Base de dados : MEDLINE
Pesquisa : D12.776.157.530.450.250 [Categoria DeCS]
Referências encontradas : 8696 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 870 ir para página                         

  1 / 8696 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29214786
[Au] Autor:Kim KY; Bae YS; Ji W; Shin D; Kim HS; Kim DS
[Ad] Endereço:Department of Pediatrics, Yonsei University College of Medicine, Severance Children's Hospital, Seoul, Korea.
[Ti] Título:ITPKC and SLC11A1 Gene Polymorphisms and Gene-Gene Interactions in Korean Patients with Kawasaki Disease.
[So] Source:Yonsei Med J;59(1):119-127, 2018 Jan.
[Is] ISSN:1976-2437
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Kawasaki disease (KD) is an acute systemic vasculitis. Both the etiology of KD and the erythema of Bacille Calmette-Guérin (BCG) injection sites observed in the disease are poorly understood. We investigated the association between KD and single nucleotide polymorphisms (SNPs) in two candidate genes: inositol 1,4,5-triphosphate 3-kinase (ITPKC), a well-studied KD-associated gene, and solute carrier 11a1 (SLC11A1), which is associated with the hypersensitive reaction to the BCG strain in Koreans. MATERIALS AND METHODS: Associations between KD and SNPs in two genes were evaluated. Potential associations between BCG injection site erythema and SNPs in two genes were also evaluated. Gene-gene interactions between ITPKC and SLC11A1 in KD and BCG injection site erythema were also analyzed. RESULTS: Three tagging SNPs in ITPKC and five tagging SNPs in SLC11A1 were genotyped in 299 KD patients and 210 control children. SNP rs28493229 in ITPKC was associated with KD and coronary artery complications. SNP rs77624405 in SLC11A1 was associated with KD. Comparisons of KD patients with and without BCG injection site erythema revealed that SNP rs17235409 in SLC11A1 was associated with erythema; no erythema-associated SNPs in ITPKC were identified. Interactions between ITPKC rs28493229_GG and SLC11A1 rs17235409_GA and between ITPKC rs10420685_GG and SLC11A1 rs17235409_AA were strongly associated with BCG injection site erythema. CONCLUSION: This study identified several important polymorphisms in the ITPKC and SLC11A1 genes in Koreans. The genetic variants identified in this study affected KD and erythema of BCG injection sites independently and through gene-gene interactions. Also, the effects of the polymorphisms were age-dependent.
[Mh] Termos MeSH primário: Grupo com Ancestrais do Continente Asiático/genética
Proteínas de Transporte de Cátions/genética
Epistasia Genética
Predisposição Genética para Doença
Síndrome de Linfonodos Mucocutâneos/genética
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Vacina BCG/administração & dosagem
Estudos de Casos e Controles
Criança
Pré-Escolar
Eritema/complicações
Feminino
Estudos de Associação Genética
Seres Humanos
Lactente
Masculino
Taxa de Mutação
República da Coreia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BCG Vaccine); 0 (Cation Transport Proteins); 0 (natural resistance-associated macrophage protein 1); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.127 (Inositol 1,4,5-trisphosphate 3-kinase)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171208
[St] Status:MEDLINE
[do] DOI:10.3349/ymj.2018.59.1.119


  2 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27771699
[Au] Autor:van Breda GF; Bongartz LG; Zhuang W; van Swelm RP; Pertijs J; Braam B; Cramer MJ; Swinkels DW; Doevendans PA; Verhaar MC; Masereeuw R; Joles JA; Gaillard CA
[Ad] Endereço:Department of Nephrology and Immunology, University of Alberta, Edmonton, Alta., Canada.
[Ti] Título:Cardiac Hepcidin Expression Associates with Injury Independent of Iron.
[So] Source:Am J Nephrol;44(5):368-378, 2016.
