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[PMID]:29320567
[Au] Autor:Gil-Cayuela C; Ortega A; Tarazón E; Martínez-Dolz L; Cinca J; González-Juanatey JR; Lago F; Roselló-Lletí E; Rivera M; Portolés M
[Ad] Endereço:Cardiocirculatory Unit, Health Research Institute of La Fe University Hospital (IIS La Fe), Valencia, Spain.
[Ti] Título:Myocardium of patients with dilated cardiomyopathy presents altered expression of genes involved in thyroid hormone biosynthesis.
[So] Source:PLoS One;13(1):e0190987, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The association between dilated cardiomyopathy (DCM) and low thyroid hormone (TH) levels has been previously described. In these patients abnormal thyroid function is significantly related to impaired left ventricular (LV) function and increased risk of death. Although TH was originally thought to be produced exclusively by the thyroid gland, we recently reported TH biosynthesis in the human ischemic heart. OBJECTIVES: Based on these findings, we evaluated whether the genes required for TH production are also altered in patients with DCM. METHODS: Twenty-three LV tissue samples were obtained from patients with DCM (n = 13) undergoing heart transplantation and control donors (n = 10), and used for RNA sequencing analysis. The number of LV DCM samples was increased to 23 to determine total T4 and T3 tissue levels by ELISA. RESULTS: We found that all components of TH biosynthesis are expressed in human dilated heart tissue. Expression of genes encoding thyroperoxidase (-2.57-fold, P < 0.05) and dual oxidase 2 (2.64-fold, P < 0.01), the main enzymatic system of TH production, was significantly altered in patients with DCM and significantly associated with LV remodeling parameters. Thyroxine (T4) cardiac tissue levels were significantly increased (P < 0.01), whilst triiodothyronine (T3) levels were significantly diminished (P < 0.05) in the patients. CONCLUSIONS: Expression of TH biosynthesis machinery in the heart and total tissue levels of T4 and T3, are altered in patients with DCM. Given the relevance of TH in cardiac pathology, our results provide a basis for new gene-based therapeutic strategies for treating DCM.
[Mh] Termos MeSH primário: Autoantígenos/genética
Cardiomiopatia Dilatada/genética
Oxidases Duais/genética
Iodeto Peroxidase/genética
Proteínas de Ligação ao Ferro/genética
Miocárdio/metabolismo
Receptores da Tireotropina/genética
Hormônios Tireóideos/biossíntese
[Mh] Termos MeSH secundário: Autoantígenos/metabolismo
Biomarcadores/metabolismo
Cardiomiopatia Dilatada/patologia
Estudos de Casos e Controles
Oxidases Duais/metabolismo
Feminino
Perfilação da Expressão Gênica
Regulação da Expressão Gênica
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Seres Humanos
Iodeto Peroxidase/metabolismo
Proteínas de Ligação ao Ferro/metabolismo
Masculino
Meia-Idade
Receptores da Tireotropina/metabolismo
Remodelação Ventricular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (Biomarkers); 0 (Iron-Binding Proteins); 0 (Receptors, Thyrotropin); 0 (Thyroid Hormones); EC 1.11.1.- (Dual Oxidases); EC 1.11.1.7 (TPO protein, human); EC 1.11.1.8 (Iodide Peroxidase); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190987


  2 / 2249 MEDLINE  
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[PMID]:28456899
[Au] Autor:Kemp K; Dey R; Cook A; Scolding N; Wilkins A
[Ad] Endereço:Multiple Sclerosis and Stem Cell Group, School of Clinical Sciences, Clinical Neurosciences office, University of Bristol, 1st floor, Learning and Research building, Southmead Hospital, Bristol, BS10 5NB, UK. kevin.kemp@bristol.ac.uk.
[Ti] Título:Mesenchymal Stem Cell-Derived Factors Restore Function to Human Frataxin-Deficient Cells.
[So] Source:Cerebellum;16(4):840-851, 2017 Aug.
