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[PMID]:29061305
[Au] Autor:Tichá T; Lochman J; Cincalová L; Luhová L; Petrivalský M
[Ad] Endereço:Department of Biochemistry, Faculty of Science, Palacký University, Slechtitelu 27, CZ-783 71 Olomouc, Czech Republic.
[Ti] Título:Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues.
[So] Source:Biochem Biophys Res Commun;494(1-2):27-33, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Proteínas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/antagonistas & inibidores
Aldeído Oxirredutases/química
Animais
Cisteína/química
Cisteína/metabolismo
Peróxido de Hidrogênio/farmacologia
Lycopersicon esculentum/genética
Lycopersicon esculentum/crescimento & desenvolvimento
Lycopersicon esculentum/metabolismo
Óxido Nítrico/metabolismo
Doadores de Óxido Nítrico/farmacologia
Nitrosação
Oxirredução
Proteínas de Plantas/antagonistas & inibidores
Proteínas de Plantas/química
Processamento de Proteína Pós-Traducional
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
S-Nitrosoglutationa/metabolismo
S-Nitrosotióis/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nitric Oxide Donors); 0 (Plant Proteins); 0 (Recombinant Proteins); 0 (S-Nitrosothiols); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); BBX060AN9V (Hydrogen Peroxide); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


  2 / 3911 MEDLINE  
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[PMID]:28949132
[Au] Autor:Goetzl S; Teutloff C; Werther T; Hennig SE; Jeoung JH; Bittl R; Dobbek H
[Ad] Endereço:Institut für Biologie, Strukturbiologie/Biochemie, Humboldt-Universität zu Berlin , Berlin, Germany.
[Ti] Título:Protein Dynamics in the Reductive Activation of a B12-Containing Enzyme.
[So] Source:Biochemistry;56(41):5496-5502, 2017 Oct 17.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:B12-dependent proteins are involved in methyl transfer reactions ranging from the biosynthesis of methionine in humans to the formation of acetyl-CoA in anaerobic bacteria. During their catalytic cycle, they undergo large conformational changes to interact with various proteins. Recently, the crystal structure of the B12-containing corrinoid iron-sulfur protein (CoFeSP) in complex with its reductive activator (RACo) was determined, providing a first glimpse of how energy is transduced in the ATP-dependent reductive activation of corrinoid-containing methyltransferases. The thermodynamically uphill electron transfer from RACo to CoFeSP is accompanied by large movements of the cofactor-binding domains of CoFeSP. To refine the structure-based mechanism, we analyzed the conformational change of the B12-binding domain of CoFeSP by pulsed electron-electron double resonance and Förster resonance energy transfer spectroscopy. We show that the site-specific labels on the flexible B12-binding domain and the small subunit of CoFeSP move within 11 Å in the RACo:CoFeSP complex, consistent with the recent crystal structures. By analyzing the transient kinetics of formation and dissociation of the RACo:CoFeSP complex, we determined values of 0.75 µM s and 0.33 s for rate constants k and k , respectively. Our results indicate that the large movement observed in crystals also occurs in solution and that neither the formation of the protein encounter complex nor the large movement of the B12-binding domain is rate-limiting for the ATP-dependent reductive activation of CoFeSP by RACo.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Coenzimas/metabolismo
Ativadores de Enzimas/metabolismo
Firmicutes/enzimologia
Proteínas com Ferro-Enxofre/metabolismo
Modelos Moleculares
Vitamina B 12/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/química
Aldeído Oxirredutases/genética
Aldeído Oxirredutases/metabolismo
Substituição de Aminoácidos
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Coenzimas/química
Cristalografia por Raios X
Bases de Dados de Proteínas
Dimerização
Ativadores de Enzimas/química
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Cinética
Complexos Multienzimáticos/química
Complexos Multienzimáticos/genética
Complexos Multienzimáticos/metabolismo
Mutagênese Sítio-Dirigida
Mutação
Oxirredução
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Subunidades Proteicas/química
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Solubilidade
Vitamina B 12/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Coenzymes); 0 (Enzyme Activators); 0 (Iron-Sulfur Proteins); 0 (Multienzyme Complexes); 0 (Protein Subunits); 0 (Recombinant Proteins); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.99.2 (carbon monoxide dehydrogenase); P6YC3EG204 (Vitamin B 12)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00477


  3 / 3911 MEDLINE  
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[PMID]:28715469
[Au] Autor:Jayachandran C; Palanisamy Athiyaman B; Sankaranarayanan M
[Ad] Endereço:Centre for Biotechnology, Anna University, Chennai, India.
