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[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


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[PMID]:28448437
[Au] Autor:Lan K; Zhao Y; Fan Y; Ma B; Yang S; Liu Q; Linghu H; Wang H
[Ad] Endereço:Department of Obstetrics and Gynecology, The First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China. kangyun_lan@126.com.
[Ti] Título:Sulfiredoxin May Promote Cervical Cancer Metastasis via Wnt/ß-Catenin Signaling Pathway.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 27.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The abnormal elevation of sulfiredoxin (Srx/SRXN1)-an antioxidant enzyme whose main function is to protect against oxidative stress-has been shown to be closely correlated with the progression of several types of cancer, including human cervical cancer. However, the molecular mechanism by which Srx promotes tumor progression, especially cancer metastasis in cervical cancer, has not been elucidated. Here, we show that Srx expression gradually increases during the progression of human cervical cancer and its expression level is closely correlated with lymph node metastasis. Our study also reveals a significant positive correlation between the expression of Srx and ß-catenin in cervical cancer tissues. Loss-of-function studies demonstrate that Srx knockdown using a lentiviral vector-mediated specific shRNA decreases the migration and invasion capacity in HeLa (human papilloma virus 18 type cervical cancer cell line) and SiHa SiHa (cervical squamous cancer cell line). Notably, the exact opposite effects were observed in gain-of-function experiments in C-33A cells. Mechanistically, downregulation or upregulation of Srx leads to an altered expression of proteins associated with the Wnt/ß-catenin signaling pathway. Furthermore, blockage of the Wnt/ß-catenin signaling pathway contributed to attenuated Srx expression and resulted in significant inhibition of cell migration and invasion in cervical cancer cell lines. Combined, Srx might be an oncoprotein in cervical cancer, playing critical roles in activating the Wnt/ß-catenin signaling pathway; it may therefore be a therapeutic target for cervical cancer.
[Mh] Termos MeSH primário: Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Neoplasias do Colo do Útero/patologia
Via de Sinalização Wnt
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Regulação para Baixo/efeitos dos fármacos
Feminino
Glicogênio Sintase Quinase 3 beta/metabolismo
Células HeLa
Compostos Heterocíclicos com 3 Anéis/farmacologia
Seres Humanos
Imuno-Histoquímica
Metástase Linfática
Meia-Idade
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/antagonistas & inibidores
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Interferência de RNA
RNA Interferente Pequeno/metabolismo
Regulação para Cima/efeitos dos fármacos
Neoplasias do Colo do Útero/metabolismo
Via de Sinalização Wnt/efeitos dos fármacos
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Heterocyclic Compounds, 3-Ring); 0 (RNA, Small Interfering); 0 (XAV939); 0 (beta Catenin); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.98.2 (SRXN1 protein, human); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE


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[PMID]:29227591
[Au] Autor:Korneeva KL; Rodriguez RR; Ralchenko SV; Martunovska OV; Frolova AO; Martsenyuk OP; Manzhula LV; Melnyk VT; Shkoropad OY; Obolenska MY
[Ti] Título:Expression of genes, encoding the enzymes of cysteine metabolism in human placenta in the first and third trimesters of uncomplicated pregnancy.
