Base de dados : MEDLINE
Pesquisa : D12.776.157.530.625.875.500.300 [Categoria DeCS]
Referências encontradas : 28 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 3 ir para página          

  1 / 28 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27458020
[Au] Autor:Maldonado EN; DeHart DN; Patnaik J; Klatt SC; Gooz MB; Lemasters JJ
[Ad] Endereço:From the Center for Cell Death, Injury, and Regeneration, Departments of Drug Discovery and Biomedical Sciences and the Hollings Cancer Center, Medical University of South Carolina, Charleston, South Carolina 29425 and.
[Ti] Título:ATP/ADP Turnover and Import of Glycolytic ATP into Mitochondria in Cancer Cells Is Independent of the Adenine Nucleotide Translocator.
[So] Source:J Biol Chem;291(37):19642-50, 2016 Sep 09.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Non-proliferating cells oxidize respiratory substrates in mitochondria to generate a protonmotive force (Δp) that drives ATP synthesis. The mitochondrial membrane potential (ΔΨ), a component of Δp, drives release of mitochondrial ATP(4-) in exchange for cytosolic ADP(3-) via the electrogenic adenine nucleotide translocator (ANT) located in the mitochondrial inner membrane, which leads to a high cytosolic ATP/ADP ratio up to >100-fold greater than matrix ATP/ADP. In rat hepatocytes, ANT inhibitors, bongkrekic acid (BA), and carboxyatractyloside (CAT), and the F1FO-ATP synthase inhibitor, oligomycin (OLIG), inhibited ureagenesis-induced respiration. However, in several cancer cell lines, OLIG but not BA and CAT inhibited respiration. In hepatocytes, respiratory inhibition did not collapse ΔΨ until OLIG, BA, or CAT was added. Similarly, in cancer cells OLIG and 2-deoxyglucose, a glycolytic inhibitor, depolarized mitochondria after respiratory inhibition, which showed that mitochondrial hydrolysis of glycolytic ATP maintained ΔΨ in the absence of respiration in all cell types studied. However in cancer cells, BA, CAT, and knockdown of the major ANT isoforms, ANT2 and ANT3, did not collapse ΔΨ after respiratory inhibition. These findings indicated that ANT did mediate mitochondrial ATP/ADP exchange in cancer cells. We propose that suppression of ANT contributes to low cytosolic ATP/ADP, activation of glycolysis, and a Warburg metabolic phenotype in proliferating cells.
[Mh] Termos MeSH primário: Translocador 2 do Nucleotídeo Adenina/metabolismo
Translocador 3 do Nucleotídeo Adenina/metabolismo
Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Hepatócitos/metabolismo
Mitocôndrias Hepáticas/metabolismo
Proteínas de Neoplasias/metabolismo
Neoplasias/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Inibidores Enzimáticos/farmacologia
Glicólise/efeitos dos fármacos
Hepatócitos/patologia
Masculino
Mitocôndrias Hepáticas/patologia
Neoplasias/tratamento farmacológico
Neoplasias/patologia
Consumo de Oxigênio/efeitos dos fármacos
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 2); 0 (Adenine Nucleotide Translocator 3); 0 (Enzyme Inhibitors); 0 (Neoplasm Proteins); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171014
[Lr] Data última revisão:
171014
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.734814


  2 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27030664
[Au] Autor:Ruhr IM; Takei Y; Grosell M
[Ad] Endereço:Department of Marine Biology and Ecology, The Rosenstiel School of Marine and Atmospheric Science, The University of Miami, Miami, Florida; and iruhr@rsmas.miami.edu.
[Ti] Título:The role of the rectum in osmoregulation and the potential effect of renoguanylin on SLC26a6 transport activity in the Gulf toadfish (Opsanus beta).
[So] Source:Am J Physiol Regul Integr Comp Physiol;311(1):R179-91, 2016 Jul 01.