[Ti] Título:Cofactor engineering improved CALB production in Pichia pastoris through heterologous expression of NADH oxidase and adenylate kinase.
[So] Source:PLoS One;12(7):e0181370, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cofactor engineering strategy can relieve the metabolic stress induced by expression of recombinant protein in cellular metabolism related to cofactor and energy reactions. To study the effect of cofactor regeneration on recombinant protein expression, NADH oxidase (noxE) was engineered in P. pastoris expressing lipase B (GSCALB). Expression of noxE in P. pastoris (GSCALBNOX) increased NAD+ levels by 85% with a concomitant reduction in NADH/NAD+ ratio of 67% compared to GSCALB. The change in the redox level positively influenced the methanol uptake rate and made 34% augment in CALB activity. The decline in NADH level (44%) by noxE expression had lowered the adenylate energy charge (AEC) and ATP level in GSCALBNOX. In order to regenerate ATP in GSCALBNOX, adenylate kinase (ADK1) gene from S. cerevisiae S288c was co-expressed. Expression of ADK1 showed a remarkable increase in AEC and co-expression of both the genes synergistically improved CALB activity. This study shows the importance of maintenance of cellular redox homeostasis and adenylate energy charge during recombinant CALB expression in P. pastoris.
[Mh] Termos MeSH primário: Adenilato Quinase/metabolismo
Proteínas Fúngicas/biossíntese
Lipase/biossíntese
Complexos Multienzimáticos/metabolismo
NADH NADPH Oxirredutases/metabolismo
Pichia/genética
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adenilato Quinase/genética
Aldeído Oxirredutases/metabolismo
Proteínas Fúngicas/genética
Expressão Gênica
Engenharia Genética
Homeostase
Lipase/genética
Metanol/metabolismo
Complexos Multienzimáticos/genética
NAD/metabolismo
NADH NADPH Oxirredutases/genética
Oxirredução
Pichia/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Proteínas Recombinantes/biossíntese
Saccharomyces/enzimologia
Saccharomyces/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); 0 (Multienzyme Complexes); 0 (Recombinant Proteins); 0U46U6E8UK (NAD); 8L70Q75FXE (Adenosine Triphosphate); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); EC 1.6.- (NADH oxidase); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 2.7.4.3 (Adenylate Kinase); EC 3.1.1.3 (Lipase); EC 3.1.1.3 (lipase B, Candida antarctica); Y4S76JWI15 (Methanol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181370


  4 / 3911 MEDLINE  
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[PMID]:28650429
[Au] Autor:Kim JM; To TK; Matsui A; Tanoi K; Kobayashi NI; Matsuda F; Habu Y; Ogawa D; Sakamoto T; Matsunaga S; Bashir K; Rasheed S; Ando M; Takeda H; Kawaura K; Kusano M; Fukushima A; Endo TA; Kuromori T; Ishida J; Morosawa T; Tanaka M; Torii C; Takebayashi Y; Sakakibara H; Ogihara Y; Saito K; Shinozaki K; Devoto A; Seki M
[Ad] Endereço:Plant Genomic Network Research Team, RIKEN Centre for Sustainable Resource Science (CSRS), 1-7-22 Suehiro, Tsurumi, Yokohama 230-0045, Japan.
[Ti] Título:Acetate-mediated novel survival strategy against drought in plants.
[So] Source:Nat Plants;3:17097, 2017 Jun 26.