[Is] ISSN:1473-4230
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Friedreich's ataxia is an inherited neurological disorder characterised by mitochondrial dysfunction and increased susceptibility to oxidative stress. At present, no therapy has been shown to reduce disease progression. Strategies being trialled to treat Friedreich's ataxia include drugs that improve mitochondrial function and reduce oxidative injury. In addition, stem cells have been investigated as a potential therapeutic approach. We have used siRNA-induced knockdown of frataxin in SH-SY5Y cells as an in vitro cellular model for Friedreich's ataxia. Knockdown of frataxin protein expression to levels detected in patients with the disorder was achieved, leading to decreased cellular viability, increased susceptibility to hydrogen peroxide-induced oxidative stress, dysregulation of key anti-oxidant molecules and deficiencies in both cell proliferation and differentiation. Bone marrow stem cells are being investigated extensively as potential treatments for a wide range of neurological disorders, including Friedreich's ataxia. The potential neuroprotective effects of bone marrow-derived mesenchymal stem cells were therefore studied using our frataxin-deficient cell model. Soluble factors secreted by mesenchymal stem cells protected against cellular changes induced by frataxin deficiency, leading to restoration in frataxin levels and anti-oxidant defences, improved survival against oxidative stress and stimulated both cell proliferation and differentiation down the Schwann cell lineage. The demonstration that mesenchymal stem cell-derived factors can restore cellular homeostasis and function to frataxin-deficient cells further suggests that they may have potential therapeutic benefits for patients with Friedreich's ataxia.
[Mh] Termos MeSH primário: Ataxia de Friedreich/metabolismo
Proteínas de Ligação ao Ferro/metabolismo
Células Mesenquimais Estromais/metabolismo
[Mh] Termos MeSH secundário: Diferenciação Celular/fisiologia
Linhagem Celular Tumoral
Proliferação Celular/fisiologia
Sobrevivência Celular/fisiologia
Fêmur
Técnicas de Silenciamento de Genes
Homeostase/fisiologia
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Proteínas de Ligação ao Ferro/genética
Óxido Nítrico/metabolismo
Estresse Oxidativo/fisiologia
RNA Interferente Pequeno
Células de Schwann/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Binding Proteins); 0 (RNA, Small Interfering); 0 (frataxin); 31C4KY9ESH (Nitric Oxide); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/s12311-017-0860-y


  3 / 2249 MEDLINE  
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[PMID]:29261783
[Au] Autor:Long A; Napierala JS; Polak U; Hauser L; Koeppen AH; Lynch DR; Napierala M
[Ad] Endereço:Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama, United States of America.
[Ti] Título:Somatic instability of the expanded GAA repeats in Friedreich's ataxia.
[So] Source:PLoS One;12(12):e0189990, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Friedreich's ataxia (FRDA) is a genetic neurodegenerative disorder caused by transcriptional silencing of the frataxin gene (FXN) due to expansions of GAA repeats in intron 1. FRDA manifests with multiple symptoms, which may include ataxia, cardiomyopathy and diabetes mellitus. Expanded GAA tracts are genetically unstable, exhibiting both expansions and contractions. GAA length correlates with severity of FRDA symptoms and inversely with age of onset. Thus, tissue-specific somatic instability of long GAA repeats may be implicated in the development of symptoms and disease progression. Herein, we determined the extent of somatic instability of the GAA repeats in heart, cerebral cortex, spinal cord, cerebellar cortex, and pancreatic tissues from 15 FRDA patients. Results demonstrate differences in the lengths of the expanded GAAs among different tissues, with significantly longer GAA tracts detected in heart and pancreas than in other tissues. The expansion bias detected in heart and pancreas may contribute to disease onset and progression, making the mechanism of somatic instability an important target for therapy. Additionally, we detected significant differences in GAA tract lengths between lymphocytes and fibroblast pairs derived from 16 FRDA patients, with longer GAA tracts present in the lymphocytes. This result urges caution in direct comparisons of data obtained in these frequently used FRDA models. Furthermore, we conducted a longitudinal analysis of the GAA repeat length in lymphocytes collected over a span of 7-9 years and demonstrated progressive expansions of the GAAs with maximum gain of approximately 9 repeats per year. Continuous GAA expansions throughout the patient's lifespan, as observed in FRDA lymphocytes, should be considered in clinical trial designs and data interpretation.