[Is] ISSN:1522-1490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Teleosts living in seawater continually absorb water across the intestine to compensate for branchial water loss to the environment. The present study reveals that the Gulf toadfish (Opsanus beta) rectum plays a comparable role to the posterior intestine in ion and water absorption. However, the posterior intestine appears to rely more on SLC26a6 (a HCO3 (-)/Cl(-) antiporter) and the rectum appears to rely on NKCC2 (SLC12a1) for the purposes of solute-coupled water absorption. The present study also demonstrates that the rectum responds to renoguanylin (RGN), a member of the guanylin family of peptides that alters the normal osmoregulatory processes of the distal intestine, by inhibited water absorption. RGN decreases rectal water absorption more greatly than in the posterior intestine and leads to net Na(+) and Cl(-) secretion, and a reversal of the absorptive short-circuit current (ISC). It is hypothesized that maintaining a larger fluid volume within the distal segments of intestinal tract facilitates the removal of CaCO3 precipitates and other solids from the intestine. Indeed, the expression of the components of the Cl(-)-secretory response, apical CFTR, and basolateral NKCC1 (SLC12a2), are upregulated in the rectum of the Gulf toadfish after 96 h in 60 ppt, an exposure that increases CaCO3 precipitate formation relative to 35 ppt. Moreover, the downstream intracellular effects of RGN appear to directly inhibit ion absorption by NKCC2 and anion exchange by SLC26a6. Overall, the present findings elucidate key electrophysiological differences between the posterior intestine and rectum of Gulf toadfish and the potent regulatory role renoguanylin plays in osmoregulation.
[Mh] Termos MeSH primário: Translocador 3 do Nucleotídeo Adenina/metabolismo
Batracoidiformes/metabolismo
Hormônios Gastrointestinais/farmacologia
Peptídeos Natriuréticos/farmacologia
Osmorregulação/efeitos dos fármacos
Reto/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Bicarbonatos/metabolismo
Transporte Biológico Ativo/efeitos dos fármacos
Carbonato de Cálcio/farmacologia
Cloretos/metabolismo
Intestinos/efeitos dos fármacos
Intestinos/metabolismo
Sódio/metabolismo
Membro 1 da Família 12 de Carreador de Soluto/metabolismo
Água/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 3); 0 (Bicarbonates); 0 (Chlorides); 0 (Gastrointestinal Hormones); 0 (Natriuretic Peptides); 0 (Solute Carrier Family 12, Member 1); 059QF0KO0R (Water); 140653-38-9 (guanylin); 9NEZ333N27 (Sodium); H0G9379FGK (Calcium Carbonate)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1152/ajpregu.00033.2016


  3 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26212361
[Au] Autor:Guo X; Huang Y; Qi Y; Liu Z; Ma Y; Shao Y; Jiang S; Sun Z; Ruan Q
[Ad] Endereço:Virus Laboratory, Affiliated Shengjing Hospital, China Medical University, Shenyang, 110004, Liaoning, China.
[Ti] Título:Human cytomegalovirus miR-UL36-5p inhibits apoptosis via downregulation of adenine nucleotide translocator 3 in cultured cells.
[So] Source:Arch Virol;160(10):2483-90, 2015 Oct.
[Is] ISSN:1432-8798
[Cp] País de publicação:Austria
[La] Idioma:eng
[Ab] Resumo:Human cytomegalovirus (HCMV) encodes at least 26 microRNAs (miRNA). These miRNAs are utilized by HCMV to regulate its own genes as well as the genes of the host cell during infection. It has been reported that a cellular gene, solute carrier family 25, member 6 (SLC25A6), which is also designated adenine nucleotide translocator 3 (ANT3), was identified as a candidate target of hcmv-miR-UL36-5p by hybrid PCR. In this study, ANT3 was further demonstrated to be a direct target of hcmv-miR-UL36-5p by luciferase reporter assays. The expression level of ANT3 protein was confirmed, by western blotting, to be directly downregulated by overexpression of hcmv-miR-UL36-5p in HEK293 cells, U373 cells and HELF cells. Moreover, HCMV-infected cells showed a decrease in the ANT3 protein level. Using ANT3-specific small interfering RNA (siRNA) and an inhibitor for hcmv-miR-UL36-5p, it was shown that inhibition of apoptosis by hcmv-miR-UL36-5p in these cells specifically occurred via inhibition of ANT3 expression. These results imply that hcmv-miR-UL36-5 may play the same role during actual HCMV infection in order to establish a balance between the host cell and the virus.