[Is] ISSN:2055-0278
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Water deficit caused by global climate changes seriously endangers the survival of organisms and crop productivity, and increases environmental deterioration . Plants' resistance to drought involves global reprogramming of transcription, cellular metabolism, hormone signalling and chromatin modification . However, how these regulatory responses are coordinated via the various pathways, and the underlying mechanisms, are largely unknown. Herein, we report an essential drought-responsive network in which plants trigger a dynamic metabolic flux conversion from glycolysis into acetate synthesis to stimulate the jasmonate (JA) signalling pathway to confer drought tolerance. In Arabidopsis, the ON/OFF switching of this whole network is directly dependent on histone deacetylase HDA6. In addition, exogenous acetic acid promotes de novo JA synthesis and enrichment of histone H4 acetylation, which influences the priming of the JA signalling pathway for plant drought tolerance. This novel acetate function is evolutionarily conserved as a survival strategy against environmental changes in plants. Furthermore, the external application of acetic acid successfully enhanced the drought tolerance in Arabidopsis, rapeseed, maize, rice and wheat plants. Our findings highlight a radically new survival strategy that exploits an epigenetic switch of metabolic flux conversion and hormone signalling by which plants adapt to drought.
[Mh] Termos MeSH primário: Acetatos/metabolismo
Arabidopsis/fisiologia
Secas
[Mh] Termos MeSH secundário: Aclimatação
Aldeído Oxirredutases/metabolismo
Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Ciclopentanos/metabolismo
Epigênese Genética
Glicólise
Histona Desacetilases/metabolismo
Oxilipinas/metabolismo
Plantas Geneticamente Modificadas
Ligação Proteica
Piruvato Descarboxilase/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Arabidopsis Proteins); 0 (Cyclopentanes); 0 (Oxylipins); 6RI5N05OWW (jasmonic acid); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde dehydrogenase (NAD(P)+)); EC 3.5.1.- (HDA6 protein, Arabidopsis); EC 3.5.1.98 (Histone Deacetylases); EC 4.1.1.1 (Pyruvate Decarboxylase)
[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:170627
[St] Status:MEDLINE
[do] DOI:10.1038/nplants.2017.97


  5 / 3911 MEDLINE  
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[PMID]:28581514
[Au] Autor:Pérez-Alea M; McGrail K; Sánchez-Redondo S; Ferrer B; Fournet G; Cortés J; Muñoz E; Hernandez-Losa J; Tenbaum S; Martin G; Costello R; Ceylan I; Garcia-Patos V; Recio JA
[Ad] Endereço:Biomedical Research in Melanoma-Animal Models and Cancer Laboratory-Oncology Program, Vall d'Hebron Research institute VHIR-Vall d'Hebron Hospital, Barcelona-UAB, Spain.
[Ti] Título:ALDH1A3 is epigenetically regulated during melanocyte transformation and is a target for melanoma treatment.
[So] Source:Oncogene;36(41):5695-5708, 2017 Oct 12.
[Is] ISSN:1476-5594
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Despite the promising targeted and immune-based interventions in melanoma treatment, long-lasting responses are limited. Melanoma cells present an aberrant redox state that leads to the production of toxic aldehydes that must be converted into less reactive molecules. Targeting the detoxification machinery constitutes a novel therapeutic avenue for melanoma. Here, using 56 cell lines representing nine different tumor types, we demonstrate that melanoma cells exhibit a strong correlation between reactive oxygen species amounts and aldehyde dehydrogenase 1 (ALDH1) activity. We found that ALDH1A3 is upregulated by epigenetic mechanisms in melanoma cells compared with normal melanocytes. Furthermore, it is highly expressed in a large percentage of human nevi and melanomas during melanocyte transformation, which is consistent with the data from the TCGA, CCLE and protein atlas databases. Melanoma treatment with the novel irreversible isoform-specific ALDH1 inhibitor [4-dimethylamino-4-methyl-pent-2-ynthioic acid-S methylester] di-methyl-ampal-thio-ester (DIMATE) or depletion of ALDH1A1 and/or ALDH1A3, promoted the accumulation of apoptogenic aldehydes leading to apoptosis and tumor growth inhibition in immunocompetent, immunosuppressed and patient-derived xenograft mouse models. Interestingly, DIMATE also targeted the slow cycling label-retaining tumor cell population containing the tumorigenic and chemoresistant cells. Our findings suggest that aldehyde detoxification is relevant metabolic mechanism in melanoma cells, which can be used as a novel approach for melanoma treatment.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/genética
Alquinos/administração & dosagem
Melanócitos/efeitos dos fármacos
Melanoma/tratamento farmacológico
Compostos de Sulfidrila/administração & dosagem
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/antagonistas & inibidores
Animais
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Transformação Celular Neoplásica/efeitos dos fármacos
Transformação Celular Neoplásica/genética
Epigênese Genética
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Melanócitos/patologia
Melanoma/genética
Melanoma/patologia
Camundongos
Células-Tronco Neoplásicas/efeitos dos fármacos
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alkynes); 0 (Sulfhydryl Compounds); 0 (dimethylthioampal); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde dehydrogenase (NAD(P)+))
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1038/onc.2017.160


  6 / 3911 MEDLINE  
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[PMID]:28493997
[Au] Autor:Shao Q; Casin KM; Mackowski N; Murphy E; Steenbergen C; Kohr MJ
[Ad] Endereço:Department of Cardiology, Renji Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China.
