Base de dados : MEDLINE
Pesquisa : D08.244.187 [Categoria DeCS]
Referências encontradas : 4092 [refinar]
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[PMID]:28893506
[Au] Autor:Cheng F; Fransson LÅ; Mani K
[Ad] Endereço:Department of Experimental Medical Science, Division of Neuroscience, Glycobiology Group, Lund University, Biomedical Center A13, SE-221 84, Lund, Sweden.
[Ti] Título:Cytochrome b561, copper, ß-cleaved amyloid precursor protein and niemann-pick C1 protein are involved in ascorbate-induced release and membrane penetration of heparan sulfate from endosomal S-nitrosylated glypican-1.
[So] Source:Exp Cell Res;360(2):171-179, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ascorbate-induced release of heparan sulfate from S-nitrosylated heparan sulfate proteoglycan glypican-1 takes place in endosomes. Heparan sulfate penetrates the membrane and is transported to the nucleus. This process is dependent on copper and on expression and processing of the amyloid precursor protein. It remains unclear how exogenously supplied ascorbate can generate HS-anMan in endosomes and how passage through the membrane is facilitated. Here we have examined wild-type, Alzheimer Tg2576 and amyloid precursor protein (-/-) mouse fibroblasts and human fetal and Niemann-Pick C1 fibroblasts by using deconvolution immunofluorescence microscopy, siRNA technology and [S ]sulfate-labeling, vesicle isolation and gel chromatography. We found that ascorbate-induced release of heparan sulfate was dependent on expression of endosomal cytochrome b561. Formation and nuclear transport of heparan sulfate was suppressed by inhibition of ß-processing of the amyloid precursor protein and formation was restored by copper (I) ions. Membrane penetration was not dependent on amyloid beta channel formation. Inhibition of endosomal exit resulted in accumulation of heparan sulfate in vesicles that exposed the C-terminal of the amyloid precursor protein externally. Endosome-to-nucleus transport was also dependent on expression of the Niemann-Pick C1 protein. We propose that ascorbate is taken up from the medium and is oxidized by cytochrome b561 which, in turn, reduces copper (II) to copper (I) present in the N-terminal, ß-cleaved domain of the amyloid precursor protein. Re-oxidation of copper (I) is coupled to reductive, deaminative release of heparan sulfate from glypican-1. Passage through the membrane may be facilitated by the C-terminal, ß-cleaved fragment of the amyloid precursor protein and the Niemann-Pick C1 protein.
[Mh] Termos MeSH primário: Precursor de Proteína beta-Amiloide/fisiologia
Ácido Ascórbico/farmacologia
Proteínas de Transporte/fisiologia
Cobre/fisiologia
Grupo dos Citocromos b/fisiologia
Endossomos/metabolismo
Glipicanas/metabolismo
Glicoproteínas de Membrana/fisiologia
[Mh] Termos MeSH secundário: Precursor de Proteína beta-Amiloide/metabolismo
Animais
Células Cultivadas
Endossomos/efeitos dos fármacos
Heparitina Sulfato
Seres Humanos
Membranas/efeitos dos fármacos
Membranas/metabolismo
Camundongos
Camundongos Transgênicos
Nitrosação
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Protein Precursor); 0 (Carrier Proteins); 0 (Cytochrome b Group); 0 (Glypicans); 0 (Membrane Glycoproteins); 0 (NPC1 protein, human); 11130-51-1 (cytochrome b561); 789U1901C5 (Copper); 9050-30-0 (Heparitin Sulfate); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE


  2 / 4092 MEDLINE  
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[PMID]:28554542
[Au] Autor:Trost P; Picco C; Scholz-Starke J; Festa M; Lagostena L; Costa A; Sparla F; Carpaneto A
[Ad] Endereço:Department of Pharmacy and Biotechnology (FaBiT), University of Bologna, Via Irnerio 42, 40126 Bologna, Italy.
[Ti] Título:Electron current recordings in living cells.
[So] Source:Biophys Chem;229:57-61, 2017 Oct.