[Mh] Termos MeSH primário: Translocador 3 do Nucleotídeo Adenina/genética
Apoptose
Infecções por Citomegalovirus/genética
Citomegalovirus/metabolismo
MicroRNAs/metabolismo
RNA Viral/metabolismo
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Translocador 3 do Nucleotídeo Adenina/metabolismo
Linhagem Celular
Citomegalovirus/genética
Infecções por Citomegalovirus/metabolismo
Infecções por Citomegalovirus/fisiopatologia
Infecções por Citomegalovirus/virologia
Regulação para Baixo
Regulação Viral da Expressão Gênica
Seres Humanos
MicroRNAs/genética
RNA Viral/genética
Proteínas Virais/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 3); 0 (MicroRNAs); 0 (RNA, Viral); 0 (UL36 protein, Human herpesvirus 1); 0 (Viral Proteins)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150926
[Lr] Data última revisão:
150926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150728
[St] Status:MEDLINE
[do] DOI:10.1007/s00705-015-2498-8


  4 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:23506884
[Au] Autor:Clémençon B; Babot M; Trézéguet V
[Ad] Endereço:Institute of Biochemistry and Molecular Medicine, NCCR TransCure, University of Bern, Bern, Switzerland. benjamin.clemencon@ibmm.unibe.ch
[Ti] Título:The mitochondrial ADP/ATP carrier (SLC25 family): pathological implications of its dysfunction.
[So] Source:Mol Aspects Med;34(2-3):485-93, 2013 Apr-Jun.
[Is] ISSN:1872-9452
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In aerobic eukaryotic cells, the high energy metabolite ATP is generated mainly within the mitochondria following the process of oxidative phosphorylation. The mitochondrial ATP is exported to the cytoplasm using a specialized transport protein, the ADP/ATP carrier, to provide energy to the cell. Any deficiency or dysfunction of this membrane protein leads to serious consequences on cell metabolism and can cause various diseases such as muscular dystrophy. Described as a decisive player in the programmed cell death, it was recently shown to play a role in cancer. The objective of this review is to summarize the current knowledge of the involvement of the ADP/ATP carrier, encoded by the SLC25A4, SLC25A5, SLC25A6 and SLC25A31 genes, in human diseases and of the efforts made at designing different model systems to study this carrier and the associated pathologies through biochemical, genetic, and structural approaches.
[Mh] Termos MeSH primário: Apoptose/fisiologia
Redes e Vias Metabólicas/fisiologia
Translocases Mitocondriais de ADP e ATP/genética
Translocases Mitocondriais de ADP e ATP/fisiologia
Modelos Moleculares
Família Multigênica/genética
Neoplasias/fisiopatologia
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Translocador 2 do Nucleotídeo Adenina/metabolismo
Translocador 3 do Nucleotídeo Adenina/metabolismo
Sequência de Aminoácidos
Apoptose/genética
Seres Humanos
Redes e Vias Metabólicas/genética
Translocases Mitocondriais de ADP e ATP/metabolismo
Modelos Biológicos
Dados de Sequência Molecular
Neoplasias/genética
Conformação Proteica
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Adenine Nucleotide Translocator 2); 0 (Adenine Nucleotide Translocator 3); 0 (SLC25A31 protein, human); 0 (SLC25A4 protein, human); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1309
[Cu] Atualização por classe:130319
[Lr] Data última revisão:
130319
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130320
[St] Status:MEDLINE


  5 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:22978616
[Au] Autor:Dupont PY; Guttin A; Issartel JP; Stepien G
[Ad] Endereço:INRA, UMR 1019, Unité de Nutrition Humaine, 63122, St Genès-Champanelle, France.
[Ti] Título:Computational identification of transcriptionally co-regulated genes, validation with the four ANT isoform genes.