[Is] ISSN:1421-9670
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Hepcidin regulates systemic iron homeostasis by downregulating the iron exporter ferroportin. Circulating hepcidin is mainly derived from the liver but hepcidin is also produced in the heart. We studied the differential and local regulation of hepcidin gene expression in response to myocardial infarction (MI) and/or chronic kidney disease (CKD). We hypothesized that cardiac hepcidin gene expression is induced by and regulated to severity of cardiac injury, either through direct (MI) or remote (CKD) stimuli, as well as through increased local iron content. METHODS: Nine weeks after subtotal nephrectomy (SNX) or sham surgery (CON), rats were subjected to coronary ligation (CL) or sham surgery to realize 4 groups: CON, SNX, CL and SNX + CL. In week 16, the gene expression of hepcidin, iron and damage markers in cardiac and liver tissues was assessed by quantitative polymerase chain reaction and ferritin protein expression was studied by immunohistochemistry. RESULTS: Cardiac hepcidin messenger RNA (mRNA) expression was increased 2-fold in CL (p = 0.03) and 3-fold in SNX (p = 0.01). Cardiac ferritin staining was not different among groups. Cardiac hepcidin mRNA expression correlated with mRNA expression levels of brain natriuretic peptide (ß = 0.734, p < 0.001) and connective tissue growth factor (ß = 0.431, p = 0.02). In contrast, liver hepcidin expression was unaffected by SNX and CL alone, while it had decreased 50% in SNX + CL (p < 0.05). Hepatic ferritin immunostaining was not different among groups. CONCLUSIONS: Our data indicate differences in hepcidin regulation in liver and heart and suggest a role for injury rather than iron as the driving force for cardiac hepcidin expression in renocardiac failure.
[Mh] Termos MeSH primário: Hepcidinas/metabolismo
Ferro/metabolismo
Fígado/metabolismo
Infarto do Miocárdio/metabolismo
Miocárdio/metabolismo
Insuficiência Renal Crônica/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteína Morfogenética Óssea 6/metabolismo
Proteína alfa Estimuladora de Ligação a CCAAT/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Fator de Crescimento do Tecido Conjuntivo/metabolismo
Citocinas/metabolismo
Regulação da Expressão Gênica
Heme Oxigenase (Desciclizante)/metabolismo
Masculino
Peptídeo Natriurético Encefálico/metabolismo
Ratos Endogâmicos Lew
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bmp6 protein, rat); 0 (Bone Morphogenetic Protein 6); 0 (CCAAT-Enhancer-Binding Protein-alpha); 0 (Cation Transport Proteins); 0 (Ctgf protein, rat); 0 (Cytokines); 0 (Hepcidins); 0 (metal transporting protein 1); 114471-18-0 (Natriuretic Peptide, Brain); 139568-91-5 (Connective Tissue Growth Factor); E1UOL152H7 (Iron); EC 1.14.14.18 (Heme Oxygenase (Decyclizing)); EC 1.14.14.18 (Hmox1 protein, rat)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  3 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28461400
[Au] Autor:Eroglu S; Giehl RFH; Meier B; Takahashi M; Terada Y; Ignatyev K; Andresen E; Küpper H; Peiter E; von Wirén N
[Ad] Endereço:Molecular Plant Nutrition, Leibniz-Institute for Plant Genetics and Crop Plant Research, D-06466 Gatersleben, Germany.
[Ti] Título:Metal Tolerance Protein 8 Mediates Manganese Homeostasis and Iron Reallocation during Seed Development and Germination.
[So] Source:Plant Physiol;174(3):1633-1647, 2017 Jul.
