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Pesquisa : A11.148.378.590.837.250 [Categoria DeCS]
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[PMID]:27777239
[Au] Autor:Gao X; Lee HY; da Rocha EL; Zhang C; Lu YF; Li D; Feng Y; Ezike J; Elmes RR; Barrasa MI; Cahan P; Li H; Daley GQ; Lodish HF
[Ad] Endereço:Whitehead Institute for Biomedical Research, Cambridge, MA.
[Ti] Título:TGF-ß inhibitors stimulate red blood cell production by enhancing self-renewal of BFU-E erythroid progenitors.
[So] Source:Blood;128(23):2637-2641, 2016 12 08.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Burst-forming unit erythroid progenitors (BFU-Es) are so named based on their ability to generate in methylcellulose culture large colonies of erythroid cells that consist of "bursts" of smaller erythroid colonies derived from the later colony-forming unit erythroid progenitor erythropoietin (Epo)-dependent progenitors. "Early" BFU-E cells forming large BFU-E colonies presumably have higher capacities for self-renewal than do "late" BFU-Es forming small colonies, but the mechanism underlying this heterogeneity remains unknown. We show that the type III transforming growth factor ß (TGF-ß) receptor (TßRIII) is a marker that distinguishes early and late BFU-Es. Transient elevation of TßRIII expression promotes TGF-ß signaling during the early BFU-E to late BFU-E transition. Blocking TGF-ß signaling using a receptor kinase inhibitor increases early BFU-E cell self-renewal and total erythroblast production, suggesting the usefulness of this type of drug in treating Epo-unresponsive anemias.
[Mh] Termos MeSH primário: Antígenos de Diferenciação/metabolismo
Eritrócitos/metabolismo
Células Precursoras Eritroides/metabolismo
Proteoglicanas/metabolismo
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Transdução de Sinais/fisiologia
Fator de Crescimento Transformador beta/metabolismo
[Mh] Termos MeSH secundário: Anemia/metabolismo
Anemia/terapia
Animais
Eritrócitos/citologia
Células Precursoras Eritroides/citologia
Eritropoetina/metabolismo
Seres Humanos
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, Differentiation); 0 (Proteoglycans); 0 (Receptors, Transforming Growth Factor beta); 0 (Transforming Growth Factor beta); 11096-26-7 (Erythropoietin); 145170-29-2 (betaglycan)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180111
[Lr] Data última revisão:
180111
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161026
[St] Status:MEDLINE


  2 / 2989 MEDLINE  
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[PMID]:28806616
[Au] Autor:Janovitz T; Wong S; Young NS; Oliveira T; Falck-Pedersen E
[Ad] Endereço:Tri-Institutional MD-PhD Program, USA; Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, NY 10065, USA.
[Ti] Título:Parvovirus B19 integration into human CD36+ erythroid progenitor cells.
[So] Source:Virology;511:40-48, 2017 Nov.
[Is] ISSN:1096-0341
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pathogenic autonomous human parvovirus B19 (B19V) productively infects erythroid progenitor cells (EPCs). Functional similarities between B19V nonstructural protein (NS1), a DNA binding endonuclease, and the Rep proteins of Adeno-Associated Virus (AAV) led us to hypothesize that NS1 may facilitate targeted nicking of the human genome and B19 vDNA integration. We adapted an integration capture sequencing protocol (IC-Seq) to screen B19V infected human CD36+ EPCs for viral integrants, and discovered 40,000 unique B19V integration events distributed throughout the human genome. Computational analysis of integration patterns revealed strong correlations with gene intronic regions, H3K9me3 sites, and the identification of 41 base pair consensus sequence with an octanucleotide core motif. The octanucleotide core has homology to a single region of B19V, adjacent to the P6 promoter TATA box. We present the first direct evidence that B19V infection of erythroid progenitor cells disrupts the human genome and facilitates viral DNA integration.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/metabolismo
DNA/metabolismo
Endonucleases/metabolismo
Células Precursoras Eritroides/virologia
Parvovirus B19 Humano/fisiologia
Proteínas não Estruturais Virais/metabolismo
Integração Viral
[Mh] Termos MeSH secundário: Antígenos CD36/análise
Células Cultivadas
Células Precursoras Eritroides/química
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD36 Antigens); 0 (DNA-Binding Proteins); 0 (Viral Nonstructural Proteins); 9007-49-2 (DNA); EC 3.1.- (Endonucleases)
[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:170815
[St] Status:MEDLINE


  3 / 2989 MEDLINE  
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[PMID]:28776729
[Au] Autor:Dai Y; Chen T; Ijaz H; Cho EH; Steinberg MH
[Ad] Endereço:Department of Medicine, Boston University School of Medicine, Boston, Massachusetts, 02118.