[Ti] Título:Adenosine A1 receptor activation increases myocardial protein S-nitrosothiols and elicits protection from ischemia-reperfusion injury in male and female hearts.
[So] Source:PLoS One;12(5):e0177315, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitric oxide (NO) plays an important role in cardioprotection, and recent work from our group and others has implicated protein S-nitrosylation (SNO) as a critical component of NO-mediated protection in different models, including ischemic pre- and post-conditioning and sex-dependent cardioprotection. However, studies have yet to examine whether protein SNO levels are similarly increased with pharmacologic preconditioning in male and female hearts, and whether an increase in protein SNO levels, which is protective in male hearts, is sufficient to increase baseline protection in female hearts. Therefore, we pharmacologically preconditioned male and female hearts with the adenosine A1 receptor agonist N6-cyclohexyl adenosine (CHA). CHA administration prior to ischemia significantly improved functional recovery in both male and female hearts compared to baseline in a Langendorff-perfused heart model of ischemia-reperfusion injury (% of preischemic function ± SE: male baseline: 37.5±3.4% vs. male CHA: 55.3±3.2%; female baseline: 61.4±5.7% vs. female CHA: 76.0±6.2%). In a separate set of hearts, we found that CHA increased p-Akt and p-eNOS levels. We also used SNO-resin-assisted capture with LC-MS/MS to identify SNO proteins in male and female hearts, and determined that CHA perfusion induced a modest increase in protein SNO levels in both male (11.4%) and female (12.3%) hearts compared to baseline. These findings support a potential role for protein SNO in a model of pharmacologic preconditioning, and provide evidence to suggest that a modest increase in protein SNO levels is sufficient to protect both male and female hearts from ischemic injury. In addition, a number of the SNO proteins identified with CHA treatment were also observed with other forms of cardioprotective stimuli in prior studies, further supporting a role for protein SNO in cardioprotection.
[Mh] Termos MeSH primário: Miocárdio/metabolismo
Receptor A1 de Adenosina/metabolismo
Traumatismo por Reperfusão/metabolismo
Traumatismo por Reperfusão/patologia
S-Nitrosotióis/metabolismo
[Mh] Termos MeSH secundário: Adenosina/análogos & derivados
Adenosina/farmacologia
Adenosina/uso terapêutico
Agonistas do Receptor A1 de Adenosina/farmacologia
Agonistas do Receptor A1 de Adenosina/uso terapêutico
Aldeído Oxirredutases/metabolismo
Animais
Cardiotônicos/farmacologia
Cardiotônicos/uso terapêutico
Feminino
Masculino
Camundongos Endogâmicos C57BL
Contração Miocárdica/efeitos dos fármacos
Miocárdio/patologia
Óxido Nítrico Sintase Tipo III/metabolismo
Perfusão
Fosforilação/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-akt/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Recuperação de Função Fisiológica/efeitos dos fármacos
Traumatismo por Reperfusão/tratamento farmacológico
Traumatismo por Reperfusão/fisiopatologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenosine A1 Receptor Agonists); 0 (Cardiotonic Agents); 0 (Reactive Oxygen Species); 0 (Receptor, Adenosine A1); 0 (S-Nitrosothiols); 36396-99-3 (N(6)-cyclohexyladenosine); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177315


  7 / 3911 MEDLINE  
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[PMID]:28443495
[Au] Autor:Wang S; Liang C; Bao M; Li X; Zhang L; Li S; Qin C; Shao P; Li J; Hua L; Wang Z
[Ad] Endereço:1 State Key Laboratory for Reproductive Medicine and Department of Urology, The First Affiliated Hospital of Nanjing Medical University, Nanjing, China.