[So] Source:Ukr Biochem J;88(1):88-98, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The cellular cysteine is highly regulated in a narrow range of concentrations due to its cyto- and neurtoxicity when it is overwhelmed or its deficiency for protein synthesis and other vital metabolic reactions when its amount is restricted. The regulation of cysteine content and its metabolic products, glutathione, taurine and inorganic sulfur compounds, is scarcely explored in human placenta though cysteine metabolism is closely related to the maintenance of redox status and protection from free radical oxidation, elimination of homocysteine and detoxification. These processes are particularly important for placenta which meets substantial changes of oxygen supply during its development, and is the last metabolically active organ between mother and fetus. The abundance of CDO , CSAD , ADO , SUOX, GCLC and GCLM mRNAs was estimated by RT -qPCR and compared with the computationally analyzed microarray gene expression data from GEO , while the level of individual protein ­ by western-blot analysis, both in placental samples from first and third trimesters of uncomplicated pregnancies. The abundance of CDO mRNA is significantly up-regulated at term compared to the first trimester, the level of GCLM and GCLC mRNAs remains almost unchanged while the abundance of other mRNAs reduces to varying degrees. Overall, the changes of gene expression in third trimester in comparison to the first one estimated by RT-qPCR and microarray coincide while the former data are more informative for the limited group of genes. The data provide the basis for further research of these genes expression and phenotype of human placenta in health and disease
[Mh] Termos MeSH primário: Carboxiliases/genética
Cisteína Dioxigenase/genética
Cisteína/metabolismo
Dioxigenases/genética
Glutamato-Cisteína Ligase/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
[Mh] Termos MeSH secundário: Adulto
Carboxiliases/metabolismo
Cisteína Dioxigenase/metabolismo
Dioxigenases/metabolismo
Feminino
Regulação da Expressão Gênica
Glutamato-Cisteína Ligase/metabolismo
Seres Humanos
Redes e Vias Metabólicas/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Placenta/metabolismo
Gravidez
Primeiro Trimestre da Gravidez
Terceiro Trimestre da Gravidez
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); EC 1.13.11.- (Dioxygenases); EC 1.13.11.19 (cysteamine dioxygenase); EC 1.13.11.20 (Cysteine Dioxygenase); EC 1.13.11.20 (cysteine dioxygenase, type I, human); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.3.1 (SUOX protein, human); EC 4.1.1.- (Carboxy-Lyases); EC 4.1.1.29 (sulfoalanine decarboxylase); EC 6.3.2.2 (GCLC protein, human); EC 6.3.2.2 (Glutamate-Cysteine Ligase); EC 6.3.2.2 (glutamate-cysteine ligase modifier subunit, human); K848JZ4886 (Cysteine)
[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/ubj88.01.088


  4 / 1149 MEDLINE  
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[PMID]:28918898
[Au] Autor:Ponsero AJ; Igbaria A; Darch MA; Miled S; Outten CE; Winther JR; Palais G; D'Autréaux B; Delaunay-Moisan A; Toledano MB
[Ad] Endereço:Institute for Integrative Biology of the Cell (I2BC), CEA-Saclay, CNRS, Université Paris-Saclay, ISVJC/SBIGEM, Laboratoire Stress Oxydant et Cancer, 91191 Gif-sur-Yvette, France.
[Ti] Título:Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.
[So] Source:Mol Cell;67(6):962-973.e5, 2017 Sep 21.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In the endoplasmic reticulum (ER), Ero1 catalyzes disulfide bond formation and promotes glutathione (GSH) oxidation to GSSG. Since GSSG cannot be reduced in the ER, maintenance of the ER glutathione redox state and levels likely depends on ER glutathione import and GSSG export. We used quantitative GSH and GSSG biosensors to monitor glutathione import into the ER of yeast cells. We found that glutathione enters the ER by facilitated diffusion through the Sec61 protein-conducting channel, while oxidized Bip (Kar2) inhibits transport. Increased ER glutathione import triggers H O -dependent Bip oxidation through Ero1 reductive activation, which inhibits glutathione import in a negative regulatory loop. During ER stress, transport is activated by UPR-dependent Ero1 induction, and cytosolic glutathione levels increase. Thus, the ER redox poise is tuned by reciprocal control of glutathione import and Ero1 activation. The ER protein-conducting channel is permeable to small molecules, provided the driving force of a concentration gradient.
[Mh] Termos MeSH primário: Retículo Endoplasmático/enzimologia
Proteínas Fúngicas/metabolismo
Glutationa/metabolismo
Glicoproteínas/metabolismo
Proteínas de Choque Térmico HSP70/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Canais de Translocação SEC/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Citosol/enzimologia
Difusão Facilitada
Proteínas Fúngicas/genética
Dissulfeto de Glutationa/metabolismo
Glicoproteínas/genética
Proteínas de Choque Térmico HSP70/genética
Peróxido de Hidrogênio/metabolismo
Membranas Intracelulares/enzimologia
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Oxirredução
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Canais de Translocação SEC/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transdução de Sinais
Fatores de Tempo
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Glycoproteins); 0 (HSP70 Heat-Shock Proteins); 0 (KAR2 protein, yeast); 0 (Membrane Proteins); 0 (SEC Translocation Channels); 0 (SEC61 protein, S cerevisiae); 0 (SSH1 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); BBX060AN9V (Hydrogen Peroxide); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.4.- (ERO1 protein, S cerevisiae); GAN16C9B8O (Glutathione); ULW86O013H (Glutathione Disulfide)
[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:170919
[St] Status:MEDLINE


  5 / 1149 MEDLINE  
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[PMID]:28512131
[Au] Autor:Landry AP; Ballou DP; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109.
[Ti] Título:H S oxidation by nanodisc-embedded human sulfide quinone oxidoreductase.
[So] Source:J Biol Chem;292(28):11641-11649, 2017 Jul 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Buildup of hydrogen sulfide (H S), which functions as a signaling molecule but is toxic at high concentrations, is averted by its efficient oxidation by the mitochondrial sulfide oxidation pathway. The first step in this pathway is catalyzed by a flavoprotein, sulfide quinone oxidoreductase (SQR), which converts H S to a persulfide and transfers electrons to coenzyme Q via a flavin cofactor. All previous studies on human SQR have used detergent-solubilized protein. Here, we embedded human SQR in nanodiscs ( SQR) and studied highly homogenous preparations by steady-state and rapid-kinetics techniques. SQR exhibited higher catalytic rates in its membranous environment than in its solubilized state. Stopped-flow spectroscopic data revealed that transfer of the sulfane sulfur from an SQR-bound cysteine persulfide intermediate to a small-molecule acceptor is the rate-limiting step. The physiological acceptor of sulfane sulfur from SQR has been the subject of controversy; we report that the kinetic analysis of SQR is consistent with glutathione rather than sulfite being the predominant acceptor at physiologically relevant concentrations of the respective metabolites. The identity of the acceptor has an important bearing on how the sulfide oxidation pathway is organized. Our data are more consistent with the reaction sequence for sulfide oxidation being: H S → glutathione persulfide → sulfite → sulfate, than with a more convoluted route that would result if sulfite were the primary acceptor of sulfane sulfur. In summary, nanodisc-incorporated human SQR exhibits enhanced catalytic performance, and pre-steady-state kinetics characterization of the complete SQR catalytic cycle indicates that GSH serves as the physiologically relevant sulfur acceptor.
[Mh] Termos MeSH primário: Enzimas Imobilizadas/metabolismo
Sulfeto de Hidrogênio/metabolismo
Modelos Moleculares
Nanopartículas/química
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
[Mh] Termos MeSH secundário: Apolipoproteína A-I/química
Apolipoproteína A-I/genética
Apolipoproteína A-I/metabolismo
Biocatálise
Cisteína/química
Transporte de Elétrons
Enzimas Imobilizadas/química
Enzimas Imobilizadas/genética
Glutationa/metabolismo
Seres Humanos
Cinética
Oxirredução
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/química
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Fosfatidilcolinas/química
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Ubiquinona/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein A-I); 0 (Enzymes, Immobilized); 0 (Peptide Fragments); 0 (Phosphatidylcholines); 0 (Recombinant Proteins); 1339-63-5 (Ubiquinone); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.- (SQRDL protein, human); GAN16C9B8O (Glutathione); K848JZ4886 (Cysteine); TE895536Y5 (1-palmitoyl-2-oleoylphosphatidylcholine); YY9FVM7NSN (Hydrogen Sulfide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788547


  6 / 1149 MEDLINE  
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[PMID]:28442570
[Au] Autor:Li Z; Shanmuganathan A; Ruetz M; Yamada K; Lesniak NA; Kräutler B; Brunold TC; Koutmos M; Banerjee R
[Ad] Endereço:From the Department of Biological Chemistry, University of Michigan Medical Center, Ann Arbor, Michigan 48109-0600.