[Ti] Título:SIRT1 activates the expression of fetal hemoglobin genes.
[So] Source:Am J Hematol;92(11):1177-1186, 2017 Nov.
[Is] ISSN:1096-8652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High fetal hemoglobin (HbF, α γ ) levels ameliorate the clinical manifestations of sickle cell disease and ß thalassemia. The mechanisms that repress HbF expression and silence γ-globin genes in adults are incompletely characterized and only a single HbF inducer, hydroxyurea, is approved for treatment, and only in patients with sickle cell disease. We identified SIRT1, a protein deacetylase, as a new inducer of γ-globin. SIRT1 knockdown decreased, while SIRT1 ectopic expression upregulated γ-globin gene (HBG) expression in primary human erythroid cells and in K562 cells. The small molecule SIRT1 activators SRT2104 and SRT1720 enhanced HBG expression in cord blood human erythroblasts and reactivated silenced HBG in adult human erythroblasts. Furthermore, SIRT1 binds in the ß-globin gene cluster locus control region (LCR) and HBG promoters, promotes the looping of the LCR to HBG promoter, and increases the binding of RNA polymerase II and H4K16Ac in the HBG promoter. SIRT1 suppressed the expression of the HBG suppressors BCL11A, KLF1, HDAC1 and HDAC2. Lastly, SIRT1 did not change the proliferation of human erythroid progenitor cells or the expression of differentiation marker CD235a. These data suggest that SIRT1 activates HBG expression through facilitating LCR looping to the HBG promoter, inhibiting the expression of transcriptional suppressors of HBG, and indirectly increasing histone acetylation in the HBG promoter. SIRT1 is a potential therapeutic target for γ-globin gene induction, and small molecule SIRT1 activators might serve as a lead compound for the development of new HbF inducers.
[Mh] Termos MeSH primário: Hemoglobina Fetal/genética
Regulação da Expressão Gênica
Sirtuína 1/metabolismo
Ativação Transcricional
gama-Globinas/genética
[Mh] Termos MeSH secundário: Diferenciação Celular/genética
Proliferação Celular/genética
Expressão Ectópica do Gene
Eritroblastos/metabolismo
Células Precursoras Eritroides/metabolismo
Eritropoese/genética
Hemoglobina Fetal/metabolismo
Técnicas de Silenciamento de Genes
Inativação Gênica
Seres Humanos
Células K562
Região de Controle de Locus Gênico
Especificidade de Órgãos/genética
Regiões Promotoras Genéticas
Ligação Proteica
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Sirtuína 1/genética
gama-Globinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (gamma-Globins); 9034-63-3 (Fetal Hemoglobin); EC 3.5.1.- (Sirtuin 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1002/ajh.24879


  4 / 2989 MEDLINE  
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[PMID]:28615454
[Au] Autor:Philpott CC; Ryu MS; Frey A; Patel S
[Ad] Endereço:From the Genetics and Metabolism Section, Liver Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, Carolinep@mail.nih.gov.
[Ti] Título:Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.
[So] Source:J Biol Chem;292(31):12764-12771, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Eukaryotic cells contain hundreds of metalloproteins that are supported by intracellular systems coordinating the uptake and distribution of metal cofactors. Iron cofactors include heme, iron-sulfur clusters, and simple iron ions. Poly(rC)-binding proteins are multifunctional adaptors that serve as iron ion chaperones in the cytosolic/nuclear compartment, binding iron at import and delivering it to enzymes, for storage (ferritin) and export (ferroportin). Ferritin iron is mobilized by autophagy through the cargo receptor, nuclear co-activator 4. The monothiol glutaredoxin Glrx3 and BolA2 function as a [2Fe-2S] chaperone complex. These proteins form a core system of cytosolic iron cofactor chaperones in mammalian cells.