[So] Source:BMC Genomics;13:482, 2012 Sep 15.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The analysis of gene promoters is essential to understand the mechanisms of transcriptional regulation required under the effects of physiological processes, nutritional intake or pathologies. In higher eukaryotes, transcriptional regulation implies the recruitment of a set of regulatory proteins that bind on combinations of nucleotide motifs. We developed a computational analysis of promoter nucleotide sequences, to identify co-regulated genes by combining several programs that allowed us to build regulatory models and perform a crossed analysis on several databases. This strategy was tested on a set of four human genes encoding isoforms 1 to 4 of the mitochondrial ADP/ATP carrier ANT. Each isoform has a specific tissue expression profile linked to its role in cellular bioenergetics. RESULTS: From their promoter sequence and from the phylogenetic evolution of these ANT genes in mammals, we constructed combinations of specific regulatory elements. These models were screened using the full human genome and databases of promoter sequences from human and several other mammalian species. For each of transcriptionally regulated ANT1, 2 and 4 genes, a set of co-regulated genes was identified and their over-expression was verified in microarray databases. CONCLUSIONS: Most of the identified genes encode proteins with a cellular function and specificity in agreement with those of the corresponding ANT isoform. Our in silico study shows that the tissue specific gene expression is mainly driven by promoter regulatory sequences located up to about a thousand base pairs upstream the transcription start site. Moreover, this computational strategy on the study of regulatory pathways should provide, along with transcriptomics and metabolomics, data to construct cellular metabolic networks.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
Translocador 2 do Nucleotídeo Adenina/genética
Translocador 3 do Nucleotídeo Adenina/genética
Regulação da Expressão Gênica/genética
Translocases Mitocondriais de ADP e ATP/genética
Transcrição Genética/genética
[Mh] Termos MeSH secundário: Biologia Computacional
Análise de Sequência com Séries de Oligonucleotídeos
Regiões Promotoras Genéticas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Adenine Nucleotide Translocator 2); 0 (Adenine Nucleotide Translocator 3); 0 (SLC25A31 protein, human); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1302
[Cu] Atualização por classe:150223
[Lr] Data última revisão:
150223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120918
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2164-13-482


  6 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:22187496
[Au] Autor:Echaniz-Laguna A; Chassagne M; Ceresuela J; Rouvet I; Padet S; Acquaviva C; Nataf S; Vinzio S; Bozon D; Mousson de Camaret B
[Ad] Endereço:Département de Neurologie, Hôpitaux Universitaires, Strasbourg cedex, France. andoni.echaniz-laguna@chru-strasbourg.fr
[Ti] Título:Complete loss of expression of the ANT1 gene causing cardiomyopathy and myopathy.
[So] Source:J Med Genet;49(2):146-50, 2012 Feb.
[Is] ISSN:1468-6244
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The ANT1 gene, encoding ADP/ATP translocase 1, was investigated in an adult patient with an autosomal recessive mitochondrial disorder characterised by congenital cataracts, hypertrophic cardiomyopathy, myopathy and lactic acidosis. METHODS AND RESULTS: ANT1 sequencing showed that the patient was homozygous for a new nucleotide variation, c.111+1G→A, abolishing the invariant GT splice donor site of intron 1. The ANT1 transcript was undetectable in both muscle and skin fibroblasts. A markedly abnormal metabolic profile was found, and skeletal muscle showed a dramatic proliferation of abnormal mitochondria, increased mitochondrial mass, and multiple mitochondrial DNA deletions. No compensating increase in the transcript level of the ANT3 gene, which encodes the human ubiquitous isoform of the ADP/ATP translocase, was observed. The patient's heterozygous mother had normal clinical, biochemical and pathological features. CONCLUSIONS: Complete loss of expression of the ANT1 gene causes a clinical syndrome mainly characterised by cardiomyopathy and myopathy. This report expands the clinical spectrum of ANT1-related human diseases, and emphasises the crucial role of the mitochondrial ADP/ATP carriers in muscle function and pathophysiology of human myopathies.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
Cardiomiopatia Hipertrófica/genética
Miopatias Mitocondriais/genética
[Mh] Termos MeSH secundário: Translocador 3 do Nucleotídeo Adenina/genética
Adulto
Sequência de Bases
Cardiomiopatia Hipertrófica/diagnóstico
Células Cultivadas
DNA Polimerase gama
DNA Polimerase Dirigida por DNA/genética
Éxons
Feminino
Expressão Gênica
Seres Humanos
Imagem por Ressonância Magnética
Miopatias Mitocondriais/diagnóstico
Músculo Esquelético/metabolismo
Músculo Esquelético/patologia
Músculo Esquelético/ultraestrutura
Mutação
Neuroimagem
Linhagem
Adulto Jovem
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Adenine Nucleotide Translocator 3); EC 2.7.7.7 (DNA Polymerase gamma); EC 2.7.7.7 (DNA-Directed DNA Polymerase); EC 2.7.7.7 (POLG protein, human)
[Em] Mês de entrada:1205
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:111222
[St] Status:MEDLINE
[do] DOI:10.1136/jmedgenet-2011-100504


  7 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:21858006
[Au] Autor:Lim CH; Hamazaki T; Braun EL; Wade J; Terada N
[Ad] Endereço:Department of Pathology, College of Medicine, University of Florida, Gainesville, Florida, United States of America.