[Mh] Termos MeSH primário: Ataxia de Friedreich/genética
Instabilidade Genômica
Expansão das Repetições de Trinucleotídeos/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Pré-Escolar
Feminino
Fibroblastos/metabolismo
Fibroblastos/patologia
Seres Humanos
Proteínas de Ligação ao Ferro/genética
Estudos Longitudinais
Linfócitos/metabolismo
Masculino
Fatores de Tempo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Binding Proteins); 0 (frataxin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171221
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189990


  4 / 2249 MEDLINE  
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[PMID]:29200434
[Au] Autor:Ahlgren EC; Fekry M; Wiemann M; Söderberg CA; Bernfur K; Gakh O; Rasmussen M; Højrup P; Emanuelsson C; Isaya G; Al-Karadaghi S
[Ad] Endereço:Center for Molecular Protein Science, Department of Biochemistry and Structural Biology, Lund University, Lund, Sweden.
[Ti] Título:Iron-induced oligomerization of human FXN81-210 and bacterial CyaY frataxin and the effect of iron chelators.
[So] Source:PLoS One;12(12):e0188937, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Patients suffering from the progressive neurodegenerative disease Friedreich's ataxia have reduced expression levels of the protein frataxin. Three major isoforms of human frataxin have been identified, FXN42-210, FXN56-210 and FXN81-210, of which FXN81-210 is considered to be the mature form. Both long forms, FXN42-210 and FXN56-210, have been shown to spontaneously form oligomeric particles stabilized by the extended N-terminal sequence. The short variant FXN81-210, on other hand, has only been observed in the monomeric state. However, a highly homologous E. coli frataxin CyaY, which also lacks an N-terminal extension, has been shown to oligomerize in the presence of iron. To explore the mechanisms of stabilization of short variant frataxin oligomers we compare here the effect of iron on the oligomerization of CyaY and FXN81-210. Using dynamic light scattering, small-angle X-ray scattering, electron microscopy (EM) and cross linking mass spectrometry (MS), we show that at aerobic conditions in the presence of iron both FXN81-210 and CyaY form oligomers. However, while CyaY oligomers are stable over time, FXN81-210 oligomers are unstable and dissociate into monomers after about 24 h. EM and MS studies suggest that within the oligomers FXN81-210 and CyaY monomers are packed in a head-to-tail fashion in ring-shaped structures with potential iron-binding sites located at the interface between monomers. The higher stability of CyaY oligomers can be explained by a higher number of acidic residues at the interface between monomers, which may result in a more stable iron binding. We also show that CyaY oligomers may be dissociated by ferric iron chelators deferiprone and DFO, as well as by the ferrous iron chelator BIPY. Surprisingly, deferiprone and DFO stimulate FXN81-210 oligomerization, while BIPY does not show any effect on oligomerization in this case. The results suggest that FXN81-210 oligomerization is primarily driven by ferric iron, while both ferric and ferrous iron participate in CyaY oligomer stabilization. Analysis of the amino acid sequences of bacterial and eukaryotic frataxins suggests that variations in the position of the acidic residues in helix 1, ß-strand 1 and the loop between them may control the mode of frataxin oligomerization.
[Mh] Termos MeSH primário: Proteínas de Escherichia coli/metabolismo
Quelantes de Ferro/química
Proteínas de Ligação ao Ferro/metabolismo
Ferro/química
Multimerização Proteica
[Mh] Termos MeSH secundário: Sítios de Ligação
Reagentes para Ligações Cruzadas
Difusão Dinâmica da Luz
Proteínas de Escherichia coli/ultraestrutura
Ataxia de Friedreich/metabolismo
Seres Humanos
Proteínas de Ligação ao Ferro/ultraestrutura
Espectrometria de Massas
Microscopia Eletrônica
Modelos Moleculares
Isoformas de Proteínas/metabolismo
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/ultraestrutura
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Escherichia coli Proteins); 0 (Iron Chelating Agents); 0 (Iron-Binding Proteins); 0 (Protein Isoforms); 0 (Recombinant Proteins); 0 (frataxin); E1UOL152H7 (Iron)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188937


  5 / 2249 MEDLINE  
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[PMID]:27771440
[Au] Autor:Marcus D; Lichtenstein M; Cohen N; Hadad R; Erlich-Hadad T; Greif H; Lorberboum-Galski H
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Institute for Medical Research Israel-Canada (IMRIC), Faculty of Medicine, Hebrew University of Jerusalem, Jerusalem 91120, Israel.