[Is] ISSN:1532-2548
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Metal accumulation in seeds is a prerequisite for germination and establishment of plants but also for micronutrient delivery to humans. To investigate metal transport processes and their interactions in seeds, we focused on METAL TOLERANCE PROTEIN8 (MTP8), a tonoplast transporter of the manganese (Mn) subclade of cation diffusion facilitators, which in Arabidopsis ( ) is expressed in embryos of seeds. The x-ray fluorescence imaging showed that expression of MTP8 was responsible for Mn localization in subepidermal cells on the abaxial side of the cotyledons and in cortical cells of the hypocotyl. Accordingly, under low Mn availability, MTP8 increased seed stores of Mn, required for efficient seed germination. In mutant embryos lacking expression of ( ), MTP8 built up iron (Fe) hotspots in -expressing cells types, suggesting that MTP8 transports Fe in addition to Mn. In double mutant seeds, Mn and Fe were distributed in all cell types of the embryo. An Fe transport function of MTP8 was confirmed by its ability to complement Fe hypersensitivity of a yeast mutant defective in vacuolar Fe transport. Imbibing mutant seeds in the presence of Mn or subjecting seeds to wet-dry cycles showed that MTP8 conferred Mn tolerance. During germination, MTP8 promoted reallocation of Fe from the vasculature. These results indicate that cell type-specific accumulation of Mn and Fe in seeds depends on MTP8 and that this transporter plays an important role in the generation of seed metal stores as well as for metal homeostasis and germination efficiency under challenging environmental conditions.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/metabolismo
Arabidopsis/embriologia
Arabidopsis/metabolismo
Proteínas de Transporte de Cátions/metabolismo
Germinação
Homeostase
Ferro/metabolismo
Manganês/metabolismo
Sementes/embriologia
[Mh] Termos MeSH secundário: Arabidopsis/genética
Regulação da Expressão Gênica no Desenvolvimento
Regulação da Expressão Gênica de Plantas
Técnicas de Inativação de Genes
Teste de Complementação Genética
Germinação/genética
Modelos Biológicos
Mutação/genética
Regiões Promotoras Genéticas/genética
Saccharomyces cerevisiae/metabolismo
Sementes/genética
Espectrometria por Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Cation Transport Proteins); 0 (MTP8 protein, Arabidopsis); 42Z2K6ZL8P (Manganese); E1UOL152H7 (Iron)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1104/pp.16.01646


  4 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29223159
[Au] Autor:Baleva MV; Meyer M; Entelis N; Tarassov I; Kamenski P; Masquida B
[Ad] Endereço:GMGM, CNRS - University of Strasbourg, UMR 7156, Strasbourg, 67081, France. b.masquida@unistra.fr.
[Ti] Título:Factors beyond Enolase 2 and Mitochondrial Lysyl-tRNA Synthetase Precursor Are Required for tRNA Import into Yeast Mitochondria.
[So] Source:Biochemistry (Mosc);82(11):1324-1335, 2017 Nov.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In yeast, the import of tRNA with CUU anticodon (tRK1) relies on a complex mechanism where interaction with enolase 2 (Eno2p) dictates a deep conformational change of the tRNA. This event is believed to mask the tRNA from the cytosolic translational machinery to re-direct it towards the mitochondria. Once near the mitochondrial outer membrane, the precursor of the mitochondrial lysyl-tRNA synthetase (preMsk1p) takes over enolase to carry the tRNA within the mitochondrial matrix, where it is supposed to participate in translation following correct refolding. Biochemical data presented in this report focus on the role of enolase. They show that despite the inability of Eno2p alone to form a complex with tRK1, mitochondrial import can be recapitulated in vitro using fractions of yeast extracts sharing either recombinant or endogenous yeast Eno2p as one of the main components. Taken together, our data suggest the existence of a protein complex containing Eno2p that is involved in RNA mitochondrial import.
[Mh] Termos MeSH primário: Lisina-tRNA Ligase/fisiologia
Mitocôndrias/metabolismo
Fosfopiruvato Hidratase/fisiologia
RNA de Transferência de Lisina/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/ultraestrutura
[Mh] Termos MeSH secundário: Transporte Biológico
Proteínas de Transporte de Cátions/metabolismo
Mitocôndrias/enzimologia
Complexos Multiproteicos/química
Complexos Multiproteicos/fisiologia
Fosfopiruvato Hidratase/metabolismo
RNA de Transferência/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Multiprotein Complexes); 0 (RNA, Transfer, Lys); 0 (Saccharomyces cerevisiae Proteins); 136956-54-2 (TRK1 protein, S cerevisiae); 9014-25-9 (RNA, Transfer); EC 4.2.1.11 (Phosphopyruvate Hydratase); EC 6.1.1.6 (Lysine-tRNA Ligase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917110104


  5 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28461334
[Au] Autor:Hutchens S; Liu C; Jursa T; Shawlot W; Chaffee BK; Yin W; Gore AC; Aschner M; Smith DR; Mukhopadhyay S
[Ad] Endereço:From the Division of Pharmacology & Toxicology, College of Pharmacy, Institute for Cellular & Molecular Biology, and Institute for Neuroscience and.