[Ti] Título:ALDH1A3 correlates with luminal phenotype in prostate cancer.
[So] Source:Tumour Biol;39(4):1010428317703652, 2017 Apr.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostate cancer is the most common male malignancies in the United States. The specific characteristics of different disease stages have been deeply investigated. We present our data on ALDH1A3 as a potential therapeutic target for the prostate cancer based on several functional investigations. Also, we used The Cancer Genome Atlas datasets for primary prostate cancer to detect the relevance of ALDH1A3 and prostate cancer luminal phenotype. We found that ALDH1A3 correlated with androgen receptor signaling pathway in primary prostate cancer, which is consistent with its luminal layer localization. Then, from the genetic manipulation assay, we knocked out the ALDH1A3 in PC-3 cells and found significantly reduced proliferation rate as well as the invasion ability. Furthermore, we looked up our single center primary prostate cancer post-operative follow-up data and suggested that the high level ALDH1A3 expression could predict the poor progression-free survival in a 158-patient cohort. We concluded that ALDH1A3, localized in luminal layer in prostate epithelium, is highly expressed in prostate cancer. It played important role in maintaining the proliferation, invasion, and cell cycle. It can also become the potential biomarker in the future to guide the therapeutic manipulations for primary prostate cancer.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/biossíntese
Biomarcadores Tumorais/biossíntese
Neoplasias da Próstata/genética
[Mh] Termos MeSH secundário: Idoso
Aldeído Oxirredutases/genética
Biomarcadores Tumorais/genética
Proliferação Celular/genética
Intervalo Livre de Doença
Regulação Neoplásica da Expressão Gênica/genética
Seres Humanos
Masculino
Meia-Idade
Gradação de Tumores
Invasividade Neoplásica/genética
Neoplasias da Próstata/patologia
Neoplasias da Próstata/cirurgia
Receptores Androgênicos/genética
Transdução de Sinais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Receptors, Androgen); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde dehydrogenase (NAD(P)+))
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317703652


  8 / 3911 MEDLINE  
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[PMID]:28423611
[Au] Autor:Sullivan KE; Rojas K; Cerione RA; Nakano I; Wilson KF
[Ad] Endereço:Department of Molecular Medicine, Cornell University, Ithaca, NY, USA.
[Ti] Título:The stem cell/cancer stem cell marker ALDH1A3 regulates the expression of the survival factor tissue transglutaminase, in mesenchymal glioma stem cells.