[Ti] Título:Heterologous mitochondrial targeting sequences can deliver functional proteins into mitochondria.
[So] Source:Int J Biochem Cell Biol;81(Pt A):48-56, 2016 12.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Mitochondrial Targeting Sequences (MTSs) are responsible for trafficking nuclear-encoded proteins into mitochondria. Once entering the mitochondria, the MTS is recognized and cleaved off. Some MTSs are long and undergo two-step processing, as in the case of the human frataxin (FXN) protein (80aa), implicated in Friedreich's ataxia (FA). Therefore, we chose the FXN protein to examine whether nuclear-encoded mitochondrial proteins can efficiently be targeted via a heterologous MTS (hMTS) and deliver a functional protein into mitochondria. We examined three hMTSs; that of citrate synthase (cs), lipoamide deydrogenase (LAD) and C6ORF66 (ORF), as classically MTS sequences, known to be removed by one-step processing, to deliver FXN into mitochondria, in the form of fusion proteins. We demonstrate that using hMTSs for delivering FXN results in the production of 4-5-fold larger amounts of the fusion proteins, and at 4-5-fold higher concentrations. Moreover, hMTSs delivered a functional FXN protein into the mitochondria even more efficiently than the native MTSfxn, as evidenced by the rescue of FA patients' cells from oxidative stress; demonstrating a 18%-54% increase in cell survival; and a 13%-33% increase in ATP levels, as compared to the fusion protein carrying the native MTS. One fusion protein with MTScs increased aconitase activity within patients' cells, by 400-fold. The implications form our studies are of vast importance for both basic and translational research of mitochondrial proteins as any mitochondrial protein can be delivered efficiently by an hMTS. Moreover, effective targeting of functional proteins is important for restoration of mitochondrial function and treatment of related disorders.
[Mh] Termos MeSH primário: Proteínas de Ligação ao Ferro/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Aconitato Hidratase/metabolismo
Ataxia de Friedreich/metabolismo
Seres Humanos
Estresse Oxidativo
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Binding Proteins); 0 (frataxin); EC 4.2.1.3 (Aconitate Hydratase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171217
[Lr] Data última revisão:
171217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE


  6 / 2249 MEDLINE  
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[PMID]:28911134
[Au] Autor:Korevaar TIM; Steegers EAP; Chaker L; Medici M; Jaddoe VWV; Visser TJ; de Rijke YB; Peeters RP
[Ad] Endereço:The Generation R Study Group, Erasmus Medical Center and/or Sophia Children's Hospital, 3015 GE Rotterdam, The Netherlands.
[Ti] Título:Thyroid Function and Premature Delivery in TPO Antibody-Negative Women: The Added Value of hCG.
[So] Source:J Clin Endocrinol Metab;102(9):3360-3367, 2017 Sep 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: Human chorionic gonadotropin (hCG) stimulates thyroid function during pregnancy. We recently showed that thyroid autoimmunity severely attenuated the thyroidal response to hCG stimulation and that this may underlie the higher risk of premature delivery in thyroperoxidase antibody (TPOAb)-positive women. We hypothesized that a lower thyroidal response to hCG stimulation in TPOAb-negative women is also associated with a higher risk of premature delivery and preterm premature rupture of membranes (pPROM). Design, Setting, and Participants: Thyrotropin (TSH), free thyroxine (FT4), and hCG concentrations were available in 5644 TPOAb-negative women from a prospective cohort. We tested for interaction between TSH or FT4 and hCG in linear regression models for duration of pregnancy and logistic regression models for premature delivery/pPROM. Accordingly, analyses were stratified per TSH percentile (TSH ≥ 85th percentile) and hCG per 10,000 IU/L. Results: Women with high TSH and low hCG concentrations did not have a higher risk of premature delivery or pPROM, with protective effect estimates. In contrast, women with a high TSH concentration despite a high hCG concentration had twofold to 10-fold higher risk of premature delivery (Pdifference = 0.022) and an up to fourfold higher risk of pPROM (Pdifference = 0.079). hCG concentrations were not associated with premature delivery or pPROM. Conclusion: In TPOAb-negative women with high-normal TSH concentrations, only women with high hCG concentrations had a higher risk of premature delivery or pPROM. These results suggest a lower thyroidal response to hCG stimulation is also associated with premature delivery in TPOAb-negative women and that an additional measurement of hCG may improve thyroid-related risk assessments during pregnancy.