[Ti] Título:Coordination chemistry controls the thiol oxidase activity of the B -trafficking protein CblC.
[So] Source:J Biol Chem;292(23):9733-9744, 2017 Jun 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cobalamin or B cofactor supports sulfur and one-carbon metabolism and the catabolism of odd-chain fatty acids, branched-chain amino acids, and cholesterol. CblC is a B -processing enzyme involved in an early cytoplasmic step in the cofactor-trafficking pathway. It catalyzes the glutathione (GSH)-dependent dealkylation of alkylcobalamins and the reductive decyanation of cyanocobalamin. CblC from ( CblC) also exhibits a robust thiol oxidase activity, converting reduced GSH to oxidized GSSG with concomitant scrubbing of ambient dissolved O The mechanism of thiol oxidation catalyzed by CblC is not known. In this study, we demonstrate that novel coordination chemistry accessible to CblC-bound cobalamin supports its thiol oxidase activity via a glutathionyl-cobalamin intermediate. Deglutathionylation of glutathionyl-cobalamin by a second molecule of GSH yields GSSG. The crystal structure of CblC provides insights into how architectural differences at the α- and ß-faces of cobalamin promote the thiol oxidase activity of CblC but mute it in wild-type human CblC. The R161G and R161Q mutations in human CblC unmask its latent thiol oxidase activity and are correlated with increased cellular oxidative stress disease. In summary, we have uncovered key architectural features in the cobalamin-binding pocket that support unusual cob(II)alamin coordination chemistry and enable the thiol oxidase activity of CblC.
[Mh] Termos MeSH primário: Proteínas de Caenorhabditis elegans/química
Caenorhabditis elegans/enzimologia
Proteínas de Transporte/química
Cobamidas/química
Estresse Oxidativo
[Mh] Termos MeSH secundário: Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Cobamidas/genética
Cobamidas/metabolismo
Seres Humanos
Mutação de Sentido Incorreto
Oxirredutases atuantes sobre Doadores de Grupo Enxofre
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Carrier Proteins); 0 (Cobamides); 0 (MMACHC protein, human); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170616
[Lr] Data última revisão:
170616
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.788554


  7 / 1149 MEDLINE  
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[PMID]:28351308
[Au] Autor:Chen X; Lan K; Liu Q; Yang X; Wang H
[Ad] Endereço:Department of Obstetrics and Gynecology, The First Affiliated Hospital of Chongqing Medical University, Chongqing, People's Republic of China.
[Ti] Título:Sulfiredoxin may promote metastasis and invasion of cervical squamous cell carcinoma by epithelial-mesenchymal transition.
[So] Source:Tumour Biol;39(3):1010428317695942, 2017 Mar.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sulfiredoxin (Srx), a novel oxidative stress-induced antioxidant protein, has been reported to be expressed in several human tumour tissues. However, the expression and functions of Srx in cervical squamous cell carcinoma remain unknown. Here, we proved that expression of Srx was upregulated in cervical tissues as revealed by immunohistochemistry, and revealed a close correlation between the protein's expression and the expression level of one core epithelial-mesenchymal transition marker, E-cadherin. We demonstrated that Srx was overexpressed in cervical squamous cell carcinoma and its expression level was closely correlated with lymph node metastasis and invasion of cervical squamous cell carcinoma. Meanwhile, Srx expression was negatively correlated with E-cadherin expression. The remission time (tumour-free status after surgery) of the Srx strong staining group was significantly shorter than that of the Srx weak staining group. We silenced Srx by short hairpin RNA in HeLa and SiHa cells. Diminished Srx expression upregulated E-cadherin expression. The cell invasion and migration activity in the ShSrx group were obviously decreased in HeLa and SiHa cells. Moreover, Srx regulated the expression of the other marker of epithelial-mesenchymal transition, vimentin. In conclusion, the study suggested that Srx was highly expressed in cervical squamous cell carcinoma and may promote invasion and metastasis of cervical squamous cell carcinoma via regulating epithelial-mesenchymal transition.