[So] Source:Oncotarget;8(14):22325-22343, 2017 Apr 04.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tissue transglutaminase (tTG), a dual-function enzyme with GTP-binding and acyltransferase activities, has been implicated in the survival and chemotherapy resistance of aggressive cancer cells and cancer stem cells, including glioma stem cells (GSCs). Using a model system comprising two distinct subtypes of GSCs referred to as proneural (PN) and mesenchymal (MES), we find that the phenotypically aggressive and radiation therapy-resistant MES GSCs exclusively express tTG relative to PN GSCs. As such, the self-renewal, proliferation, and survival of these cells was sensitive to treatment with tTG inhibitors, with a benefit being observed when combined with the standard of care for high grade gliomas (i.e. radiation or temozolomide). Efforts to understand the molecular drivers of tTG expression in MES GSCs revealed an unexpected link between tTG and a common marker for stem cells and cancer stem cells, Aldehyde dehydrogenase 1A3 (ALDH1A3). ALDH1A3, as well as other members of the ALDH1 subfamily, can function in cells as a retinaldehyde dehydrogenase to generate retinoic acid (RA) from retinal. We show that the enzymatic activity of ALDH1A3 and its product, RA, are necessary for the observed expression of tTG in MES GSCs. Additionally, the ectopic expression of ALDH1A3 in PN GSCs is sufficient to induce the expression of tTG in these cells, further demonstrating a causal link between ALDH1A3 and tTG. Together, these findings ascribe a novel function for ALDH1A3 in an aggressive GSC phenotype via the up-regulation of tTG, and suggest the potential for a similar role by ALDH1 family members across cancer types.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Neoplasias Encefálicas/metabolismo
Proteínas de Ligação ao GTP/metabolismo
Glioma/metabolismo
Células Mesenquimais Estromais/fisiologia
Células-Tronco Neoplásicas/fisiologia
Células-Tronco/fisiologia
Transglutaminases/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/genética
Biomarcadores Tumorais/metabolismo
Neoplasias Encefálicas/genética
Linhagem Celular Tumoral
Proliferação Celular
Sobrevivência Celular
Dacarbazina/análogos & derivados
Dacarbazina/farmacologia
Proteínas de Ligação ao GTP/genética
Regulação Neoplásica da Expressão Gênica
Glioma/genética
Seres Humanos
RNA Interferente Pequeno/genética
Transglutaminases/genética
Tretinoína/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (RNA, Small Interfering); 5688UTC01R (Tretinoin); 7GR28W0FJI (Dacarbazine); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.5 (aldehyde dehydrogenase (NAD(P)+)); EC 2.3.2.- (transglutaminase 2); EC 2.3.2.13 (Transglutaminases); EC 3.6.1.- (GTP-Binding Proteins); YF1K15M17Y (temozolomide)
[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:170421
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.16479


  9 / 3911 MEDLINE  
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[PMID]:28393572
[Au] Autor:Barnett SD; Buxton ILO
[Ad] Endereço:a Department of Pharmacology , University of Nevada, Reno School of Medicine , Reno , NV , USA.
[Ti] Título:The role of S-nitrosoglutathione reductase (GSNOR) in human disease and therapy.
[So] Source:Crit Rev Biochem Mol Biol;52(3):340-354, 2017 Jun.
[Is] ISSN:1549-7798
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:S-nitrosoglutathione reductase (GSNOR), or ADH5, is an enzyme in the alcohol dehydrogenase (ADH) family. It is unique when compared to other ADH enzymes in that primary short-chain alcohols are not its principle substrate. GSNOR metabolizes S-nitrosoglutathione (GSNO), S-hydroxymethylglutathione (the spontaneous adduct of formaldehyde and glutathione), and some alcohols. GSNOR modulates reactive nitric oxide (•NO) availability in the cell by catalyzing the breakdown of GSNO, and indirectly regulates S-nitrosothiols (RSNOs) through GSNO-mediated protein S-nitrosation. The dysregulation of GSNOR can significantly alter cellular homeostasis, leading to disease. GSNOR plays an important regulatory role in smooth muscle relaxation, immune function, inflammation, neuronal development and cancer progression, among many other processes. In recent years, the therapeutic inhibition of GSNOR has been investigated to treat asthma, cystic fibrosis and interstitial lung disease (ILD). The direct action of •NO on cellular pathways, as well as the important regulatory role of protein S-nitrosation, is closely tied to GSNOR regulation and defines this enzyme as an important therapeutic target.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Asma
Fibrose Cística
Proteínas de Neoplasias/metabolismo
Neoplasias
[Mh] Termos MeSH secundário: Asma/enzimologia
Asma/terapia
Fibrose Cística/enzimologia
Fibrose Cística/terapia
Seres Humanos
Relaxamento Muscular
Músculo Liso/enzimologia
Neoplasias/enzimologia
Neoplasias/terapia
Neurônios/enzimologia
Óxido Nítrico/metabolismo
S-Nitrosoglutationa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Neoplasm Proteins); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE
[do] DOI:10.1080/10409238.2017.1304353


  10 / 3911 MEDLINE  
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[PMID]:28381519
[Au] Autor:Yamashita AMS; Ancillotti MTC; Rangel LP; Fontenele M; Figueiredo-Freitas C; Possidonio AC; Soares CP; Sorenson MM; Mermelstein C; Nogueira L
[Ad] Endereço:Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
[Ti] Título:Balance between -nitrosylation and denitrosylation modulates myoblast proliferation independently of soluble guanylyl cyclase activation.