[Ti] Título:Evolutionary genomics implies a specific function of Ant4 in mammalian and anole lizard male germ cells.
[So] Source:PLoS One;6(8):e23122, 2011.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Most vertebrates have three paralogous genes with identical intron-exon structures and a high degree of sequence identity that encode mitochondrial adenine nucleotide translocase (Ant) proteins, Ant1 (Slc25a4), Ant2 (Slc25a5) and Ant3 (Slc25a6). Recently, we and others identified a fourth mammalian Ant paralog, Ant4 (Slc25a31), with a distinct intron-exon structure and a lower degree of sequence identity. Ant4 was expressed selectively in testis and sperm in adult mammals and was indeed essential for mouse spermatogenesis, but it was absent in birds, fish and frogs. Since Ant2 is X-linked in mammalian genomes, we hypothesized that the autosomal Ant4 gene may compensate for the loss of Ant2 gene expression during male meiosis in mammals. Here we report that the Ant4 ortholog is conserved in green anole lizard (Anolis carolinensis) and demonstrate that it is expressed in the anole testis. Further, a degenerate DNA fragment of putative Ant4 gene was identified in syntenic regions of avian genomes, indicating that Ant4 was present in the common amniote ancestor. Phylogenetic analyses suggest an even more ancient origin of the Ant4 gene. Although anole lizards are presumed male (XY) heterogametic, like mammals, copy numbers of the Ant2 as well as its neighboring gene were similar between male and female anole genomes, indicating that the anole Ant2 gene is either autosomal or located in the pseudoautosomal region of the sex chromosomes, in contrast to the case to mammals. These results imply the conservation of Ant4 is not likely simply driven by the sex chromosomal localization of the Ant2 gene and its subsequent inactivation during male meiosis. Taken together with the fact that Ant4 protein has a uniquely conserved structure when compared to other somatic Ant1, 2 and 3, there may be a specific advantage for mammals and lizards to express Ant4 in their male germ cells.
[Mh] Termos MeSH primário: Genômica/métodos
Lagartos/genética
Mamíferos/genética
Translocases Mitocondriais de ADP e ATP/genética
Proteínas de Répteis/genética
Espermatozoides/metabolismo
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/genética
Translocador 1 do Nucleotídeo Adenina/metabolismo
Translocador 2 do Nucleotídeo Adenina/genética
Translocador 2 do Nucleotídeo Adenina/metabolismo
Translocador 3 do Nucleotídeo Adenina/genética
Translocador 3 do Nucleotídeo Adenina/metabolismo
Sequência de Aminoácidos
Animais
Proteínas Aviárias/genética
Proteínas Aviárias/metabolismo
Galinhas
Mapeamento Cromossômico
Evolução Molecular
Feminino
Regulação Enzimológica da Expressão Gênica
Seres Humanos
Lagartos/metabolismo
Masculino
Mamíferos/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Translocases Mitocondriais de ADP e ATP/classificação
Translocases Mitocondriais de ADP e ATP/metabolismo
Dados de Sequência Molecular
Filogenia
Proteínas de Répteis/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Homologia de Sequência de Aminoácidos
Espermatozoides/enzimologia
Sintenia
Testículo/citologia
Testículo/enzimologia
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Adenine Nucleotide Translocator 2); 0 (Adenine Nucleotide Translocator 3); 0 (Avian Proteins); 0 (Reptilian Proteins); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1202
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:110823
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0023122


  8 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:20060930
[Au] Autor:Gallerne C; Touat Z; Chen ZX; Martel C; Mayola E; Sharaf el dein O; Buron N; Le Bras M; Jacotot E; Borgne-Sanchez A; Lemoine A; Lemaire C; Pervaiz S; Brenner C
[Ad] Endereço:LGBC, CNRS UMR8159, Université Versailles-SQY, PRES Universud Paris, 45, avenue des Etats-Unis, 78035 Versailles, France.
[Ti] Título:The fourth isoform of the adenine nucleotide translocator inhibits mitochondrial apoptosis in cancer cells.
[So] Source:Int J Biochem Cell Biol;42(5):623-9, 2010 May.