[Mh] Termos MeSH primário: Autoantígenos/imunologia
Gonadotropina Coriônica/sangue
Iodeto Peroxidase/imunologia
Proteínas de Ligação ao Ferro/imunologia
Resultado da Gravidez
Nascimento Prematuro/imunologia
Tireotropina/sangue
[Mh] Termos MeSH secundário: Adulto
Biomarcadores/sangue
Estudos de Coortes
Feminino
Idade Gestacional
Seres Humanos
Gravidez
Estudos Prospectivos
Medição de Risco
Testes de Função Tireóidea
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantigens); 0 (Biomarkers); 0 (Chorionic Gonadotropin); 0 (Iron-Binding Proteins); 9002-71-5 (Thyrotropin); EC 1.11.1.7 (TPO protein, human); EC 1.11.1.8 (Iodide Peroxidase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170916
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2017-00846


  7 / 2249 MEDLINE  
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[PMID]:28789479
[Au] Autor:Becker AB; Qian J; Gelman BB; Yang M; Bauer P; Koeppen AH
[Ad] Endereço:Research Service, Veterans Affairs Medical Center, Albany, New York (ABB, AHK); Department of Pathology, Albany Medical Center, Albany, New York (JQ, AHK); Department of Pathology and Laboratory Medicine, University of Texas Medical Branch, Galveston, Texas (BBG); Department of Pediatrics and Neurol
[Ti] Título:Heart and Nervous System Pathology in Compound Heterozygous Friedreich Ataxia.
[So] Source:J Neuropathol Exp Neurol;76(8):665-675, 2017 Aug 01.
[Is] ISSN:1554-6578
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In a small percentage of patients with Friedreich ataxia (FA), the pathogenic mutation is compound heterozygous, consisting of a guanine-adenine-adenine (GAA) trinucleotide repeat expansion in one allele, and a deletion, point mutation, or insertion in the other. In 2 cases of compound heterozygous FA, the GAA expansion was inherited from the mother, and deletions from the father. Compound heterozygous FA patient 1, an 11-year-old boy (GAA, 896/c.11_12TCdel), had ataxia, chorea, cardiomyopathy, and diabetes mellitus. Compound heterozygous FA patient 2, a 28-year-old man (GAA, 744/exon 5 del), had ataxia, cardiomyopathy, and diabetes mellitus. Microscopy showed cardiomyocyte hypertrophy, iron-positive inclusions, and disrupted intercalated discs. The cardiac lesions were similar to those in age-matched homozygous FA patients with cardiomyopathy and diabetes mellitus (boy, 10, GAA 1016/1016; woman, 25, GAA 800/1100). The neuropathology was also similar and included hypoplasia of spinal cord and dorsal root ganglia, loss of large axons in dorsal roots, and atrophy of the dentate nucleus (DN). Frataxin levels in heart and DN of all 4 FA cases were at or below the detection limits of the enzyme-linked immunosorbent assay (≤10 ng/g wet weight) (normal DN: 126 ± 43 ng/g; normal heart: 266 ± 92 ng/g). The pathologic phenotype in homozygous and compound heterozygous FA is determined by residual frataxin levels rather than unique mutations.