[Mh] Termos MeSH primário: Caderinas/biossíntese
Carcinoma de Células Escamosas/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Neoplasias do Colo do Útero/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Caderinas/genética
Carcinoma de Células Escamosas/patologia
Movimento Celular/genética
Transição Epitelial-Mesenquimal/genética
Feminino
Regulação Neoplásica da Expressão Gênica
Células HeLa
Seres Humanos
Meia-Idade
Invasividade Neoplásica/genética
Metástase Neoplásica
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/antagonistas & inibidores
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/biossíntese
RNA Interferente Pequeno/genética
Neoplasias do Colo do Útero/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cadherins); 0 (RNA, Small Interfering); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.98.2 (SRXN1 protein, human)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170407
[Lr] Data última revisão:
170407
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317695942


  8 / 1149 MEDLINE  
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[PMID]:28298220
[Au] Autor:Kobayashi J; Sasaki D; Hara KY; Hasunuma T; Kondo A
[Ad] Endereço:Graduate School of Science, Technology and Innovation, Kobe University, 1-1 Rokkodaicho, Nada-ku, Kobe, Hyogo, 657-8501, Japan.
[Ti] Título:Enzymatic improvement of mitochondrial thiol oxidase Erv1 for oxidized glutathione fermentation by Saccharomyces cerevisiae.
[So] Source:Microb Cell Fact;16(1):44, 2017 Mar 15.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Oxidized glutathione (GSSG) is the preferred form for industrial mass production of glutathione due to its high stability compared with reduced glutathione (GSH). In our previous study, over-expression of the mitochondrial thiol oxidase ERV1 gene was the most effective for high GSSG production in Saccharomyces cerevisiae cells among three types of different thiol oxidase genes. RESULTS: We improved Erv1 enzyme activity for oxidation of GSH and revealed that S32 and N34 residues are critical for the oxidation. Five engineered Erv1 variant proteins containing S32 and/or N34 replacements exhibited 1.7- to 2.4-fold higher in vitro GSH oxidation activity than that of parental Erv1, whereas the oxidation activities of these variants for γ-glutamylcysteine were comparable. According to three-dimensional structures of Erv1 and protein stability assays, S32 and N34 residues interact with nearby residues through hydrogen bonding and greatly contribute to protein stability. These results suggest that increased flexibility by amino acid replacements around the active center decrease inhibitory effects on GSH oxidation. Over-expressions of mutant genes coding these Erv1 variants also increased GSSG and consequently total glutathione production in S. cerevisiae cells. Over-expression of the ERV1 gene was the most effective for GSSG production in S. cerevisiae cells among the parent and other mutant genes, and it increased GSSG production about 1.5-fold compared to that of the parental ERV1 gene. CONCLUSIONS: This is the first study demonstrating the pivotal effects of S32 and N34 residues to high GSH oxidation activity of Erv1. Furthermore, in vivo validity of Erv1 variants containing these S32 and N34 replacements were also demonstrated. This study indicates potentials of Erv1 for high GSSG production.
[Mh] Termos MeSH primário: Fermentação
Glutationa/metabolismo
Mitocôndrias/enzimologia
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Dipeptídeos/metabolismo
Engenharia Metabólica/métodos
Modelos Moleculares
Mutação
Oxirredução
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dipeptides); 0 (Mitochondrial Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.3.2 (ERV1 protein, S cerevisiae); GAN16C9B8O (Glutathione); M984VJS48P (gamma-glutamylcysteine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170420
[Lr] Data última revisão:
170420
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0658-0


  9 / 1149 MEDLINE  
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[PMID]:28274319
[Au] Autor:Lan K; Chen X; Liu Q; Fan Y; Zhao Y; Wang H
[Ad] Endereço:Department of Obstetrics and Gynecology, First Affiliated Hospital of Chongqing Medical University, Chongqing 400016, China.