[Ti] Título:Deficiency in the manganese efflux transporter SLC30A10 induces severe hypothyroidism in mice.
[So] Source:J Biol Chem;292(23):9760-9773, 2017 06 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Manganese is an essential metal that becomes toxic at elevated levels. Loss-of-function mutations in SLC30A10, a cell-surface-localized manganese efflux transporter, cause a heritable manganese metabolism disorder resulting in elevated manganese levels and parkinsonian-like movement deficits. The underlying disease mechanisms are unclear; therefore, treatment is challenging. To understand the consequences of loss of function at the organism level, we generated knock-out mice. During early development, knock-outs were indistinguishable from controls. Surprisingly, however, after weaning and compared with controls, knock-out mice failed to gain weight, were smaller, and died prematurely (by ∼6-8 weeks of age). At 6 weeks, manganese levels in the brain, blood, and liver of the knock-outs were ∼20-60-fold higher than controls. Unexpectedly, histological analyses revealed that the brain and liver of the knock-outs were largely unaffected, but their thyroid exhibited extensive alterations. Because hypothyroidism leads to growth defects and premature death in mice, we assayed for changes in thyroid and pituitary hormones. At 6 weeks and compared with controls, the knock-outs had markedly reduced thyroxine levels (∼50-80%) and profoundly increased thyroid-stimulating hormone levels (∼800-1000-fold), indicating that knock-out mice develop hypothyroidism. Importantly, a low-manganese diet produced lower tissue manganese levels in the knock-outs and rescued the phenotype, suggesting that manganese toxicity was the underlying cause. Our unanticipated discovery highlights the importance of determining the role of thyroid dysfunction in the onset and progression of manganese-induced disease and identifies knock-out mice as a new model for studying thyroid biology.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/deficiência
Hipotireoidismo/genética
Hipotireoidismo/metabolismo
Manganês/metabolismo
Glândula Tireoide/metabolismo
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Hipotireoidismo/patologia
Camundongos
Camundongos Knockout
Glândula Tireoide/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Cation Transport Proteins); 42Z2K6ZL8P (Manganese)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.783605


  6 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29187939
[Au] Autor:Souraka TDM; Shi MJ; Meng XY
[Ad] Endereço:Département de Diagnostic Génétique, Hôpital Zhongnan de l'Université de Wuhan, 169 Rue Donghu, Wuchang, Wuhan 430071, Chine.
[Ti] Título:[The relationship between tumor recurrence and polymorphisms of hGPX1 and NRAMP1 in superficial bladder cancer patients: a meta-analysis].
[Ti] Título:La relation entre la récurrence de la tumeur et les polymorphismes génétiques de hGPX1 et NRAMP1 chez les patients atteints du cancer superficiel de la vessie: une méta-analyse..
[So] Source:Pan Afr Med J;27:270, 2017.
[Is] ISSN:1937-8688
[Cp] País de publicação:Uganda
[La] Idioma:fre
[Ab] Resumo:Introduction: Previous studies about the relationship between tumor recurrence and NRAMP1 and HGPX1 gene polymorphism in patients with non-muscle-invasive bladder cancer (NMIBC) showed inconsistent results. Methods: We conducted a systematic review of the literature on the basis of data from PubMed and China National Knowledge Infrastructure. According to the predefined selection criteria, the eligibility criteria for the studies found in the literature were assessed by two independent authors. The basic characteristics of the included studies and of data relevant to the meta-analysis were extracted. Patients? survival without recurrence was selected as the measure of effect of meta-analysis. Results: Four publications were retained. Three studies evaluated the NRAMP1 D534N and three the hGPX1 Pro168Leu. Depending on the association between NRAMP1 D534N and tumor recurrence, the meta-analysis revealed no significant heterogeneity and the combined effect was 3.28 [1.77, 6.11]. Depending on the association between hGPX1 Pro198Leu and tumor recurrence, the meta-analysis showed significant heterogeneity and the combined effect was 1.12 [0.45, 2.77]. Publication bias was uncertain, due to the limited number of included studies.The instability of the combined effects was reported. Conclusion: Very little data are available on the association between tumor recurrence and NRAMP1 D534N and hGPX1 Pro168Leu poolymorphisms in patients with NMIBC. The NRAMP1 D534N could increase the risk of recurrence, but hGPX1 Pro168Leu effect is not clear. A more thorough investigation should be conducted on a larger sample size in order to better explain this phenomenon.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/genética
Glutationa Peroxidase/genética
Neoplasias da Bexiga Urinária/patologia
[Mh] Termos MeSH secundário: Seres Humanos
Recidiva Local de Neoplasia/genética
Polimorfismo Genético
Análise de Sobrevida
Neoplasias da Bexiga Urinária/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (natural resistance-associated macrophage protein 1); EC 1.11.1.- (glutathione peroxidase GPX1); EC 1.11.1.9 (Glutathione Peroxidase)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171201
[St] Status:MEDLINE
[do] DOI:10.11604/pamj.2017.27.270.12282


  7 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28941825
[Au] Autor:Smith AT; Sestok AE
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, MD, 21250, USA. Electronic address: smitha@umbc.edu.