[Is] ISSN:1873-4200
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Living cells exploit the electrical properties of matter for a multitude of fundamental physiological processes, such as accumulation of nutrients, cellular homeostasis, signal transmission. While ion channels and transporters (able to couple ions to various substrates) have been extensively studied, direct measurements of electron currents mediated by specific proteins are just at the beginning. Here, we present the various electrophysiological approaches that have allowed recordings of electron currents and highlight the future potential of such experiments.
[Mh] Termos MeSH primário: Fenômenos Eletrofisiológicos
Xenopus/fisiologia
[Mh] Termos MeSH secundário: Animais
Grupo dos Citocromos b/genética
Grupo dos Citocromos b/metabolismo
Elétrons
Ferricianetos/química
Íons/química
Íons/metabolismo
NADPH Oxidases/genética
NADPH Oxidases/metabolismo
Oócitos/fisiologia
Técnicas de Patch-Clamp
Xenopus/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome b Group); 0 (Ferricyanides); 0 (Ions); 11130-51-1 (cytochrome b561); 13408-62-3 (hexacyanoferrate III); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170531
[St] Status:MEDLINE


  3 / 4092 MEDLINE  
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[PMID]:28351984
[Au] Autor:Thomas DC; Clare S; Sowerby JM; Pardo M; Juss JK; Goulding DA; van der Weyden L; Storisteanu D; Prakash A; Espéli M; Flint S; Lee JC; Hoenderdos K; Kane L; Harcourt K; Mukhopadhyay S; Umrania Y; Antrobus R; Nathan JA; Adams DJ; Bateman A; Choudhary JS; Lyons PA; Condliffe AM; Chilvers ER; Dougan G; Smith KG
[Ad] Endereço:Department of Medicine, University of Cambridge, University of Cambridge School of Clinical Medicine, Cambridge CB2 0QQ, England, UK.
[Ti] Título:Eros is a novel transmembrane protein that controls the phagocyte respiratory burst and is essential for innate immunity.
[So] Source:J Exp Med;214(4):1111-1128, 2017 Apr 03.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The phagocyte respiratory burst is crucial for innate immunity. The transfer of electrons to oxygen is mediated by a membrane-bound heterodimer, comprising gp91 and p22 subunits. Deficiency of either subunit leads to severe immunodeficiency. We describe Eros (essential for reactive oxygen species), a protein encoded by the previously undefined mouse gene , and show that it is essential for host defense via the phagocyte NAPDH oxidase. Eros is required for expression of the NADPH oxidase components, gp91 and p22 Consequently, -deficient mice quickly succumb to infection. also contributes to the formation of neutrophil extracellular traps (NETS) and impacts on the immune response to melanoma metastases. is an ortholog of the plant protein Ycf4, which is necessary for expression of proteins of the photosynthetic photosystem 1 complex, itself also an NADPH oxio-reductase. We thus describe the key role of the previously uncharacterized protein Eros in host defense.
[Mh] Termos MeSH primário: Proteínas de Membrana/fisiologia
Fagócitos/fisiologia
Espécies Reativas de Oxigênio/metabolismo
Explosão Respiratória/fisiologia
[Mh] Termos MeSH secundário: Animais
Grupo dos Citocromos b/análise
Grupo dos Citocromos b/fisiologia
Retículo Endoplasmático/metabolismo
Células HEK293
Seres Humanos
Imunidade Inata
Macrófagos/imunologia
Glicoproteínas de Membrana/análise
Glicoproteínas de Membrana/fisiologia
Camundongos
Camundongos Endogâmicos C57BL
NADPH Oxidase 2
NADPH Oxidases/análise
NADPH Oxidases/fisiologia
Neutrófilos/imunologia
Fagocitose
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome b Group); 0 (Eros protein, mouse); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (Reactive Oxygen Species); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (p22(phox) protein, mouse)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20161382


  4 / 4092 MEDLINE  
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[PMID]:28316240
[Au] Autor:Hanna DA; Martinez-Guzman O; Reddi AR
[Ad] Endereço:School of Chemistry and Biochemistry and Parker H. Petit Institute for Bioengineering and Biosciences, Georgia Institute of Technology , Atlanta, Georgia 30332, United States.