[Is] ISSN:1878-5875
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The adenine nucleotide translocator (ANT) is a mitochondrial bi-functional protein, which catalyzes the exchange of ADP and ATP between cytosol and mitochondria and participates in many models of mitochondrial apoptosis. The human adenine nucleotide translocator sub-family is composed of four isoforms, namely ANT1-4, encoded by four nuclear genes, whose expression is highly regulated. Previous studies have revealed that ANT1 and 3 induce mitochondrial apoptosis, whereas ANT2 is anti-apoptotic. However, the role of the recently identified isoform ANT4 in the apoptotic pathway has not yet been elucidated. Here, we investigated the effects of stable heterologous expression of the ANT4 on proliferation, mitochondrial respiration and cell death in human cancer cells, using ANT3 as a control of pro-apoptotic isoform. As expected, ANT3 enhanced mitochondria-mediated apoptosis in response to lonidamine, a mitochondriotoxic chemotherapeutic drug, and staurosporine, a protein kinase inhibitor. Our results also indicate that the pro-apoptotic effect of ANT3 was accompanied by decreased rate of cell proliferation, alteration in the mitochondrial network topology, and decreased reactive oxygen species production. Of note, we demonstrate for the first time that ANT4 enhanced cell growth without impacting mitochondrial network or respiration. Moreover, ANT4 differentially regulated the intracellular levels of hydrogen peroxide without affecting superoxide anion levels. Finally, stable ANT4 overexpression protected cancer cells from lonidamine and staurosporine apoptosis in a manner independent of Bcl-2 expression. These data highlight a hitherto undefined cytoprotective activity of ANT4, and provide a novel dichotomy in the human ANT isoform sub-family with ANT1 and 3 isoforms functioning as pro-apoptotic while ANT2 and 4 isoforms render cells resistant to death inducing stimuli.
[Mh] Termos MeSH primário: Apoptose
Mitocôndrias/fisiologia
Translocases Mitocondriais de ADP e ATP/fisiologia
[Mh] Termos MeSH secundário: Translocador 3 do Nucleotídeo Adenina/biossíntese
Translocador 3 do Nucleotídeo Adenina/genética
Translocador 3 do Nucleotídeo Adenina/fisiologia
Antineoplásicos/farmacologia
Caspase 9/metabolismo
Proliferação Celular
Forma Celular
Citoproteção
Células HeLa
Seres Humanos
Peróxido de Hidrogênio/análise
Indazóis/farmacologia
Isoenzimas/biossíntese
Isoenzimas/genética
Isoenzimas/fisiologia
Translocases Mitocondriais de ADP e ATP/biossíntese
Translocases Mitocondriais de ADP e ATP/sangue
Translocases Mitocondriais de ADP e ATP/genética
Fosforilação Oxidativa
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Estaurosporina/farmacologia
Superóxidos/análise
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 3); 0 (Antineoplastic Agents); 0 (Indazoles); 0 (Isoenzymes); 0 (Protein Kinase Inhibitors); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (SLC25A31 protein, human); 11062-77-4 (Superoxides); 9068-80-8 (Mitochondrial ADP, ATP Translocases); BBX060AN9V (Hydrogen Peroxide); EC 3.4.22.- (Caspase 9); H88EPA0A3N (Staurosporine); U78804BIDR (lonidamine)
[Em] Mês de entrada:1006
[Cu] Atualização por classe:131121
[Lr] Data última revisão:
131121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100112
[St] Status:MEDLINE
[do] DOI:10.1016/j.biocel.2009.12.024


  9 / 28 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:19763879
[Au] Autor:Yang L; He Y; Kong Q; Zhang W; Xi D; Mao H; Deng W
[Ad] Endereço:Faculty of Animal Science and Technology, Yunnan Agricultural University, Kunming 650201, China.
[Ti] Título:Isolation, nucleotide identification and tissue expression of three novel ovine genes-SLC25A4, SLC25A5 and SLC25A6.
[So] Source:Mol Biol Rep;37(6):2743-8, 2010 Jul.