[Ti] Título:[Highly expressed sulfiredoxin and ß-catenin are associated with malignancy of cervical squamous cell carcinoma].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;33(3):376-379, 2017 Mar.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Objective To investigate the expressions of sulfiredoxin (Srx) and ß-catenin in human cervical squamous cell carcinoma (CSCC) and their clinical significance. Methods Immunohistochemistry was used to detect the expressions of Srx and ß-catenin in human cervical specimens, including normal cervical squamous cell epithelium tissues (NC), cervical intraepithelial neoplasia tissues (CIN), and CSCC. The correlation between Srx expression and ß-catenin expression and the relationship of the two proteins to clinical the pathological features of cervical cancer were analyzed. Results The expression of Srx in CIN and CSCC was significantly higher than that in NC. In addition, Srx and ß-catenin expressions were positively correlated to CSCC tissues. Furthermore, the up-regulated expression of Srx was significantly associated with lymph node metastasis, infiltration of vessels, and the depth of cancer invasion. However, its expression was not associated with age, tumor size, degree of differentiation, and International Federation of Gynecology and Obstetrics (FIGO) grade. Finally, the overexpression of ß-catenin was significantly correlated with lymph node metastasis, degree of differentiation, and FIGO grade. However, ß-catenin expression was not correlated with age, tumor size, and the depth of cancer invasion. Conclusion Srx and ß-catenin are highly expressed in CSCC and associated with malignancy.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/genética
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/genética
Neoplasias do Colo do Útero/genética
beta Catenina/genética
[Mh] Termos MeSH secundário: Adulto
Idoso
Carcinoma de Células Escamosas/metabolismo
Carcinoma de Células Escamosas/patologia
Feminino
Seres Humanos
Metástase Linfática
Meia-Idade
Estadiamento de Neoplasias
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Neoplasias do Colo do Útero/metabolismo
Neoplasias do Colo do Útero/patologia
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (beta Catenin); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); EC 1.8.98.2 (SRXN1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170310
[St] Status:MEDLINE


  10 / 1149 MEDLINE  
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[PMID]:28257465
[Au] Autor:Grabarczyk DB; Berks BC
[Ad] Endereço:Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
[Ti] Título:Intermediates in the Sox sulfur oxidation pathway are bound to a sulfane conjugate of the carrier protein SoxYZ.
[So] Source:PLoS One;12(3):e0173395, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Sox pathway found in many sulfur bacteria oxidizes thiosulfate to sulfate. Pathway intermediates are covalently bound to a cysteine residue in the carrier protein SoxYZ. We have used biochemical complementation by SoxYZ-conjugates to probe the identity of the intermediates in the Sox pathway. We find that unconjugated SoxYZ and SoxYZ-S-sulfonate are unlikely to be intermediates during normal turnover in disagreement with current models. By contrast, conjugates with multiple sulfane atoms are readily metabolised by the Sox pathway. The most parsimonious interpretation of these data is that the true carrier species in the Sox pathway is a SoxYZ-S-sulfane adduct.
[Mh] Termos MeSH primário: Bactérias/enzimologia
Proteínas de Transporte/metabolismo
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/metabolismo
Enxofre/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Transporte/química
Proteínas de Transporte/genética
Cisteína/metabolismo
Oxirredução
Oxirredutases atuantes sobre Doadores de Grupo Enxofre/química
Ligação Proteica
Transdução de Sinais
Tiossulfatos/química
Tiossulfatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Thiosulfates); 70FD1KFU70 (Sulfur); EC 1.8.- (Oxidoreductases Acting on Sulfur Group Donors); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0173395



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