[So] Source:Am J Physiol Cell Physiol;313(1):C11-C26, 2017 Jul 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitric oxide (NO) contributes to myogenesis by regulating the transition between myoblast proliferation and fusion through cGMP signaling. NO can form -nitrosothiols (RSNO), which control signaling pathways in many different cell types. However, neither the role of RSNO content nor its regulation by the denitrosylase activity of -nitrosoglutathione reductase (GSNOR) during myogenesis is understood. Here, we used primary cultures of chick embryonic skeletal muscle cells to investigate whether changes in intracellular RSNO alter proliferation and fusion of myoblasts in the presence and absence of cGMP. Cultures were grown to fuse most of the myoblasts into myotubes, with and without -nitrosocysteine (CysNO), 8-Br-cGMP, DETA-NO, or inhibitors for NO synthase (NOS), GSNOR, soluble guanylyl cyclase (sGC), or a combination of these, followed by analysis of GSNOR activity, protein expression, RSNO, cGMP, and cell morphology. Although the activity of GSNOR increased progressively over 72 h, inhibiting GSNOR (by GSNOR inhibitor - GSNORi - or by knocking down GSNOR with siRNA) produced an increase in RSNO and in the number of myoblasts and fibroblasts, accompanied by a decrease in myoblast fusion index. This was also detected with CysNO supplementation. Enhanced myoblast number was proportional to GSNOR inhibition. Effects of the GSNORi and GSNOR knockdown were blunted by NOS inhibition, suggesting their dependence on NO synthesis. Interestingly, GSNORi and GSNOR knockdown reversed the attenuated proliferation obtained with sGC inhibition in myoblasts, but not in fibroblasts. Hence myoblast proliferation is enhanced by increasing RSNO, and regulated by GSNOR activity, independently of cGMP production and signaling.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Desenvolvimento Muscular/genética
Mioblastos/metabolismo
Óxido Nítrico/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/antagonistas & inibidores
Aldeído Oxirredutases/genética
Animais
Diferenciação Celular
Fusão Celular
Embrião de Galinha
AMP Cíclico/metabolismo
AMP Cíclico/farmacologia
GMP Cíclico/análogos & derivados
GMP Cíclico/farmacologia
Cisteína/análogos & derivados
Cisteína/metabolismo
Cisteína/farmacologia
Inibidores Enzimáticos/farmacologia
Fibroblastos/citologia
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Desenvolvimento Muscular/efeitos dos fármacos
Fibras Musculares Esqueléticas/citologia
Fibras Musculares Esqueléticas/efeitos dos fármacos
Fibras Musculares Esqueléticas/metabolismo
Mioblastos/citologia
Mioblastos/efeitos dos fármacos
Óxido Nítrico Sintase Tipo II/genética
Óxido Nítrico Sintase Tipo II/metabolismo
Cultura Primária de Células
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
S-Nitrosoglutationa/metabolismo
S-Nitrosotióis/metabolismo
S-Nitrosotióis/farmacologia
Transdução de Sinais
Guanilil Ciclase Solúvel/genética
Guanilil Ciclase Solúvel/metabolismo
Guanilil Ciclase Solúvel/farmacologia
Tionucleotídeos/farmacologia
Triazenos/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-hydroxy-2-oxo-3,3-bis(2-aminoethyl)-1-triazene); 0 (Enzyme Inhibitors); 0 (RNA, Small Interfering); 0 (S-Nitrosothiols); 0 (Thionucleotides); 0 (Triazenes); 150418-07-8 (8-bromoguanosino-3',5'-cyclic monophosphorothioate); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); 926P2322P4 (S-nitrosocysteine); E0399OZS9N (Cyclic AMP); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); EC 4.6.1.2 (Soluble Guanylyl Cyclase); H2D2X058MU (Cyclic GMP); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170407
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00140.2016



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