[Ti] Título:Heme Gazing: Illuminating Eukaryotic Heme Trafficking, Dynamics, and Signaling with Fluorescent Heme Sensors.
[So] Source:Biochemistry;56(13):1815-1823, 2017 Apr 04.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heme (iron protoporphyrin IX) is an essential protein prosthetic group and signaling molecule required for most life on Earth. All heme-dependent processes require the dynamic and rapid mobilization of heme from sites of synthesis or uptake to hemoproteins present in virtually every subcellular compartment. The cytotoxicity and hydrophobicity of heme necessitate that heme mobilization be carefully controlled to mitigate the deleterious effects of this essential toxin. Indeed, a number of disorders, including certain cancers, cardiovascular diseases, and aging and age-related neurodegenerative diseases, are tied to defects in heme homeostasis. However, the molecules and mechanisms that mediate heme transport and trafficking, and the dynamics of these processes, are poorly understood. This is in large part due to the lack of physical tools for probing cellular heme. Herein, we discuss the recent development of fluorescent probes that can monitor and image kinetically labile heme with respect to its mobilization and role in signaling. In particular, we will highlight how heme gazing with these tools can uncover new heme trafficking factors upon being integrated with genetic screens and illuminate the concentration, subcellular distribution, and dynamics of labile heme in various physiological contexts. Altogether, the monitoring of labile heme, along with recent biochemical and cell biological studies demonstrating the reversible regulation of certain cellular processes by heme, is challenging us to reconceptualize heme from being a static cofactor buried in protein active sites to a dynamic and mobile signaling molecule.
[Mh] Termos MeSH primário: Grupo dos Citocromos b/química
Proteínas de Escherichia coli/química
Corantes Fluorescentes/química
Heme/química
Chaperonas Moleculares/química
Proteínas Recombinantes de Fusão/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Transporte Biológico
Linhagem Celular
Grupo dos Citocromos b/genética
Grupo dos Citocromos b/metabolismo
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Transferência Ressonante de Energia de Fluorescência
Corantes Fluorescentes/metabolismo
Expressão Gênica
Genes Reporter
Proteínas de Fluorescência Verde/química
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Heme/metabolismo
Seres Humanos
Proteínas Luminescentes/química
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Modelos Moleculares
Chaperonas Moleculares/genética
Chaperonas Moleculares/metabolismo
Estrutura Secundária de Proteína
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytochrome b Group); 0 (Escherichia coli Proteins); 0 (Fluorescent Dyes); 0 (Luminescent Proteins); 0 (Molecular Chaperones); 0 (Recombinant Fusion Proteins); 0 (yellow fluorescent protein, Bacteria); 147336-22-9 (Green Fluorescent Proteins); 42VZT0U6YR (Heme); 9064-79-3 (cytochrome b562, E coli)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171008
[Lr] Data última revisão:
171008
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170321
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00007


  5 / 4092 MEDLINE  
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[PMID]:28270217
[Au] Autor:Lemler DJ; Lynch ML; Tesfay L; Deng Z; Paul BT; Wang X; Hegde P; Manz DH; Torti SV; Torti FM
[Ad] Endereço:Department of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT, 06030, USA.
[Ti] Título:DCYTB is a predictor of outcome in breast cancer that functions via iron-independent mechanisms.
[So] Source:Breast Cancer Res;19(1):25, 2017 Mar 07.