[Is] ISSN:1573-4978
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The complete coding sequences of three of sheep genes SLC25A4, SLC25A5 and SLC25A6 were firstly amplified using the reverse transcriptase polymerase chain reaction (RT-PCR) according to the conserved sequence information of the cattle or other mammals and known highly homologous sheep ESTs. Sheep SLC25A4, SLC25A5 and SLC25A6 genes encode three corresponding proteins of 298 amino acids which contain the identically conserved putative mitochondrial carrier protein domain. Sheep SLC25A4 protein has high homology with the SLC25A4 proteins of six species-cattle (99%), human (95%), rat (95%), mouse (94%), dog (94%) and chicken (89%). Sheep SLC25A5 protein has high identity with the SLC25A5 proteins of five species-cattle (100%), dog (99%), mouse (98%), rat (98%) and human (98%). Sheep SLC25A6 protein also has high homology with the SLC25A6 proteins of four species-cattle (99%), human (97%), pig (97%) and chicken (93%). The phylogenetic tree analysis demonstrated that sheep SLC25A4, SLC25A5 and SLC25A6 proteins share a common ancestor. Moreover, SLC25A4, SLC25A5 and SLC25A6 proteins present stronger interaction each other. The tissue expression analysis indicated that sheep SLC25A4, SLC25A5 and SLC25A6 genes were expressed in a range of tissues including leg muscle, kidney, skin, longissimus dorsi muscle, spleen, heart and liver. Our experiment is the first to provide the primary foundation for further insight into these three sheep genes.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
Translocador 2 do Nucleotídeo Adenina/genética
Translocador 3 do Nucleotídeo Adenina/genética
Perfilação da Expressão Gênica
Ovinos/genética
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/química
Translocador 1 do Nucleotídeo Adenina/metabolismo
Translocador 2 do Nucleotídeo Adenina/química
Translocador 2 do Nucleotídeo Adenina/metabolismo
Translocador 3 do Nucleotídeo Adenina/química
Translocador 3 do Nucleotídeo Adenina/metabolismo
Animais
Sequência de Bases
Regulação da Expressão Gênica
Dados de Sequência Molecular
Filogenia
Ligação Proteica
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Análise de Sequência de DNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Adenine Nucleotide Translocator 2); 0 (Adenine Nucleotide Translocator 3)
[Em] Mês de entrada:1010
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090919
[St] Status:MEDLINE
[do] DOI:10.1007/s11033-009-9812-z


  10 / 28 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:19669810
[Au] Autor:Danishuddin M; Khan SN; Khan AU
[Ad] Endereço:Aligarh Muslim University, Aligarh, 202002, India.
[Ti] Título:Molecular interactions between mitochondrial membrane proteins and the C-terminal domain of PB1-F2: an in silico approach.
[So] Source:J Mol Model;16(3):535-41, 2010 Mar.
[Is] ISSN:0948-5023
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PB1-F2 is a recently described influenza A viral protein that induces apoptosis by binding with two mitochondrial membrane proteins, i.e. VDAC1 (outer membrane) and ANT3 (inner membrane). Knowledge of this binding mechanism could provide insights that would aid in the design of novel inhibitors against this protein. Therefore, to better understand these interactions, we have undertaken this study to model the PB1-F2 protein of the highly pathogenic influenza A virus subtype H5N1. Moreover, a model of human ANT3 was also established. The dynamics of the molecular interactions between the C-terminal region of PB1-F2 protein and VDAC1 and ANT3 were expounded by employing an in silico approach. Our results suggest the involvement of 12 amino acids of PB1-F2 protein, which form hydrophobic contacts with 22 amino acids of VDAC1. Of these, Leu64, Arg75 and Val76 were found to be crucial for mitochondrial targetting. In the case of the PB1-F2-ANT3 complex, 14 amino acids of ANT3 were found to make hydrophobic contacts with 9 amino acids of PB1-F2. Furthermore, two hydrogen bonds were predicted in both complexes PB1-F2/VDAC1 and PB1-F2/ANT3. This study reveals the molecular interactions required for PB1-F2-induced apoptosis and suggests a hypothetical model for future study.
[Mh] Termos MeSH primário: Translocador 3 do Nucleotídeo Adenina/química
Translocador 3 do Nucleotídeo Adenina/metabolismo
Biologia Computacional
Membranas Mitocondriais/química
Modelos Moleculares
Proteínas Virais/química
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Seres Humanos
Ligações de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Vírus da Influenza A/classificação
Dados de Sequência Molecular
Ligação Proteica
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Homologia Estrutural de Proteína
Canal de Ânion 1 Dependente de Voltagem/química
Canal de Ânion 1 Dependente de Voltagem/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 3); 0 (PB1-F2 protein, Influenza A virus); 0 (Viral Proteins); EC 1.6.- (Voltage-Dependent Anion Channel 1)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090812
[St] Status:MEDLINE
[do] DOI:10.1007/s00894-009-0555-5



página 1 de 3 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