[Mh] Termos MeSH primário: Citosol/metabolismo
Ferritinas/metabolismo
Proteínas com Ferro-Enxofre/metabolismo
Ferro/metabolismo
Modelos Biológicos
Modelos Moleculares
Chaperonas Moleculares/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoenzimas/química
Apoenzimas/metabolismo
Apoferritinas/química
Apoferritinas/metabolismo
Autofagia
Proteínas de Transporte/química
Proteínas de Transporte/metabolismo
Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/metabolismo
Dimerização
Células Precursoras Eritroides/citologia
Células Precursoras Eritroides/metabolismo
Ferritinas/química
Ribonucleoproteínas Nucleares Heterogêneas/química
Ribonucleoproteínas Nucleares Heterogêneas/metabolismo
Seres Humanos
Proteínas com Ferro-Enxofre/química
Chaperonas Moleculares/química
Coativadores de Receptor Nuclear/química
Coativadores de Receptor Nuclear/metabolismo
Multimerização Proteica
Transporte Proteico
Proteínas/química
Proteínas/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Apoenzymes); 0 (BOLA2 protein, human); 0 (Carrier Proteins); 0 (Cation Transport Proteins); 0 (GLRX3 protein, human); 0 (Heterogeneous-Nuclear Ribonucleoproteins); 0 (Iron-Sulfur Proteins); 0 (Molecular Chaperones); 0 (NCOA4 protein, human); 0 (Nuclear Receptor Coactivators); 0 (PCBP1 protein, human); 0 (PCBP2 protein, human); 0 (Proteins); 0 (RNA-Binding Proteins); 0 (metal transporting protein 1); 9007-73-2 (Ferritins); 9013-31-4 (Apoferritins); E1UOL152H7 (Iron)
[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.R117.791962


  5 / 2989 MEDLINE  
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[PMID]:28615441
[Au] Autor:Knutson MD
[Ad] Endereço:From the Food Science and Human Nutrition Department, University of Florida, Gainesville, Florida 32611-03170 mknutson@ufl.edu.
[Ti] Título:Iron transport proteins: Gateways of cellular and systemic iron homeostasis.
[So] Source:J Biol Chem;292(31):12735-12743, 2017 Aug 04.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular iron homeostasis is maintained by iron and heme transport proteins that work in concert with ferrireductases, ferroxidases, and chaperones to direct the movement of iron into, within, and out of cells. Systemic iron homeostasis is regulated by the liver-derived peptide hormone, hepcidin. The interface between cellular and systemic iron homeostasis is readily observed in the highly dynamic iron handling of four main cell types: duodenal enterocytes, erythrocyte precursors, macrophages, and hepatocytes. This review provides an overview of how these cell types handle iron, highlighting how iron and heme transporters mediate the exchange and distribution of body iron in health and disease.
[Mh] Termos MeSH primário: Homeostase
Ferro/fisiologia
Modelos Biológicos
[Mh] Termos MeSH secundário: Animais
Duodeno/citologia
Duodeno/fisiologia
Enterócitos/fisiologia
Células Precursoras Eritroides/citologia
Células Precursoras Eritroides/fisiologia
Eritropoese
Heme/efeitos adversos
Heme/metabolismo
Hepatócitos/fisiologia
Hepcidinas/fisiologia
Seres Humanos
Absorção Intestinal
Mucosa Intestinal/citologia
Mucosa Intestinal/fisiologia
Ferro/sangue
Ferro na Dieta/efeitos adversos
Ferro na Dieta/metabolismo
Macrófagos/imunologia
Macrófagos/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (HAMP protein, human); 0 (Hepcidins); 0 (Iron, Dietary); 42VZT0U6YR (Heme); E1UOL152H7 (Iron)
[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.R117.786632


  6 / 2989 MEDLINE  
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[PMID]:28412459
[Au] Autor:Steinkellner H; Singh HN; Muckenthaler MU; Goldenberg H; Moganty RR; Scheiber-Mojdehkar B; Sturm B
[Ad] Endereço:Department of Medical Chemistry and Pathobiochemistry, Medical University of Vienna, Vienna, Austria; Department of Medical Genetics, Medical University of Vienna, Vienna, Austria.
[Ti] Título:No changes in heme synthesis in human Friedreich´s ataxia erythroid progenitor cells.
[So] Source:Gene;621:5-11, 2017 Jul 20.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Friedreich's ataxia (FRDA) is a neurodegenerative disease caused by reduced expression of the protein frataxin. Frataxin is thought to play a role in iron-sulfur cluster biogenesis and heme synthesis. In this study, we used erythroid progenitor stem cells obtained from FRDA patients and healthy donors to investigate the putative role, if any, of frataxin deficiency in heme synthesis. We used electrochemiluminescence and qRT-PCR for frataxin protein and mRNA quantification. We used atomic absorption spectrophotometry for iron levels and a photometric assay for hemoglobin levels. Protoporphyrin IX and Ferrochelatase were analyzed using auto-fluorescence. An "IronChip" microarray analysis followed by a protein-protein interaction analysis was performed. FRDA patient cells showed no significant changes in iron levels, hemoglobin synthesis, protoporphyrin IX levels, and ferrochelatase activity. Microarray analysis presented 11 genes that were significantly changed in all patients compared to controls. The genes are especially involved in oxidative stress, iron homeostasis and angiogenesis. The mystery about the involvement of frataxin on iron metabolism raises the question why frataxin deficiency in primary FRDA cells did not lead to changes in biochemical parameters of heme synthesis. It seems that alternative pathways can circumvent the impact of frataxin deficiency on heme synthesis. We show for the first time in primary FRDA patient cells that reduced frataxin levels are still sufficient for heme synthesis and possibly other mechanisms can overcome reduced frataxin levels in this process. Our data strongly support the fact that so far no anemia in FRDA patients was reported.
[Mh] Termos MeSH primário: Células Precursoras Eritroides/metabolismo
Eritropoese
Ataxia de Friedreich/metabolismo
Heme/biossíntese
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Células Cultivadas
Células Precursoras Eritroides/citologia
Ferroquelatase/metabolismo
Ataxia de Friedreich/sangue
Hemoglobinas/metabolismo
Seres Humanos
Ferro/metabolismo
Proteínas de Ligação ao Ferro/genética
Proteínas de Ligação ao Ferro/metabolismo
Estresse Oxidativo
Protoporfirinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hemoglobins); 0 (Iron-Binding Proteins); 0 (Protoporphyrins); 0 (frataxin); 42VZT0U6YR (Heme); C2K325S808 (protoporphyrin IX); E1UOL152H7 (Iron); EC 4.99.1.1 (Ferrochelatase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170615
[Lr] Data última revisão:
170615
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170417
[St] Status:MEDLINE


  7 / 2989 MEDLINE  
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[PMID]:28377277
[Au] Autor:Bonvicini F; Bua G; Conti I; Manaresi E; Gallinella G
[Ad] Endereço:Department of Pharmacy and Biotechnology, University of Bologna, Via Massarenti 9, 40138 Bologna, Italy. Electronic address: francesca.bonvicini4@unibo.it.
[Ti] Título:Hydroxyurea inhibits parvovirus B19 replication in erythroid progenitor cells.
[So] Source:Biochem Pharmacol;136:32-39, 2017 Jul 15.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Parvovirus B19 (B19V) infection is restricted to erythroid progenitor cells (EPCs) of the human bone marrow, leading to transient arrest of erythropoiesis and severe complications mainly in subjects with underlying hematological disorders or with immune system deficits. Currently, there are no specific antiviral drugs for B19V treatment, but identification of compounds inhibiting B19V replication can be pursued by a drug repositioning strategy. In this frame, the present study investigates the activity of hydroxyurea (HU), the only disease-modifying therapy approved for sickle cell disease (SCD), towards B19V replication in the two relevant cellular systems, the UT7/EpoS1 cell line and EPCs. Results demonstrate that HU inhibits B19V replication with EC values of 96.2µM and 147.1µM in UT7/EpoS1 and EPCs, respectively, providing experimental evidence of the antiviral activity of HU towards B19V replication, and confirming the efficacy of a drug discovery process by drug repositioning strategy. The antiviral activity occurs in vitro at concentrations lower than those affecting cellular DNA replication and viability, and at levels measured in plasma samples of SCD patients undergoing HU therapy. HU might determine a dual beneficial effect on SCD patients, not only for the treatment of the disease but also towards a virus responsible for severe complications.
[Mh] Termos MeSH primário: Células Precursoras Eritroides/efeitos dos fármacos
Células Precursoras Eritroides/fisiologia
Hidroxiureia/farmacologia
Parvovirus B19 Humano/fisiologia
Replicação Viral/efeitos dos fármacos
Replicação Viral/fisiologia
[Mh] Termos MeSH secundário: Antivirais/farmacologia
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/fisiologia
Células Cultivadas
Relação Dose-Resposta a Droga
Células Precursoras Eritroides/virologia
Seres Humanos
Leucócitos Mononucleares/efeitos dos fármacos
Leucócitos Mononucleares/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiviral Agents); X6Q56QN5QC (Hydroxyurea)
[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:170406
[St] Status:MEDLINE


  8 / 2989 MEDLINE  
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[PMID]:28359802
[Au] Autor:Medina S; Xu H; Wang SC; Lauer FT; Liu KJ; Burchiel SW
[Ad] Endereço:The University of New Mexico College of Pharmacy, Department of Pharmaceutical Sciences, Albuquerque, NM 87131, United States.
[Ti] Título:Low level arsenite exposures suppress the development of bone marrow erythroid progenitors and result in anemia in adult male mice.
[So] Source:Toxicol Lett;273:106-111, 2017 May 05.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Epidemiological studies report an association between chronic arsenic (As) exposure and anemia in men, and women who are predisposed to anemia. The purpose of these studies was to determine whether a 60 d drinking water exposure of adult male C57BL/6J mice to 0, 100, and 500ppb arsenite (As ) results in anemia due to alterations in erythroid progenitor cell development in the bone marrow. Exposure to 500ppb As for 60 d resulted in a reduction of mean corpuscular hemoglobin (MCH) levels, but did not significantly alter red blood cell (RBC) counts, hemoglobin (Hgb) levels, mean corpuscular Hgb concentrations (MCHC), or mean corpuscular volumes (MCV). Attenuation of burst-forming unit-erythroid (BFU-E) colony formation was observed in bone marrow cells of mice exposed to 500ppb As . The differentiation of late-stage bone marrow erythroblasts as defined by CD71 and Ter119 surface marker expression was reduced with the 500ppb As exposure. Mice exposed to 500ppb As also had elevated serum levels of erythropoietin (EPO). Collectively, these results show that exposure to low levels of As attenuate the development of early BFU-E cells and reduce the differentiation of late-stage erythroblasts. This suppression of bone marrow erythropoiesis may be a contributing factor to the mild hypochromic anemia observed in 500ppb As exposed mice.
[Mh] Termos MeSH primário: Anemia/induzido quimicamente
Arsenitos/toxicidade
Células da Medula Óssea/efeitos dos fármacos
Poluentes Ambientais/toxicidade
Células Precursoras Eritroides/efeitos dos fármacos
Eritropoese/efeitos dos fármacos
[Mh] Termos MeSH secundário: Anemia/sangue
Anemia/patologia
Animais
Células da Medula Óssea/citologia
Relação Dose-Resposta a Droga
Ingestão de Líquidos
Células Precursoras Eritroides/citologia
Eritropoetina/sangue
Hemoglobinas/análise
Masculino
Camundongos Endogâmicos C57BL
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arsenites); 0 (Environmental Pollutants); 0 (Hemoglobins); 11096-26-7 (Erythropoietin); N5509X556J (arsenite)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170704
[Lr] Data última revisão:
170704
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170401
[St] Status:MEDLINE


  9 / 2989 MEDLINE  
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[PMID]:28264028
[Au] Autor:Xu P; Zhou Z; Xiong M; Zou W; Deng X; Ganaie SS; Kleiboeker S; Peng J; Liu K; Wang S; Ye SQ; Qiu J
[Ad] Endereço:School of Life Sciences, Central China Normal University, Wuhan, China.
[Ti] Título:Parvovirus B19 NS1 protein induces cell cycle arrest at G2-phase by activating the ATR-CDC25C-CDK1 pathway.
[So] Source:PLoS Pathog;13(3):e1006266, 2017 Mar.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human parvovirus B19 (B19V) infection of primary human erythroid progenitor cells (EPCs) arrests infected cells at both late S-phase and G2-phase, which contain 4N DNA. B19V infection induces a DNA damage response (DDR) that facilitates viral DNA replication but is dispensable for cell cycle arrest at G2-phase; however, a putative C-terminal transactivation domain (TAD2) within NS1 is responsible for G2-phase arrest. To fully understand the mechanism underlying B19V NS1-induced G2-phase arrest, we established two doxycycline-inducible B19V-permissive UT7/Epo-S1 cell lines that express NS1 or NS1mTAD2, and examined the function of the TAD2 domain during G2-phase arrest. The results confirm that the NS1 TAD2 domain plays a pivotal role in NS1-induced G2-phase arrest. Mechanistically, NS1 transactivated cellular gene expression through the TAD2 domain, which was itself responsible for ATR (ataxia-telangiectasia mutated and Rad3-related) activation. Activated ATR phosphorylated CDC25C at serine 216, which in turn inactivated the cyclin B/CDK1 complex without affecting nuclear import of the complex. Importantly, we found that the ATR-CHK1-CDC25C-CDK1 pathway was activated during B19V infection of EPCs, and that ATR activation played an important role in B19V infection-induced G2-phase arrest.
[Mh] Termos MeSH primário: Pontos de Checagem da Fase G2 do Ciclo Celular/fisiologia
Infecções por Parvoviridae/metabolismo
Transdução de Sinais/fisiologia
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Proteínas Mutadas de Ataxia Telangiectasia/metabolismo
Western Blotting
Proteína Quinase CDC2
Linhagem Celular
Quinases Ciclina-Dependentes/metabolismo
Células Precursoras Eritroides/virologia
Citometria de Fluxo
Seres Humanos
Imunoprecipitação
Análise de Sequência com Séries de Oligonucleotídeos
Parvovirus B19 Humano
Fosfatases cdc25/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (NS1 protein, parvovirus); 0 (Viral Nonstructural Proteins); EC 2.7.11.1 (ATR protein, human); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.22 (CDC2 Protein Kinase); EC 2.7.11.22 (CDK1 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinases); EC 3.1.3.48 (CDC25C protein, human); EC 3.1.3.48 (cdc25 Phosphatases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170307
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006266


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[PMID]:28173615
[Au] Autor:Feng G; Zhang T; Liu J; Ma X; Li B; Yang L; Zhang Y; Xu Z; Qin T; Zhou J; Huang G; Shi L; Xiao Z
[Ad] Endereço:State Key Laboratory of Experimental Hematology, Institute of Hematology and Blood Diseases Hospital, Chinese Academy of Medical Sciences & Peking Union Medical College, Tianjin, China.
[Ti] Título:MLF1IP promotes normal erythroid proliferation and is involved in the pathogenesis of polycythemia vera.
[So] Source:FEBS Lett;591(5):760-773, 2017 Mar.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Myelodysplasia/myeloid leukemia factor 1-interacting protein (MLF1IP) appears to be an erythroid lineage-specific gene in mice; however, its role in normal erythropoiesis and erythropoietic disorders have not yet been elucidated. Here, we found that MLF1IP is abundantly expressed in human erythroid progenitor cells and that MLF1IP-deficiency reduces cell proliferation resulting from cell cycle arrest. Moreover, MLF1IP expression is exclusively elevated in CFU-E cells from polycythemia vera (PV) patients, and MLF1IP transgenic mice develop a PV-like disorder. Further analyses revealed that the erythroid progenitors and early-stage erythroblasts from these transgenic mice expand by up-regulating cyclin D2 and down-regulating p27 and p21. Thus, our data demonstrate that MLF1IP promotes erythroid proliferation and is involved in the pathogenesis of PV, suggesting that it might be a novel molecular target for erythropoietic disorders.
[Mh] Termos MeSH primário: Células da Medula Óssea/metabolismo
Células Precursoras Eritroides/metabolismo
Proteínas Nucleares/genética
Policitemia Vera/genética
[Mh] Termos MeSH secundário: Animais
Células da Medula Óssea/patologia
Diferenciação Celular
Proliferação Celular
Células Precursoras Eritroides/patologia
Regulação da Expressão Gênica
Seres Humanos
Células K562
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteínas Nucleares/antagonistas & inibidores
Proteínas Nucleares/metabolismo
Policitemia Vera/metabolismo
Policitemia Vera/patologia
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Transdução de Sinais
Transgenes
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (MLF1IP protein, human); 0 (Nuclear Proteins); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170515
[Lr] Data última revisão:
170515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170208
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12587



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