[Is] ISSN:1465-542X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Duodenal cytochrome b (DCYTB) is a ferrireductase that functions together with divalent metal transporter 1 (DMT1) to mediate dietary iron reduction and uptake in the duodenum. DCYTB is also a member of a 16-gene iron regulatory gene signature (IRGS) that predicts metastasis-free survival in breast cancer patients. To better understand the relationship between DCYTB and breast cancer, we explored in detail the prognostic significance and molecular function of DCYTB in breast cancer. METHODS: The prognostic significance of DCYTB expression was evaluated using publicly available microarray data. Signaling Pathway Impact Analysis (SPIA) of microarray data was used to identify potential novel functions of DCYTB. The role of DCYTB was assessed using immunohistochemistry and measurements of iron uptake, iron metabolism, and FAK signaling. RESULTS: High DCYTB expression was associated with prolonged survival in two large independent cohorts, together totaling 1610 patients (cohort #1, p = 1.6e-11, n = 741; cohort #2, p = 1.2e-05, n = 869; log-rank test) as well as in the Gene expression-based Outcome for Breast cancer Online (GOBO) cohort (p < 1.0e-05, n = 1379). High DCYTB expression was also associated with increased survival in homogeneously treated groups of patients who received either tamoxifen or chemotherapy. Immunohistochemistry revealed that DCYTB is localized on the plasma membrane of breast epithelial cells, and that expression is dramatically reduced in high-grade tumors. Surprisingly, neither overexpression nor knockdown of DCYTB affected levels of ferritin H, transferrin receptor, labile iron or total cellular iron in breast cancer cells. Because SPIA pathway analysis of patient microarray data revealed an association between DCYTB and the focal adhesion pathway, we examined the influence of DCYTB on FAK activation in breast cancer cells. These experiments reveal that DCYTB reduces adhesion and activation of focal adhesion kinase (FAK) and its adapter protein paxillin. CONCLUSIONS: DCYTB is an important predictor of outcome and is associated with response to therapy in breast cancer patients. DCYTB does not affect intracellular iron in breast cancer cells. Instead, DCYTB may retard cancer progression by reducing activation of FAK, a kinase that plays a central role in tumor cell adhesion and metastasis.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Neoplasias da Mama/mortalidade
Grupo dos Citocromos b/metabolismo
Ferro/metabolismo
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Biomarcadores Tumorais
Neoplasias da Mama/patologia
Neoplasias da Mama/terapia
Adesão Celular/genética
Grupo dos Citocromos b/genética
Bases de Dados Genéticas
Feminino
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Expressão Gênica
Técnicas de Silenciamento de Genes
Seres Humanos
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Metástase Neoplásica
Estadiamento de Neoplasias
Oxirredutases/genética
Prognóstico
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (Cytochrome b Group); E1UOL152H7 (Iron); EC 1.- (Oxidoreductases); EC 1.6.99.- (CYBRD1 protein, human); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1186/s13058-017-0814-9


  6 / 4092 MEDLINE  
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[PMID]:28213559
[Au] Autor:Hackett JB; Shi X; Kobylarz AT; Lucas MK; Wessendorf RL; Hines KM; Bentolila S; Hanson MR; Lu Y
[Ad] Endereço:Department of Biological Sciences, Western Michigan University, Kalamazoo, Michigan 49008-5410 (J.B.H., A.T.K., M.K.L., R.L.W., Y.L.); and.
[Ti] Título:An Organelle RNA Recognition Motif Protein Is Required for Photosystem II Subunit Transcript Editing.
