Source:Biochem Biophys Res Commun;496(2):648-653, 2018 02 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It has been known that hydrogen sulfide and/or polysulfides are produced from a (poly)sulfurated sulfur-acceptor substrate of 3-mercaptopyruvate sulfurtransferase (MST) via thioredoxin (Trx) reduction in vitro. In this study, we used thiosulfate as the donor substrate and the catalytic reaction was terminated on the formation of a persulfide or polysulfides. We can present alternative pathway of production of hydrogen sulfide and/or polysulfides from (poly)sulfurated catalytic-site cysteine of reaction intermediates of MST via Trx reduction. Matrix-assisted laser desorption ionization tandem time-of-flight mass spectrometric analysis revealed that after prolonged incubation of MST with thiosulfate, a trisulfide adduct becomes predominant at the sulfurated catalytic-site cysteine. When these adducts were reduced by Trx with reducing system (MST:Escherichia coli Trx:E. coli Trx reductase:NADPH = 1:5:0.02:12.5 molar ratio), liquid chromatography with tandem mass spectrometric analysis for monobromobimane-derivatized H S revealed that H S first appeared, and then H S and H S did later. The results were confirmed by high-performance liquid chromatography-fluorescence analysis.
[Mh] Termos MeSH primário: Cisteína/metabolismo
Sulfeto de Hidrogênio/metabolismo
Sulfetos/metabolismo
Sulfurtransferases/metabolismo
[Mh] Termos MeSH secundário: Animais
Escherichia coli/metabolismo
Proteínas de Escherichia coli/metabolismo
Oxirredução
Ratos
Proteínas Recombinantes/metabolismo
Tiorredoxina Dissulfeto Redutase/metabolismo
Tiorredoxinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 0 (Sulfides); 52500-60-4 (Thioredoxins); 9080-49-3 (polysulfide); EC 1.8.1.9 (Thioredoxin-Disulfide Reductase); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.2 (3-mercaptopyruvate sulphurtransferase); K848JZ4886 (Cysteine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180115
[St] Status:MEDLINE


  10 / 33264 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29317320
[Au] Autor:Feng Y; Feng J; Zheng H; Wang W; Chen F; Yu Y; Cui J
[Ad] Endereço:Lab of Tissue Engineering, College of Life Sciences, Northwest University, Xi'an 710069, PR China.
[Ti] Título:Molecular cloning, characterization, and expression analysis of the three cysteine and glycine-rich protein genes in the Chinese fire-bellied newt Cynops orientalis.
[So] Source:Gene;647:226-234, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The cysteine- and glycine-rich protein (CRP) family members, including the cysteine- and glycine-rich protein 1 (CSRP1), cysteine- and glycine-rich protein 2 (CSRP2), and the cysteine- and glycine-rich protein 3 (CSRP3), have exhibited various cellular functions during cell development and differentiation. However, the sequences of the three CSRP genes and their functions are still poorly understood in newts. In this study, we cloned the complete open reading frame (ORF) sequences of the three CSRP genes from the Chinese fire-bellied newt, Cynops orientalis (C. orientalis). The complete ORF sequences of Co-CSRP1, Co-CSRP2, and Co-CSRP3 were 582, 582, and 576bp, respectively, and encoded 193, 193, and 191 amino acids, respectively. The deduced amino acid sequences of the three CRP members showed high similarities with that of other species, particularly, with amphibians. Co-CSRP1 was highly expressed in the kidney, limb, and stomach, however, the expression was low in the spleen, heart, intestine, liver, and tail (P<0.05). The mRNA expression of Co-CSRP2 was higher in the kidney and heart than that in other organs (P<0.05). It was observed that Co-CSRP3 was only expressed in the heart, limb, and tail. The mRNA expression of Co-CSRP1 and Co-CSRP3 was lower in the digits in comparison to other limb segments. However, there was no significant difference of Co-CSRP2 mRNA expression in the four limb segments. The Co-CSRP1 and Co-CSRP2 mRNA expressions were significantly increased, whereas the expression of Co-CSRP3 was remarkably decreased during the limb regeneration. This study will provide useful information for further elucidating the role of Co-CSRP genes during newt limb regeneration.
[Mh] Termos MeSH primário: Proteínas Nucleares/genética
Salamandridae/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Clonagem Molecular/métodos
Cisteína/genética
Glicina/genética
Alinhamento de Sequência
Análise de Sequência de DNA/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nuclear Proteins); K848JZ4886 (Cysteine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE



página 1 de 3327 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde