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  1 / 2028 MEDLINE  
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[PMID]:28646128
[Au] Autor:Duangtum N; Junking M; Phadngam S; Sawasdee N; Castiglioni A; Charngkaew K; Limjindaporn T; Isidoro C; Yenchitsomanus PT
[Ad] Endereço:Division of Molecular Medicine, Department of Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand.
[Ti] Título:γ-COPI mediates the retention of kAE1 G701D protein in Golgi apparatus - a mechanistic explanation of distal renal tubular acidosis associated with the G701D mutation.
[So] Source:Biochem J;474(15):2573-2584, 2017 Jul 17.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations of the ( ) gene encoding kidney anion (chloride/bicarbonate ion) exchanger 1 (kAE1) can cause genetic distal renal tubular acidosis (dRTA). Different mutations give rise to mutant kAE1 proteins with distinct defects in protein trafficking. The mutant kAE1 protein may be retained in endoplasmic reticulum (ER) or Golgi apparatus, or mis-targeted to the apical membrane, failing to display its function at the baso-lateral membrane. The ER-retained mutant kAE1 interacts with calnexin chaperone protein; disruption of this interaction permits the mutant kAE1 to reach the cell surface and display anion exchange activity. However, the mechanism of Golgi retention of mutant kAE1 G701D protein, which is otherwise functional, is still unclear. In the present study, we show that Golgi retention of kAE1 G701D is due to a stable interaction with the Golgi-resident protein, coat protein complex I (COPI), that plays a role in retrograde vesicular trafficking and Golgi-based quality control. The interaction and co-localization of kAE1 G701D with the γ-COPI subunit were demonstrated in human embryonic kidney (HEK-293T) cells by co-immunoprecipitation and immunofluorescence staining. Small interference RNA (siRNA) silencing of COPI expression in the transfected HEK-293T cells increased the cell surface expression of transgenic kAE1 G701D, as shown by immunofluorescence staining. Our data unveil the molecular mechanism of Golgi retention of kAE1 G701D and suggest that disruption of the COPI-kAE1 G701D interaction could be a therapeutic strategy to treat dRTA caused by this mutant.
[Mh] Termos MeSH primário: Acidose Tubular Renal/metabolismo
Proteína 1 de Troca de Ânion do Eritrócito/genética
Proteína Coatomer/metabolismo
Complexo de Golgi/metabolismo
Mutação/genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Técnicas de Silenciamento de Genes
Complexo de Golgi/ultraestrutura
Células HEK293
Seres Humanos
Rim/patologia
Rim/ultraestrutura
Modelos Biológicos
Proteínas Mutantes/metabolismo
Ligação Proteica
Subunidades Proteicas/metabolismo
RNA Interferente Pequeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Anion Exchange Protein 1, Erythrocyte); 0 (COPG protein, human); 0 (Coatomer Protein); 0 (Mutant Proteins); 0 (Protein Subunits); 0 (RNA, Small Interfering)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170625
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170088


  2 / 2028 MEDLINE  
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[PMID]:28634183
[Au] Autor:Pantaleo A; Kesely KR; Pau MC; Tsamesidis I; Schwarzer E; Skorokhod OA; Chien HD; Ponzi M; Bertuccini L; Low PS; Turrini FM
[Ad] Endereço:Department of Biomedical Sciences, University of Sassari, Sassari, Italy.
[Ti] Título:Syk inhibitors interfere with erythrocyte membrane modification during growth and suppress parasite egress.
[So] Source:Blood;130(8):1031-1040, 2017 Aug 24.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Band 3 (also known as the anion exchanger, SLCA1, AE1) constitutes the major attachment site of the spectrin-based cytoskeleton to the erythrocyte's lipid bilayer and thereby contributes critically to the stability of the red cell membrane. During the intraerythrocytic stage of 's lifecycle, band 3 becomes tyrosine phosphorylated in response to oxidative stress, leading to a decrease in its affinity for the spectrin/actin cytoskeleton and causing global membrane destabilization. Because this membrane weakening is hypothesized to facilitate parasite egress and the consequent dissemination of released merozoites throughout the bloodstream, we decided to explore which tyrosine kinase inhibitors might block the kinase-induced membrane destabilization. We demonstrate here that multiple Syk kinase inhibitors both prevent parasite-induced band 3 tyrosine phosphorylation and inhibit parasite-promoted membrane destabilization. We also show that the same Syk kinase inhibitors suppress merozoite egress near the end of the parasite's intraerythrocytic lifecycle. Because the entrapped merozoites die when prevented from escaping their host erythrocytes and because some Syk inhibitors have displayed long-term safety in human clinical trials, we suggest Syk kinase inhibitors constitute a promising class of antimalarial drugs that can suppress parasitemia by inhibiting a host target that cannot be mutated by the parasite to evolve drug resistance.
[Mh] Termos MeSH primário: Membrana Eritrocítica/metabolismo
Membrana Eritrocítica/parasitologia
Parasitos/crescimento & desenvolvimento
Plasmodium falciparum/crescimento & desenvolvimento
Inibidores de Proteínas Quinases/farmacologia
Quinase Syk/antagonistas & inibidores
[Mh] Termos MeSH secundário: Adulto
Animais
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Diferenciação Celular/efeitos dos fármacos
Membrana Eritrocítica/efeitos dos fármacos
Membrana Eritrocítica/ultraestrutura
Feminino
Seres Humanos
Concentração Inibidora 50
Malária Falciparum
Masculino
Parasitos/efeitos dos fármacos
Parasitos/ultraestrutura
Fosforilação/efeitos dos fármacos
Plasmodium falciparum/efeitos dos fármacos
Plasmodium falciparum/ultraestrutura
Quinase Syk/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (Protein Kinase Inhibitors); EC 2.7.10.2 (Syk Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170622
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-11-748053


  3 / 2028 MEDLINE  
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[PMID]:28596233
[Au] Autor:Hsu K; Lee TY; Periasamy A; Kao FJ; Li LT; Lin CY; Lin HJ; Lin M
[Ad] Endereço:Transfusion Medicine Laboratory, Mackay Memorial Hospital, Tamsui, Taiwan; khsu1@mmh.org.tw.
[Ti] Título:Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO transport.
[So] Source:FASEB J;31(10):4256-4264, 2017 Oct.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human CO respiration requires rapid conversion between CO and HCO Carbonic anhydrase II facilitates this reversible reaction inside red blood cells, and band 3 [anion exchanger 1 (AE1)] provides a passage for HCO flux across the cell membrane. These 2 proteins are core components of the CO transport metabolon. Intracellular H O is necessary for CO /HCO conversion. However, abundantly expressed aquaporin 1 (AQP1) in erythrocytes is thought not to be part of band 3 complexes or the CO transport metabolon. To solve this conundrum, we used Förster resonance energy transfer (FRET) measured by fluorescence lifetime imaging (FLIM-FRET) and identified interaction between aquaporin-1 and band 3 at a distance of 8 nm, within the range of dipole-dipole interaction. Notably, their interaction was adaptable to membrane tonicity changes. This suggests that the function of AQP1 in tonicity response could be coupled or correlated to its function in band 3-mediated CO /HCO exchange. By demonstrating AQP1 as a mobile component of the CO transport metabolon, our results uncover a potential role of water channel in blood CO transport and respiration.-Hsu, K., Lee, T.-Y., Periasamy, A., Kao, F.-J., Li, L.-T., Lin, C.-Y., Lin, H.-J., Lin, M. Adaptable interaction between aquaporin-1 and band 3 reveals a potential role of water channel in blood CO transport.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Aquaporina 1/metabolismo
Transporte Biológico/fisiologia
Dióxido de Carbono/sangue
Permeabilidade da Membrana Celular/fisiologia
Eritrócitos/metabolismo
[Mh] Termos MeSH secundário: Membrana Eritrocítica/metabolismo
Seres Humanos
Concentração de Íons de Hidrogênio
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 142M471B3J (Carbon Dioxide); 146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601282R


  4 / 2028 MEDLINE  
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[PMID]:28494002
[Au] Autor:Kurano M; Nishikawa M; Kuma H; Jona M; Yatomi Y
[Ad] Endereço:Department of Clinical Laboratory Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo, Japan.
[Ti] Título:Involvement of Band3 in the efflux of sphingosine 1-phosphate from erythrocytes.
[So] Source:PLoS One;12(5):e0177543, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sphingosine 1-phosphate (S1P) is a bioactive lipid mediator that is thought to be involved in various diseases. Although the main source of S1P in the plasma is erythrocytes, how S1P is exported from erythrocytes has not been elucidated. When we differentiated K562 cells into erythroblast-like cells with sodium butyrate, we observed that the efflux of S1P was increased without increased expression of previously proposed S1P transporters, while the expression levels of Band3 were increased. Therefore, in this study, we investigated the involvement of Band 3, the most characteristic membranous transporter for erythrocytes, in S1P efflux, using 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonic acid, disodium salt (H2DIDS), which is an inhibitor of Band3. First, we treated human washed erythrocytes with H2DIDS and found that H2DIDS decreased the S1P levels in the supernatant, while it increased the cellular S1P contents. Next, when we injected H2DIDS into mice, the plasma S1P level was significantly decreased. Finally, when we overexpressed or suppressed Band3 in K562 cells, S1P efflux was enhanced or decreased, respectively, while the overexpression of Band3 in HEK293 cells did not modulate S1P efflux. These results suggested the possible involvement of Band3 in the transport of S1P, a multi-functional bioactive phospholipid, from erythrocytes.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Eritrócitos/metabolismo
Lisofosfolipídeos/metabolismo
Esfingosina/análogos & derivados
[Mh] Termos MeSH secundário: Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/administração & dosagem
Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/análogos & derivados
Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/farmacologia
Albuminas/metabolismo
Animais
Transporte Biológico/efeitos dos fármacos
Ácido Butírico/farmacologia
Diferenciação Celular/efeitos dos fármacos
Eritrócitos/efeitos dos fármacos
Células HEK293
Homeostase/efeitos dos fármacos
Seres Humanos
Injeções
Células K562
Lisofosfolipídeos/sangue
Camundongos Endogâmicos C57BL
Esfingosina/sangue
Esfingosina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Albumins); 0 (Anion Exchange Protein 1, Erythrocyte); 0 (Lysophospholipids); 107-92-6 (Butyric Acid); 26993-30-6 (sphingosine 1-phosphate); 61481-03-6 (dihydro-DIDS); NGZ37HRE42 (Sphingosine); Q1O6DSW23R (4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170911
[Lr] Data última revisão:
170911
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177543


  5 / 2028 MEDLINE  
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[PMID]:28407820
[Au] Autor:DU J; Pang QQ; Jiang Y; Wang O; Li M; Xing XP; Xia WB
[Ad] Endereço:Department of Endocrinology/Key Laboratory of Endocrinology, Ministry of Health, Peking Union Medical College Hospital, Chinese Academy of Medical Sciences, Peking Union Medical College, Beijing 100730, China. xiaweibo@medmail.com.cn.
[Ti] Título:[Clinical features of hereditary distal renal tubular acidosis and SLC4A1 gene mutation].
[So] Source:Zhongguo Dang Dai Er Ke Za Zhi;19(4):381-384, 2017 Apr.
[Is] ISSN:1008-8830
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To study the clinical features of two families with distal renal tubular acidosis (dRTA) and mutations in the pathogenic gene SLC4A1. METHODS: Family investigation, medical history collection, and measurement of biochemical parameters were performed to analyze the clinical phenotype and genetic characteristics of dRTA. Direct sequencing was used to detect SLC4A1 gene mutations. RESULTS: Three patients in these two families (two of them were mother and son) were diagnosed with dRTA with typical clinical features, including short stature, metabolic acidosis, alkaline urine, hypokalemia, and nephrocalcinosis. SLC4A1 gene analysis showed that all the three patients had a pathogenic missense mutation R589H (c.1766G>A). The child in family 1 had a de novo mutation of SLC4A1, and the child in family 2 had an SLC4A1 gene mutation inherited from the mother, which met the characteristic of autosomal dominant inheritance. CONCLUSIONS: This study reports the R589H mutation in SLC4A1 gene in families with hereditary dRTA for the first time in China. Clinical physicians should perform gene detection for patients suspected of hereditary dRTA to improve the diagnosis and treatment of this disease.
[Mh] Termos MeSH primário: Acidose Tubular Renal/genética
Proteína 1 de Troca de Ânion do Eritrócito/genética
Mutação
[Mh] Termos MeSH secundário: Criança
Seres Humanos
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (SLC4A1 protein, human)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170801
[Lr] Data última revisão:
170801
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE


  6 / 2028 MEDLINE  
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[PMID]:28272532
[Au] Autor:Edvardson S; Prunetti L; Arraf A; Haas D; Bacusmo JM; Hu JF; Ta-Shma A; Dedon PC; de Crécy-Lagard V; Elpeleg O
[Ad] Endereço:Monique and Jacques Roboh Department of Genetic Research, Hadassah Medical Center, Hebrew University of Jerusalem, Jerusalem, Israel.
[Ti] Título:tRNA N6-adenosine threonylcarbamoyltransferase defect due to KAE1/TCS3 (OSGEP) mutation manifest by neurodegeneration and renal tubulopathy.
[So] Source:Eur J Hum Genet;25(5):545-551, 2017 May.
[Is] ISSN:1476-5438
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Post-transcriptional tRNA modifications are numerous and require a large set of highly conserved enzymes in humans and other organisms. In yeast, the loss of many modifications is tolerated under unstressed conditions; one exception is the N -threonyl-carbamoyl-adenosine (t A) modification, loss of which causes a severe growth phenotype. Here we aimed at a molecular diagnosis in a brother and sister from a consanguineous family who presented with global developmental delay, failure to thrive and a renal defect manifesting in proteinuria and hypomagnesemia. Using exome sequencing, the patients were found to be homozygous for the c.974G>A (p.(Arg325Gln)) variant of the KAE1 gene. KAE1 is a constituent of the KEOPS complex, a five-subunit complex that catalyzes the second biosynthetic step of t A in the cytosol. The yeast KAE1 allele carrying the equivalent mutation did not rescue the t A deficiency of the kae1Δ yeast strain as efficiently as the WT allele; furthermore, t A levels quantified by LC-MS/MS were lower in the kae1Δ strain which was complemented by the mutation than in the kae1Δ strain, which was complemented by the WT allele. We conclude that homozygosity for c.974G>A (p.(Arg325Gln)) in KAE1 likely exerts its pathogenic effect by perturbing t A synthesis, thereby interfering with global protein production. This is the first report of t A biosynthesis defect in human. KAE1 joins the growing list of cytoplasmic tRNA modification enzymes, all associated with severe neurological disorders.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/genética
Deficiências do Desenvolvimento/genética
Nefropatias/genética
Erros Inatos do Metabolismo/genética
Mutação
RNA de Transferência/metabolismo
[Mh] Termos MeSH secundário: Adenosina/análogos & derivados
Adenosina/metabolismo
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Criança
Deficiências do Desenvolvimento/diagnóstico
Exoma
Feminino
Teste de Complementação Genética
Homozigoto
Seres Humanos
Nefropatias/diagnóstico
Magnésio/metabolismo
Masculino
Erros Inatos do Metabolismo/diagnóstico
Processamento Pós-Transcricional do RNA
RNA de Transferência/genética
Saccharomyces cerevisiae/genética
Síndrome
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (SLC4A1 protein, human); 24719-82-2 (N(6)-(N-threonylcarbonyl)adenosine); 9014-25-9 (RNA, Transfer); I38ZP9992A (Magnesium); K72T3FS567 (Adenosine)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1038/ejhg.2017.30


  7 / 2028 MEDLINE  
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[PMID]:28233610
[Au] Autor:Palazzo V; Provenzano A; Becherucci F; Sansavini G; Mazzinghi B; Orlandini V; Giunti L; Roperto RM; Pantaleo M; Artuso R; Andreucci E; Bargiacchi S; Traficante G; Stagi S; Murer L; Benetti E; Emma F; Giordano M; Rivieri F; Colussi G; Penco S; Manfredini E; Caruso MR; Garavelli L; Andrulli S; Vergine G; Miglietti N; Mancini E; Malaventura C; Percesepe A; Grosso E; Materassi M; Romagnani P; Giglio S
[Ad] Endereço:Department of Biomedical Experimental and Clinical Sciences "Mario Serio", University of Florence, Florence, Italy.
[Ti] Título:The genetic and clinical spectrum of a large cohort of patients with distal renal tubular acidosis.
[So] Source:Kidney Int;91(5):1243-1255, 2017 May.
[Is] ISSN:1523-1755
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Primary distal renal tubular acidosis is a rare genetic disease. Mutations in SLC4A1, ATP6V0A4, and ATP6V1B1 genes have been described as the cause of the disease, transmitted as either an autosomal dominant or recessive trait. Particular clinical features, such as sensorineural hearing loss, have been mainly described in association with mutations in one gene instead of the others. Nevertheless, the diagnosis of distal renal tubular acidosis is essentially based on clinical and laboratory findings, and the series of patients described so far are usually represented by small cohorts. Therefore, a strict genotype-phenotype correlation is still lacking, and questions about whether clinical and laboratory data should direct the genetic analysis remain open. Here, we applied next-generation sequencing in 89 patients with a clinical diagnosis of distal renal tubular acidosis, analyzing the prevalence of genetic defects in SLC4A1, ATP6V0A4, and ATP6V1B1 genes and the clinical phenotype. A genetic cause was determined in 71.9% of cases. In our group of sporadic cases, clinical features, including sensorineural hearing loss, are not specific indicators of the causal underlying gene. Mutations in the ATP6V0A4 gene are quite as frequent as mutations in ATP6V1B1 in patients with recessive disease. Chronic kidney disease was frequent in patients with a long history of the disease. Thus, our results suggest that when distal renal tubular acidosis is suspected, complete genetic testing could be considered, irrespective of the clinical phenotype of the patient.
[Mh] Termos MeSH primário: Acidose Tubular Renal/genética
Proteína 1 de Troca de Ânion do Eritrócito/genética
Doenças Raras/genética
Insuficiência Renal Crônica/genética
ATPases Vacuolares Próton-Translocadoras/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Pré-Escolar
Análise Mutacional de DNA
Feminino
Estudos de Associação Genética
Testes Genéticos
Genótipo
Perda Auditiva Neurossensorial/genética
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Lactente
Masculino
Meia-Idade
Mutação
Fenótipo
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (SLC4A1 protein, human); EC 3.6.1.- (ATP6V0A4 protein, human); EC 3.6.1.- (Vacuolar Proton-Translocating ATPases); EC 3.6.3.14 (ATP6V1B1 protein, human)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE


  8 / 2028 MEDLINE  
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[PMID]:28216155
[Au] Autor:Fujiwara T; Sasaki K; Saito K; Hatta S; Ichikawa S; Kobayashi M; Okitsu Y; Fukuhara N; Onishi Y; Harigae H
[Ad] Endereço:Department of Hematology and Rheumatology, Tohoku University Graduate School, Sendai, 2-1 Seiryo-cho, Aoba-ku, Sendai 980-8575, Japan. Electronic address: fujiwara-to@apple.email.ne.jp.
[Ti] Título:Forced FOG1 expression in erythroleukemia cells: Induction of erythroid genes and repression of myelo-lymphoid transcription factor PU.1.
[So] Source:Biochem Biophys Res Commun;485(2):380-387, 2017 Apr 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The transcription factor GATA-1-interacting protein Friend of GATA-1 (FOG1) is essential for proper transcriptional activation and repression of GATA-1 target genes; yet, the mechanisms by which FOG1 exerts its activating and repressing functions remain unknown. Forced FOG1 expression in human K562 erythroleukemia cells induced the expression of erythroid genes (SLC4A1, globins) but repressed that of GATA-2 and PU.1. A quantitative chromatin immunoprecipitation (ChIP) analysis demonstrated increased GATA-1 chromatin occupancy at both FOG1-activated as well as FOG1-repressed gene loci. However, while TAL1 chromatin occupancy was significantly increased at FOG1-activated gene loci, it was significantly decreased at FOG1-repressed gene loci. When FOG1 was overexpressed in TAL1-knocked down K562 cells, FOG1-mediated activation of HBA, HBG, and SLC4A1 was significantly compromised by TAL1 knockdown, suggesting that FOG1 may require TAL1 to activate GATA-1 target genes. Promoter analysis and quantitative ChIP analysis demonstrated that FOG1-mediated transcriptional repression of PU.1 would be mediated through a GATA-binding element located at its promoter, accompanied by significantly decreased H3 acetylation at lysine 4 and 9 (K4 and K9) as well as H3K4 trimethylation. Our results provide important mechanistic insight into the role of FOG1 in the regulation of GATA-1-regulated genes and suggest that FOG1 has an important role in inducing cells to differentiate toward the erythroid lineage rather than the myelo-lymphoid one by repressing the expression of PU.1.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/genética
Regulação Leucêmica da Expressão Gênica
Proteínas Nucleares/genética
Proteínas Proto-Oncogênicas/genética
Transativadores/genética
Fatores de Transcrição/genética
[Mh] Termos MeSH secundário: Acetilação
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Western Blotting
Linhagem Celular
Cromatina/genética
Cromatina/metabolismo
Fator de Transcrição GATA1/genética
Fator de Transcrição GATA1/metabolismo
Histonas/metabolismo
Seres Humanos
Células K562
Leucemia Eritroblástica Aguda/genética
Leucemia Eritroblástica Aguda/metabolismo
Leucemia Eritroblástica Aguda/patologia
Lisina/metabolismo
Proteínas Nucleares/metabolismo
Regiões Promotoras Genéticas/genética
Ligação Proteica
Proteínas Proto-Oncogênicas/metabolismo
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Proteína 1 de Leucemia Linfocítica Aguda de Células T
Transativadores/metabolismo
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (Chromatin); 0 (GATA1 Transcription Factor); 0 (GATA1 protein, human); 0 (Histones); 0 (Nuclear Proteins); 0 (Proto-Oncogene Proteins); 0 (SLC4A1 protein, human); 0 (T-Cell Acute Lymphocytic Leukemia Protein 1); 0 (Trans-Activators); 0 (Transcription Factors); 0 (ZFPM1 protein, human); 0 (proto-oncogene protein Spi-1); 135471-20-4 (TAL1 protein, human); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


  9 / 2028 MEDLINE  
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[PMID]:28160546
[Au] Autor:Shiozaki A; Kudou M; Ichikawa D; Shimizu H; Arita T; Kosuga T; Konishi H; Komatsu S; Fujiwara H; Okamoto K; Kishimoto M; Marunaka Y; Otsuji E
[Ad] Endereço:Division of Digestive Surgery, Department of Surgery, Kyoto Prefectural University of Medicine, Kyoto, 602-8566, Japan.
[Ti] Título:Expression and role of anion exchanger 1 in esophageal squamous cell carcinoma.
[So] Source:Oncotarget;8(11):17921-17935, 2017 Mar 14.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recent studies have described important roles for the anion exchanger (AE) in epithelial carcinogenesis and tumor behavior. The objectives of the present study were to investigate the role of AE1 in the regulation of genes involved in tumor progression and the clinicopathological significance of its expression in esophageal squamous cell carcinoma (ESCC). An immunohistochemical analysis was performed on 61 primary tumor samples obtained from ESCC patients who underwent esophagectomy. AE1 was primarily located in the cell membranes or cytoplasm of carcinoma cells, and its distribution pattern was related to the histological degree of the differentiation of SCC or the pT category. Among patients with pT2-3 ESCC, the 5-year survival rate of patients with diffuse AE1 expression (40.2%) was significantly lower than that of patients with focal expression (74.0%). AE1 was strongly expressed in KYSE150 and TE8 human ESCC cells. The depletion of AE1 using siRNA inhibited cell proliferation, migration, and invasion and induced apoptosis. The results of the microarray analysis revealed that MAPK and Hedgehog signaling pathway-related genes, such as DHH, and GLI1, were down-regulated in AE1-depleted KYSE150 cells. In conclusions, the results of the present study suggest that the diffuse expression of AE1 is related to a worse prognosis in patients with advanced ESCC, and that it regulates tumor progression by affecting MAPK and Hedgehog signaling pathways. These results provide an insight into the role of AE1 as a mediator of and/or a biomarker for ESCC.
[Mh] Termos MeSH primário: Proteína 1 de Troca de Ânion do Eritrócito/genética
Carcinogênese/genética
Carcinoma de Células Escamosas/genética
Carcinoma de Células Escamosas/patologia
Neoplasias Esofágicas/genética
Neoplasias Esofágicas/patologia
Sistema de Sinalização das MAP Quinases/genética
[Mh] Termos MeSH secundário: Idoso
Proteína 1 de Troca de Ânion do Eritrócito/biossíntese
Proteína 1 de Troca de Ânion do Eritrócito/metabolismo
Apoptose/genética
Biomarcadores Tumorais/genética
Carcinoma de Células Escamosas/mortalidade
Carcinoma de Células Escamosas/cirurgia
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Progressão da Doença
Regulação para Baixo
Neoplasias Esofágicas/mortalidade
Neoplasias Esofágicas/cirurgia
Esofagectomia
Feminino
Regulação Neoplásica da Expressão Gênica
Proteínas Hedgehog/biossíntese
Proteínas Hedgehog/metabolismo
Seres Humanos
Imuno-Histoquímica
Masculino
Análise em Microsséries
Meia-Idade
Invasividade Neoplásica/genética
Prognóstico
Interferência de RNA
RNA Interferente Pequeno/genética
Taxa de Sobrevida
Proteína GLI1 em Dedos de Zinco/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (Biomarkers, Tumor); 0 (DHH protein, human); 0 (GLI1 protein, human); 0 (Hedgehog Proteins); 0 (RNA, Small Interfering); 0 (Zinc Finger Protein GLI1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170205
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.14900


  10 / 2028 MEDLINE  
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[PMID]:28130418
[Au] Autor:Yamaguchi T; Kojima H; Kawaguchi S; Shimada M; Aso H
[Ad] Endereço:Department of Chemistry, Faculty of Science, Fukuoka University, Jonan-ku, Fukuoka 814-0180, Japan.
[Ti] Título:Papain cleavage of the 38,000-dalton fragment inhibits the binding of 4, 4'-diisothiocyanostilbene-2, 2'-disulfonate to lys-539 on the 60,000-dalton fragment in human band 3.
[So] Source:J Biochem;162(2):103-111, 2017 Aug 01.
[Is] ISSN:1756-2651
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human band 3 is a 98-kDa transmembrane (TM) protein comprising 14 TM segments. Papain cleavages band 3 into 38- and 60-kDa fragments. Under vigorous conditions, the cleavage of the loop region between the TM 7 of gate domain and the TM 8 of core domain in the 38-kDa fragment produces 7- and 31-kDa fragments. Conformational changes of the TM 5 segment containing Lys-539 by cleavage of the 38-kDa fragment remain unclear. Pressure-induced haemolysis of erythrocytes was suppressed by binding of 4, 4'-diisothiocyanostilbene-2, 2'-disulfonate (DIDS) to Lys-539. Such effect of DIDS was not observed upon cleavage of the 38-kDa fragment, because of inhibition of DIDS binding to Lys-539. Using fluorescence of DIDS labelled to Lys-539, conformational changes of band 3 were examined. Fluorescence spectra demonstrated that the molecular motion of DIDS is more restricted upon digestion of the 38-kDa fragment. Interestingly, the quenching of DIDS fluorescence showed that Hg2+ is less accessible to DIDS upon digestion of the 38-kDa fragment. Taken together, we propose that the conformational changes of the TM 5 segment characterized by the sequestration and restricted motion of Lys-539 are induced by the cleavage of the loop region between the TM 7 and the TM 8.
[Mh] Termos MeSH primário: Ácido 4,4´-Di-Isotiocianoestilbeno-2,2´-Dissulfônico/antagonistas & inibidores
Proteína 1 de Troca de Ânion do Eritrócito/antagonistas & inibidores
Lisina/antagonistas & inibidores
Papaína/farmacologia
Fragmentos de Peptídeos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Ácido 4,4'-Di-Isotiocianoestilbeno-2,2'-Dissulfônico/química
Proteína 1 de Troca de Ânion do Eritrócito/química
Sítios de Ligação/efeitos dos fármacos
Seres Humanos
Lisina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anion Exchange Protein 1, Erythrocyte); 0 (Peptide Fragments); EC 3.4.22.2 (Papain); K3Z4F929H6 (Lysine); Q1O6DSW23R (4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170129
[St] Status:MEDLINE
[do] DOI:10.1093/jb/mvx005



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