[So] Source:Plant Physiol;173(4):2278-2293, 2017 Apr.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Loss-of-function mutations in ORGANELLE RNA RECOGNITION MOTIF PROTEIN6 (ORRM6) result in the near absence of RNA editing of -C77 and the reduction in -C794 editing in Arabidopsis ( ). The mutants have decreased levels of photosystem II (PSII) proteins, especially PsbF, lower PSII activity, pale green pigmentation, smaller leaf and plant sizes, and retarded growth. Stable expression of rescues the editing defects and mutant phenotype. Unlike ORRM1, the other known ORRM plastid editing factor, ORRM6, does not contain RNA editing interacting protein/multiple organellar RNA editing factor (RIP/MORF) boxes, which are required for ORRM1 to interact with site-specific pentatricopeptide repeat protein editing factors. ORRM6 interacts with RIP1/MORF8, RIP2/MORF2, and RIP9/MORF9, known components of RNA editosomes. While some plastid RRM proteins are involved in other forms of RNA processing and translation, the primary function of ORRM6 is evidently to mediate -C77 editing, like the essential site-specific pentatricopeptide repeat protein LOW PSII ACCUMULATION66. Stable expression in the mutants of a nucleus-encoded, plastid-targeted PsbF protein from a gene carrying a T at nucleotide 77 significantly increases leaf and plant sizes, chlorophyll content, and PSII activity. These transformants demonstrate that plastid RNA editing can be bypassed through the expression of nucleus-encoded, edited forms of plastid genes.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Grupo dos Citocromos b/metabolismo
Organelas/metabolismo
Complexo de Proteína do Fotossistema II/metabolismo
Edição de RNA
Proteínas com Motivo de Reconhecimento de RNA/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/metabolismo
Proteínas de Arabidopsis/genética
Núcleo Celular/genética
Núcleo Celular/metabolismo
Clorofila/metabolismo
Grupo dos Citocromos b/genética
Regulação da Expressão Gênica de Plantas
Immunoblotting
Mutação
Organelas/genética
Fenótipo
Fotossíntese/genética
Complexo de Proteína do Fotossistema II/genética
Plantas Geneticamente Modificadas
Plastídeos/genética
Plastídeos/metabolismo
Ligação Proteica
Proteínas com Motivo de Reconhecimento de RNA/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cytochrome b Group); 0 (ORRM6 protein, Arabidopsis); 0 (Photosystem II Protein Complex); 0 (RNA Recognition Motif Proteins); 1406-65-1 (Chlorophyll)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170219
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01623


  7 / 4092 MEDLINE  
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[PMID]:28202687
[Au] Autor:Dingjan I; Linders PT; van den Bekerom L; Baranov MV; Halder P; Ter Beest M; van den Bogaart G
[Ad] Endereço:Department of Tumor Immunology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen 6525 GA, The Netherlands.
[Ti] Título:Oxidized phagosomal NOX2 complex is replenished from lysosomes.
[So] Source:J Cell Sci;130(7):1285-1298, 2017 Apr 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In dendritic cells, the NADPH oxidase 2 complex (NOX2) is recruited to the phagosomal membrane during antigen uptake. NOX2 produces reactive oxygen species (ROS) in the lumen of the phagosome that kill ingested pathogens, delay antigen breakdown and alter the peptide repertoire for presentation to T cells. How the integral membrane component of NOX2, cytochrome (which comprises CYBB and CYBA), traffics to phagosomes is incompletely understood. In this study, we show in dendritic cells derived from human blood-isolated monocytes that cytochrome is initially recruited to the phagosome from the plasma membrane during phagosome formation. Cytochrome also traffics from a lysosomal pool to phagosomes and this is required to replenish oxidatively damaged NOX2. We identified syntaxin-7, SNAP23 and VAMP8 as the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediating this process. Our data describe a key mechanism of how dendritic cells sustain ROS production after antigen uptake that is required to initiate T cell responses.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Fagossomos/metabolismo
[Mh] Termos MeSH secundário: Compartimento Celular
Membrana Celular/metabolismo
Grupo dos Citocromos b/metabolismo
Endossomos/metabolismo
Técnicas de Silenciamento de Genes
Seres Humanos
Membranas Intracelulares/metabolismo
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Modelos Biológicos
NADPH Oxidase 2
Oxirredução
Fosfatidilinositóis/metabolismo
Proteínas Qa-SNARE
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Proteínas R-SNARE/metabolismo
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome b Group); 0 (Lysosomal-Associated Membrane Protein 1); 0 (Membrane Glycoproteins); 0 (Phosphatidylinositols); 0 (Qa-SNARE Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (R-SNARE Proteins); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (SNAP23 protein, human); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (VAMP8 protein, human); 9064-78-2 (cytochrome b558); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[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:170217
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.196931


  8 / 4092 MEDLINE  
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[PMID]:28060867
[Au] Autor:Khare G; Nangpal P; Tyagi AK
[Ad] Endereço:Department of Biochemistry, University of Delhi South Campus, Benito Juarez Road, New Delhi, India.
[Ti] Título:Differential Roles of Iron Storage Proteins in Maintaining the Iron Homeostasis in Mycobacterium tuberculosis.
[So] Source:PLoS One;12(1):e0169545, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ferritins and bacterioferritins are iron storage proteins that represent key players in iron homeostasis. Several organisms possess both forms of ferritins, however, their relative physiological roles are less understood. Mycobacterium tuberculosis possesses both ferritin (BfrB) and bacterioferritin (BfrA), playing an essential role in its pathogenesis as reported by us earlier. This study provides insights into the role of these two proteins in iron homeostasis by employing M. tuberculosis bfr mutants. Our data suggests that BfrA is required for efficient utilization of stored iron under low iron conditions while BfrB plays a crucial role as the major defense protein under excessive iron conditions. We show that these two proteins provide protection against oxidative stress and hypoxia. Iron incorporation study showed that BfrB has higher capacity for storing iron than BfrA, which augurs well for efficient iron quenching under iron excess conditions. Moreover, iron release assay demonstrated that BfrA has 3 times superior ability to release stored iron emphasizing its requirement for efficient iron release under low iron conditions, facilitated by the presence of heme. Thus, for the first time, our observations suggest that the importance of BfrA or BfrB separately might vary depending upon the iron situation faced by the cell.
[Mh] Termos MeSH primário: Homeostase
Proteínas de Ligação ao Ferro/metabolismo
Ferro/metabolismo
Mycobacterium tuberculosis/metabolismo
Tuberculose/metabolismo
Tuberculose/microbiologia
[Mh] Termos MeSH secundário: Proteínas da Membrana Bacteriana Externa/metabolismo
Proteínas de Bactérias/metabolismo
Grupo dos Citocromos b/metabolismo
Ferritinas/metabolismo
Hipóxia/metabolismo
Proteínas de Ligação ao Ferro/genética
Mycobacterium tuberculosis/genética
Estresse Oxidativo
Estresse Fisiológico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (Cytochrome b Group); 0 (Iron-Binding Proteins); 9007-73-2 (Ferritins); 9035-38-5 (bacterioferritin); E1UOL152H7 (Iron)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170107
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0169545


  9 / 4092 MEDLINE  
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[PMID]:28032259
[Au] Autor:Biniek C; Heyno E; Kruk J; Sparla F; Trost P; Krieger-Liszkay A
[Ad] Endereço:Institut de Biologie Intégrative de la Cellule (I2BC), IBITECS, CEA, CNRS, Univ Paris-Sud, Université Paris-Saclay, 91198, Gif-sur-Yvette, France.
[Ti] Título:Role of the NAD(P)H quinone oxidoreductase NQR and the cytochrome b AIR12 in controlling superoxide generation at the plasma membrane.
[So] Source:Planta;245(4):807-817, 2017 Apr.
[Is] ISSN:1432-2048
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:MAIN CONCLUSION: The quinone reductase NQR and the b-type cytochrome AIR12 of the plasma membrane are important for the control of reactive oxygen species in the apoplast. AIR12 and NQR are two proteins attached to the plant plasma membrane which may be important for generating and controlling levels of reactive oxygen species in the apoplast. AIR12 (Auxin Induced in Root culture) is a single gene of Arabidopsis that codes for a mono-heme cytochrome b. The NADPH quinone oxidoreductase NQR is a two-electron-transferring flavoenzyme that contributes to the generation of O in isolated plasma membranes. A. thaliana double knockout plants of both NQR and AIR12 generated more O and germinated faster than the single mutant affected in AIR12. To test whether NQR and AIR12 are able to interact functionally, recombinant purified proteins were added to plasma membranes isolated from soybean hypocotyls. In vitro NADH-dependent O production at the plasma membrane in the presence of NQR was reduced upon addition of AIR12. Electron donation from semi-reduced menadione to AIR12 was shown to take place. Biochemical analysis showed that purified plasma membrane from soybean hypocotyls or roots contained phylloquinone and menaquinone-4 as redox carriers. This is the first report on the occurrence of menaquinone-4 in eukaryotic photosynthetic organisms. We propose that NQR and AIR12 interact via the quinone, allowing an electron transfer from cytosolic NAD(P)H to apoplastic monodehydroascorbate and control thereby the level of reactive oxygen production and the redox state of the apoplast.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Membrana Celular/metabolismo
Grupo dos Citocromos b/metabolismo
NAD(P)H Desidrogenase (Quinona)/metabolismo
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Arabidopsis/metabolismo
Arabidopsis/fisiologia
Proteínas de Arabidopsis/fisiologia
Linhagem Celular
Membrana Celular/enzimologia
Grupo dos Citocromos b/fisiologia
Técnicas de Silenciamento de Genes
Germinação/fisiologia
NAD(P)H Desidrogenase (Quinona)/fisiologia
Oxirredução
Espécies Reativas de Oxigênio/metabolismo
Feijão de Soja/metabolismo
Feijão de Soja/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AIR12 protein, Arabidopsis); 0 (Arabidopsis Proteins); 0 (Cytochrome b Group); 0 (Reactive Oxygen Species); 11062-77-4 (Superoxides); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161230
[St] Status:MEDLINE
[do] DOI:10.1007/s00425-016-2643-y


  10 / 4092 MEDLINE  
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[PMID]:28026953
[Au] Autor:Funatogawa C; Li Y; Chen Y; McDonald W; Szundi I; Fee JA; Stout CD; Einarsdóttir Ó
[Ad] Endereço:Department of Chemistry and Biochemistry, University of California , Santa Cruz, California 95064, United States.
[Ti] Título:Role of the Conserved Valine 236 in Access of Ligands to the Active Site of Thermus thermophilus ba Cytochrome Oxidase.
[So] Source:Biochemistry;56(1):107-119, 2017 Jan 10.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Knowledge of the role of conserved residues in the ligand channel of heme-copper oxidases is critical for understanding how the protein scaffold modulates the function of these enzymes. In this study, we investigated the role of the conserved valine 236 in the ligand channel of ba cytochrome c oxidase from Thermus thermophilus by mutating the residue to a more polar (V236T), smaller (V236A), or larger (V236I, V236N, V236L, V236M, and V236F) residue. The crystal structures of the mutants were determined, and the effects of the mutations on the rates of CO, O , and NO binding were investigated. O reduction and NO binding were unaffected in V236T, while the oxidation of heme b during O-O bond cleavage was not detected in V236A. The V236A results are attributed to a decrease in the rate of electron transfer between heme b and heme a during O-O bond cleavage in V236A, followed by faster re-reduction of heme b by Cu . This interpretation is supported by classical molecular dynamics simulations of diffusion of O to the active site in V236A that indicated a larger distance between the two hemes compared to that in the wild type and increased contact of heme a with water and weakened interactions with residues R444 and R445. As the size of the mutant side chain increased and protruded more into the ligand cavity, the rates of ligand binding decreased correspondingly. These results demonstrate the importance of V236 in facilitating access of ligands to the active site in T. thermophilus ba .
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Grupo dos Citocromos b/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Thermus thermophilus/enzimologia
Valina/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sítios de Ligação/genética
Monóxido de Carbono/química
Monóxido de Carbono/metabolismo
Domínio Catalítico
Cristalização
Cristalografia por Raios X
Grupo dos Citocromos b/química
Grupo dos Citocromos b/genética
Complexo IV da Cadeia de Transporte de Elétrons/química
Complexo IV da Cadeia de Transporte de Elétrons/genética
Heme/química
Heme/metabolismo
Cinética
Ligantes
Simulação de Dinâmica Molecular
Mutação de Sentido Incorreto
Óxido Nítrico/química
Óxido Nítrico/metabolismo
Oxirredução
Oxigênio/química
Oxigênio/metabolismo
Ligação Proteica
Domínios Proteicos
Espectrofotometria
Thermus thermophilus/genética
Valina/química
Valina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cytochrome b Group); 0 (Ligands); 31C4KY9ESH (Nitric Oxide); 42VZT0U6YR (Heme); 7U1EE4V452 (Carbon Monoxide); EC 1.- (cytochrome ba3); EC 1.9.3.1 (Electron Transport Complex IV); HG18B9YRS7 (Valine); S88TT14065 (Oxygen)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00590



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