[Mh] Termos MeSH primário: Ataxia de Friedreich/patologia
Miocárdio/patologia
Sistema Nervoso/patologia
[Mh] Termos MeSH secundário: Adulto
Criança
Ensaio de Imunoadsorção Enzimática
Ataxia de Friedreich/genética
Heterozigoto
Seres Humanos
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Masculino
Sistema Nervoso/metabolismo
Expansão das Repetições de Trinucleotídeos/genética
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Iron-Binding Proteins); 0 (frataxin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170822
[Lr] Data última revisão:
170822
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.1093/jnen/nlx047


  8 / 2249 MEDLINE  
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[PMID]:28630009
[Au] Autor:Buchensky C; Sánchez M; Carrillo M; Palacios O; Capdevila M; Domínguez-Vera JM; Busi MV; Atrian S; Pagani MA; Gomez-Casati DF
[Ad] Endereço:CEFOBI - CONICET, Centro de Estudios Fotosintéticos y Bioquímicos - Consejo Nacional de Investigaciones Científicas y Técnicas, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.
[Ti] Título:Identification of two frataxin isoforms in Zea mays: Structural and functional studies.
[So] Source:Biochimie;140:34-47, 2017 Sep.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Frataxin is a ubiquitous protein that plays a role in Fe-S cluster biosynthesis and iron and heme metabolism, although its molecular functions are not entirely clear. In non-photosynthetic eukaryotes, frataxin is encoded by a single gene, and the protein localizes to mitochondria. Here we report the presence of two functional frataxin isoforms in Zea mays, ZmFH-1 and ZmFH-2. We confirmed our previous findings regarding plant frataxins: both proteins have dual localization in mitochondria and chloroplasts. Physiological, biochemical and biophysical studies show some differences in the expression pattern, protection against oxidants and in the aggregation state of both isoforms, suggesting that the two frataxin homologs would play similar but not identical roles in plant cell metabolism. In addition, two specific features of plant frataxins were evidenced: their ability to form dimers and their tendency to undergo conformational change under oxygen exposure.
[Mh] Termos MeSH primário: Proteínas de Cloroplastos
Regulação da Expressão Gênica de Plantas/fisiologia
Proteínas de Ligação ao Ferro
Mitocôndrias
Proteínas Mitocondriais
Plastídeos
Zea mays
[Mh] Termos MeSH secundário: Proteínas de Cloroplastos/biossíntese
Proteínas de Cloroplastos/genética
Proteínas de Ligação ao Ferro/biossíntese
Proteínas de Ligação ao Ferro/genética
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Mitocondriais/biossíntese
Proteínas Mitocondriais/genética
Plastídeos/genética
Plastídeos/metabolismo
Isoformas de Proteínas
Zea mays/genética
Zea mays/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chloroplast Proteins); 0 (Iron-Binding Proteins); 0 (Mitochondrial Proteins); 0 (Protein Isoforms); 0 (frataxin)
[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:170621
[St] Status:MEDLINE


  9 / 2249 MEDLINE  
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[PMID]:28615445
[Au] Autor:Braymer JJ; Lill R
[Ad] Endereço:From the Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Robert-Koch-Strasse 6, 35032 Marburg and.
[Ti] Título:Iron-sulfur cluster biogenesis and trafficking in mitochondria.
[So] Source:J Biol Chem;292(31):12754-12763, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The biogenesis of iron-sulfur (Fe/S) proteins in eukaryotes is a multistage, multicompartment process that is essential for a broad range of cellular functions, including genome maintenance, protein translation, energy conversion, and the antiviral response. Genetic and cell biological studies over almost 2 decades have revealed some 30 proteins involved in the synthesis of cellular [2Fe-2S] and [4Fe-4S] clusters and their incorporation into numerous apoproteins. Mechanistic aspects of Fe/S protein biogenesis continue to be elucidated by biochemical and ultrastructural investigations. Here, we review recent developments in the pursuit of constructing a comprehensive model of Fe/S protein assembly in the mitochondrion.