[Ti] Título:Expression and purification of functionally active ferrous iron transporter FeoB from Klebsiella pneumoniae.
[So] Source:Protein Expr Purif;142:1-7, 2018 Feb.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The acquisition of ferrous iron (Fe ) is an important virulence factor utilized by several hospital-acquired (nosocomial) pathogens such as Klebsiella pneumoniae to establish infection within human hosts. Virtually all bacteria use the ferrous iron transport system (Feo) to acquire ferrous iron from their environments, which are often biological niches that stabilize Fe relative to Fe . However, the details of this process remain poorly understood, likely owing to the few expression and purification systems capable of supplying sufficient quantities of the chief component of the Feo system, the integral membrane GTPase FeoB. This bottleneck has undoubtedly hampered efforts to understand this system in order to target it for therapeutic intervention. In this study, we describe the expression, solubilization, and purification of the Fe transporter from K. pneumoniae, KpFeoB. We show that this protein may be heterologously overexpressed in Escherichia coli as the host organism. After testing several different commercially-available detergents, we have developed a solubilization and purification protocol that produces milligram quantities of KpFeoB with sufficient purity for enzymatic and biophysical analyses. Importantly, we demonstrate that KpFeoB displays robust GTP hydrolysis activity (k of ∼10 s ) in the absence of any additional stimulatory factors. Our findings suggest that K. pneumoniae may be capable of using its Feo system to drive Fe import in an active manner.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Proteínas de Transporte de Cátions/genética
Guanosina Trifosfato/metabolismo
Ferro/metabolismo
Klebsiella pneumoniae/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/isolamento & purificação
Proteínas de Bactérias/metabolismo
Proteínas de Transporte de Cátions/química
Proteínas de Transporte de Cátions/isolamento & purificação
Proteínas de Transporte de Cátions/metabolismo
Cátions Bivalentes
Clonagem Molecular
Detergentes/química
Ensaios Enzimáticos
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Hidrólise
Transporte de Íons
Cinética
Klebsiella pneumoniae/enzimologia
Maltose/análogos & derivados
Maltose/química
Plasmídeos/química
Plasmídeos/metabolismo
Polietilenoglicóis/química
Conformação Proteica em alfa-Hélice
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Solubilidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Cation Transport Proteins); 0 (Cations, Divalent); 0 (Detergents); 0 (Recombinant Proteins); 0 (dodecyl maltopyranoside); 3055-98-9 (dodecyloctaethyleneglycol monoether); 30IQX730WE (Polyethylene Glycols); 69-79-4 (Maltose); 86-01-1 (Guanosine Triphosphate); E1UOL152H7 (Iron)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170925
[St] Status:MEDLINE


  8 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29054412
[Au] Autor:Duck KA; Simpson IA; Connor JR
[Ad] Endereço:Department of Neurosurgery, Penn State Hershey Medical Center, Hershey, PA, United States.
[Ti] Título:Regulatory mechanisms for iron transport across the blood-brain barrier.