[Mh] Termos MeSH primário: Regulação Enzimológica da Expressão Gênica
Proteínas com Ferro-Enxofre/metabolismo
Mitocôndrias/metabolismo
Modelos Biológicos
Modelos Moleculares
[Mh] Termos MeSH secundário: Proteína de Transporte de Acila/química
Proteína de Transporte de Acila/genética
Proteína de Transporte de Acila/metabolismo
Adrenodoxina/química
Adrenodoxina/genética
Adrenodoxina/metabolismo
Animais
Apoenzimas/química
Apoenzimas/genética
Apoenzimas/metabolismo
Seres Humanos
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/genética
Mitocôndrias/enzimologia
Proteínas Mitocondriais/química
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Conformação Proteica
Dobramento de Proteína
Multimerização Proteica
Transporte Proteico
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Especificidade da Espécie
Sulfurtransferases/química
Sulfurtransferases/genética
Sulfurtransferases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Acyl Carrier Protein); 0 (Apoenzymes); 0 (ISU1 protein, S cerevisiae); 0 (Iron-Binding Proteins); 0 (Iron-Sulfur Proteins); 0 (Isd11 protein, S cerevisiae); 0 (Mitochondrial Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (YAH1 protein, S cerevisiae); 0 (frataxin); 12687-22-8 (Adrenodoxin); EC 2.8.1.- (Sulfurtransferases); EC 2.8.1.7 (NFS1 protein, S cerevisiae)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.787101


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[PMID]:28615439
[Au] Autor:Rouault TA; Maio N
[Ad] Endereço:From the Molecular Medicine Branch, Eunice Kennedy Shriver NICHD, National Institutes of Health, Bethesda, Maryland 20892 rouault@mail.nih.gov.
[Ti] Título:Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.
[So] Source:J Biol Chem;292(31):12744-12753, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent binding to recipient proteins. In this minireview, we discuss how discovery of the role of the mammalian cytosolic aconitase, known as iron regulatory protein 1 (IRP1), led to the characterization of the function of its Fe-S cluster in sensing and regulating cellular iron homeostasis. Moreover, we present an overview of recent studies that have provided insights into the mechanism of Fe-S cluster transfer to recipient Fe-S proteins.
[Mh] Termos MeSH primário: Homeostase
Proteína 1 Reguladora do Ferro/fisiologia
Ferro/fisiologia
Modelos Moleculares
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Liases de Carbono-Enxofre/biossíntese
Liases de Carbono-Enxofre/química
Liases de Carbono-Enxofre/fisiologia
Transporte de Elétrons
Regulação Enzimológica da Expressão Gênica
Proteínas de Choque Térmico HSP70/biossíntese
Proteínas de Choque Térmico HSP70/química
Proteínas de Choque Térmico HSP70/fisiologia
Seres Humanos
Proteína 1 Reguladora do Ferro/biossíntese
Proteína 1 Reguladora do Ferro/química
Proteínas de Ligação ao Ferro/biossíntese
Proteínas de Ligação ao Ferro/química
Proteínas de Ligação ao Ferro/fisiologia
Proteínas Reguladoras do Ferro/biossíntese
Proteínas Reguladoras do Ferro/química
Proteínas Reguladoras do Ferro/fisiologia
Proteínas com Ferro-Enxofre/biossíntese
Proteínas com Ferro-Enxofre/química
Proteínas com Ferro-Enxofre/fisiologia
Proteínas Mitocondriais/biossíntese
Proteínas Mitocondriais/química
Proteínas Mitocondriais/fisiologia
Chaperonas Moleculares/biossíntese
Chaperonas Moleculares/química
Chaperonas Moleculares/fisiologia
Dobramento de Proteína
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Elementos de Resposta
Succinato Desidrogenase/biossíntese
Succinato Desidrogenase/química
Succinato Desidrogenase/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (HSCB protein, human); 0 (HSP70 Heat-Shock Proteins); 0 (HSPA9 protein, human); 0 (ISCU protein, human); 0 (ISD11 protein, human); 0 (Iron-Binding Proteins); 0 (Iron-Regulatory Proteins); 0 (Iron-Sulfur Proteins); 0 (Mitochondrial Proteins); 0 (Molecular Chaperones); 0 (frataxin); E1UOL152H7 (Iron); EC 1.3.5.1 (SDHB protein, human); EC 1.3.99.1 (Succinate Dehydrogenase); EC 4.2.1.3 (IRP1 protein, human); EC 4.2.1.3 (Iron Regulatory Protein 1); EC 4.4.- (Carbon-Sulfur Lyases); EC 4.4.1.- (NFS1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.R117.789537



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