[So] Source:Biochem Biophys Res Commun;494(1-2):70-75, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Many critical metabolic functions in the brain require adequate and timely delivery of iron. However, most studies when considering brain iron uptake have ignored the iron requirements of the endothelial cells that form the blood-brain barrier (BBB). Moreover, current models of BBB iron transport do not address regional regulation of brain iron uptake or how neurons, when adapting to metabolic demands, can acquire more iron. In this study, we demonstrate that both iron-poor transferrin (apo-Tf) and the iron chelator, deferoxamine, stimulate release of iron from iron-loaded endothelial cells in an in vitro BBB model. The role of the endosomal divalent metal transporter 1 (DMT1) in BBB iron acquisition and transport has been questioned. Here, we show that inhibition of DMT1 alters the transport of iron and Tf across the endothelial cells. These data support an endosome-mediated model of Tf-bound iron uptake into the brain and identifies mechanisms for local regional regulation of brain iron uptake. Moreover, our data provide an explanation for the disparity in the ratio of Tf to iron transport into the brain that has confounded the field.
[Mh] Termos MeSH primário: Barreira Hematoencefálica/metabolismo
Ferro/metabolismo
[Mh] Termos MeSH secundário: Animais
Transporte Biológico Ativo/efeitos dos fármacos
Barreira Hematoencefálica/efeitos dos fármacos
Encéfalo/irrigação sanguínea
Encéfalo/metabolismo
Proteínas de Transporte de Cátions/antagonistas & inibidores
Proteínas de Transporte de Cátions/metabolismo
Bovinos
Células Cultivadas
Endossomos/metabolismo
Células Endoteliais/metabolismo
Hepcidinas/metabolismo
Microvasos/metabolismo
Modelos Neurológicos
Transferrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (Hepcidins); 0 (Transferrin); 0 (solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2); E1UOL152H7 (Iron)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171022
[St] Status:MEDLINE


  9 / 8696 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29038209
[Au] Autor:Packer M
[Ad] Endereço:From Baylor Heart and Vascular Institute, Baylor University Medical Center, Dallas, TX. milton.packer@baylorhealth.edu.
[Ti] Título:Activation and Inhibition of Sodium-Hydrogen Exchanger Is a Mechanism That Links the Pathophysiology and Treatment of Diabetes Mellitus With That of Heart Failure.
[So] Source:Circulation;136(16):1548-1559, 2017 Oct 17.
[Is] ISSN:1524-4539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mechanisms underlying the progression of diabetes mellitus and heart failure are closely intertwined, such that worsening of one condition is frequently accompanied by worsening of the other; the degree of clinical acceleration is marked when the 2 coexist. Activation of the sodium-hydrogen exchanger in the heart and vasculature (NHE1 isoform) and the kidneys (NHE3 isoform) may serve as a common mechanism that links both disorders and may underlie their interplay. Insulin insensitivity and adipokine abnormalities (the hallmarks of type 2 diabetes mellitus) are characteristic features of heart failure; conversely, neurohormonal systems activated in heart failure (norepinephrine, angiotensin II, aldosterone, and neprilysin) impair insulin sensitivity and contribute to microvascular disease in diabetes mellitus. Each of these neurohormonal derangements may act through increased activity of both NHE1 and NHE3. Drugs used to treat diabetes mellitus may favorably affect the pathophysiological mechanisms of heart failure by inhibiting either or both NHE isoforms, and drugs used to treat heart failure may have beneficial effects on glucose tolerance and the complications of diabetes mellitus by interfering with the actions of NHE1 and NHE3. The efficacy of NHE inhibitors on the risk of cardiovascular events may be enhanced when heart failure and glucose intolerance coexist and may be attenuated when drugs with NHE inhibitory actions are given concomitantly. Therefore, the sodium-hydrogen exchanger may play a central role in the interplay of diabetes mellitus and heart failure, contribute to the physiological and clinical progression of both diseases, and explain certain drug-drug and drug-disease interactions that have been reported in large-scale randomized clinical trials.
[Mh] Termos MeSH primário: Proteínas de Transporte de Cátions/metabolismo
Diabetes Mellitus/metabolismo
Insuficiência Cardíaca/metabolismo
Trocadores de Sódio-Hidrogênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Fármacos Cardiovasculares/efeitos adversos
Proteínas de Transporte de Cátions/antagonistas & inibidores
Comorbidade
Diabetes Mellitus/tratamento farmacológico
Diabetes Mellitus/epidemiologia
Diabetes Mellitus/fisiopatologia
Progressão da Doença
Interações Medicamentosas
Insuficiência Cardíaca/tratamento farmacológico
Insuficiência Cardíaca/epidemiologia
Insuficiência Cardíaca/fisiopatologia
Seres Humanos
Hipoglicemiantes/efeitos adversos
Polimedicação
Fatores de Risco
Trocador 1 de Sódio-Hidrogênio
Trocador 3 de Sódio-Hidrogênio
Trocadores de Sódio-Hidrogênio/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cardiovascular Agents); 0 (Cation Transport Proteins); 0 (Hypoglycemic Agents); 0 (SLC9A1 protein, human); 0 (SLC9A3 protein, human); 0 (Sodium-Hydrogen Exchanger 1); 0 (Sodium-Hydrogen Exchanger 3); 0 (Sodium-Hydrogen Exchangers)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171018
[St] Status:MEDLINE
[do] DOI:10.1161/CIRCULATIONAHA.117.030418


  10 / 8696 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29023457
[Au] Autor:Tolone C; Bellini G; Punzo F; Papparella A; Miele E; Vitale A; Nobili B; Strisciuglio C; Rossi F
[Ad] Endereço:Department of Woman, Child and of General and Specialist Surgery, University of Campania "Luigi Vanvitelli", Naples, Italy.
[Ti] Título:The DMT1 IVS4+44C>A polymorphism and the risk of iron deficiency anemia in children with celiac disease.
[So] Source:PLoS One;12(10):e0185822, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Iron deficiency anemia in celiac disease is related to impaired duodenal mucosal uptake, due to villous atrophy. Iron enters the enterocytes through an apical divalent metal transporter, DMT1. Different DMT1 transcripts have been identified, depending on the presence of an iron-responsive element that allows DMT1 up-regulation during iron starvation. An intronic DMT1 polymorphism, IVS4+44C>A, has been associated with metal toxicity, and the CC-carriers show high iron levels. AIMS: This study investigates the association between DMT1 IVS4+44C>A and anemia in a cohort of 387 Italian celiac children, and the functional role of the polymorphism. METHODS AND RESULTS: By association analysis, we found that DMT1 IVS4+44-AA genotype confers a four-fold risk of developing anemia, despite of atrophy degree. By analysis of mRNA from gastroesophageal biopsies, we found that total DMT1 is significantly upregulated in presence of mild, but not severe, atrophy, independently from IVS4+44C>A variant, and in normal but not in atrophic CC-biopsies. Moreover, we found that A-allele is associated to preferential expression of the DMT1 transcripts lacking the iron-responsive element, thus limiting the DMT1 overexpression that normally occurs to respond to iron starvation. DISCUSSION: Possibly, the IVS4+44-AA-related dysregulation of the iron-induced changes in DMT1 expression is not able to impair iron absorption in physiological condition. However, if exacerbated by the concomitant massive loss of functional absorbing tissue paralleling worsened stages of villus atrophy, it might be ineffective in counteracting iron deficiency, despite of DMT1 overexpression. CONCLUSION: We suggest, for the first time, that celiac disease may unmask the contribution of the DMT1 IVS4+44C>A polymorphism to the risk of anemia.
[Mh] Termos MeSH primário: Alelos
Anemia Ferropriva
Proteínas de Transporte de Cátions
Doença Celíaca
Regulação da Expressão Gênica
Polimorfismo Genético
[Mh] Termos MeSH secundário: Adolescente
Anemia Ferropriva/etiologia
Anemia Ferropriva/genética
Anemia Ferropriva/metabolismo
Anemia Ferropriva/patologia
Biópsia
Proteínas de Transporte de Cátions/biossíntese
Proteínas de Transporte de Cátions/genética
Doença Celíaca/complicações
Doença Celíaca/genética
Doença Celíaca/metabolismo
Doença Celíaca/patologia
Criança
Pré-Escolar
Estudos de Coortes
Feminino
Seres Humanos
Lactente
Masculino
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; MULTICENTER STUDY
[Nm] Nome de substância:
0 (Cation Transport Proteins); 0 (solute carrier family 11- (proton-coupled divalent metal ion transporters), member 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171022
[Lr] Data última revisão:
171022
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185822



página 1 de 870 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde