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Pesquisa : D12.776.157.530.625.875.500.100 [Categoria DeCS]
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  1 / 171 MEDLINE  
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[PMID]:28947214
[Au] Autor:Dallabona C; Baruffini E; Goffrini P; Lodi T
[Ad] Endereço:Department of Chemistry, Life Sciences and Environmental Sustainability, University of Parma, 43124 Parma, Italy.
[Ti] Título:Dominance of yeast aac2 and aac2 mutations, equivalent to pathological mutations in ant1, is due to gain of function.
[So] Source:Biochem Biophys Res Commun;493(2):909-913, 2017 Nov 18.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitochondrial ADP/ATP carrier is a nuclear encoded protein, which catalyzes the exchange of ATP generated in mitochondria with ADP produced in the cytosol. In humans, mutations in the major ADP/ATP carrier gene, ANT1, are involved in several degenerative mitochondrial pathologies, leading to instability of mitochondrial DNA. Recessive mutations have been associated with mitochondrial myopathy and cardiomyopathy whereas dominant mutations have been associated with autosomal dominant Progressive External Ophtalmoplegia (adPEO). Recently, two de novo dominant mutations, R80H and R235G, leading to extremely severe symptoms, have been identified. In order to evaluate if the dominance is due to haploinsufficiency or to a gain of function, the two mutations have been introduced in the equivalent positions of the AAC2 gene, the yeast orthologue of human ANT1, and their dominant effect has been studied in heteroallelic strains, containing both one copy of wild type AAC2 and one copy of mutant aac2 allele. Through phenotypic characterization of these yeast models we showed that the OXPHOS phenotypes in the heteroallelic strains were more affected than in the hemiallelic strain indicating that the dominant trait of the two mutations is due to gain of function.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
DNA Mitocondrial/genética
Translocases Mitocondriais de ADP e ATP/genética
Miopatias Mitocondriais/genética
Mutação Puntual
Proteínas de Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/genética
[Mh] Termos MeSH secundário: Alelos
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (DNA, Mitochondrial); 0 (PET9 protein, S cerevisiae); 0 (SLC25A4 protein, human); 0 (Saccharomyces cerevisiae Proteins); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE


  2 / 171 MEDLINE  
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[PMID]:28712724
[Au] Autor:Vukotic M; Nolte H; König T; Saita S; Ananjew M; Krüger M; Tatsuta T; Langer T
[Ad] Endereço:Institute for Genetics, Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Center for Molecular Medicine (CMMC), University of Cologne, Cologne, Germany.
[Ti] Título:Acylglycerol Kinase Mutated in Sengers Syndrome Is a Subunit of the TIM22 Protein Translocase in Mitochondria.
[So] Source:Mol Cell;67(3):471-483.e7, 2017 Aug 03.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in mitochondrial acylglycerol kinase (AGK) cause Sengers syndrome, which is characterized by cataracts, hypertrophic cardiomyopathy, and skeletal myopathy. AGK generates phosphatidic acid and lysophosphatidic acid, bioactive phospholipids involved in lipid signaling and the regulation of tumor progression. However, the molecular mechanisms of the mitochondrial pathology remain enigmatic. Determining its mitochondrial interactome, we have identified AGK as a constituent of the TIM22 complex in the mitochondrial inner membrane. AGK assembles with TIMM22 and TIMM29 and supports the import of a subset of multi-spanning membrane proteins. The function of AGK as a subunit of the TIM22 complex does not depend on its kinase activity. However, enzymatically active AGK is required to maintain mitochondrial cristae morphogenesis and the apoptotic resistance of cells. The dual function of AGK as lipid kinase and constituent of the TIM22 complex reveals that disturbances in both phospholipid metabolism and mitochondrial protein biogenesis contribute to the pathogenesis of Sengers syndrome.
[Mh] Termos MeSH primário: Cardiomiopatias/enzimologia
Catarata/enzimologia
Mitocôndrias/enzimologia
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Antiporters/metabolismo
Apoptose
Proteínas de Ligação ao Cálcio/metabolismo
Cardiomiopatias/genética
Cardiomiopatias/patologia
Catarata/genética
Catarata/patologia
Predisposição Genética para Doença
Células HEK293
Células HeLa
Seres Humanos
Mitocôndrias/patologia
Proteínas de Transporte da Membrana Mitocondrial/genética
Proteínas Mitocondriais/metabolismo
Complexos Multiproteicos
Mutação
Fenótipo
Fosfolipídeos/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Transporte Proteico
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Antiporters); 0 (Calcium-Binding Proteins); 0 (Mitochondrial Membrane Transport Proteins); 0 (Mitochondrial Proteins); 0 (Multiprotein Complexes); 0 (Phospholipids); 0 (SLC25A24 protein, human); 0 (SLC25A4 protein, human); 0 (TIM29 protein, human); EC 2.7.1.- (AGK protein, human); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170718
[St] Status:MEDLINE


  3 / 171 MEDLINE  
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[PMID]:27861892
[Au] Autor:Jiang H; Zhang C; Tang Y; Zhao J; Wang T; Liu H; Sun X
[Ad] Endereço:Otolaryngology Key Lab, Qilu Hospital of Shandong University, Jinan, Shandong, China.
[Ti] Título:The regulator of calcineurin 1 increases adenine nucleotide translocator 1 and leads to mitochondrial dysfunctions.
[So] Source:J Neurochem;140(2):307-319, 2017 Jan.
[Is] ISSN:1471-4159
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The over-expression of regulator of calcineurin 1 isoform 1 (RCAN1.1) has been implicated in mitochondrial dysfunctions of Alzheimer's disease; however, the mechanism linking RCAN1.1 over-expression and the mitochondrial dysfunctions remains unknown. In this study, we use human neuroblastoma SH-SY5Y cells stably expressing RCAN1.1S and rat primary neurons infected with RCAN1.1S expression lentivirus to study the association of RCAN1 with mitochondrial functions. Our study here showed that the over-expression of RCAN1.1S remarkably up-regulates the expression of adenine nucleotide translocator (ANT1) by stabilizing ANT1 mRNA. The increased ANT1 level leads to accelerated ATP-ADP exchange rate, more Ca -induced mitochondrial permeability transition pore opening, increased cytochrome c release, and eventually cell apoptosis. Furthermore, knockdown of ANT1 expression brings these mitochondria perturbations caused by RCAN1.1S back to normal. The effect of RCAN1.1S on ANT1 was independent of its inhibition on calcineurin. This study elucidated a novel function of RCAN1 in mitochondria and provides a molecular basis for the RCAN1.1S over-expression-induced mitochondrial dysfunctions and neuronal apoptosis.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Calcineurina/metabolismo
Mitocôndrias/metabolismo
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Citocromos c/metabolismo
Seres Humanos
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas Musculares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Intracellular Signaling Peptides and Proteins); 0 (Mitochondrial Membrane Transport Proteins); 0 (Muscle Proteins); 0 (mitochondrial permeability transition pore); 9007-43-6 (Cytochromes c); EC 3.1.3.16 (Calcineurin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1111/jnc.13900


  4 / 171 MEDLINE  
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[PMID]:27876151
[Au] Autor:Basavalingappa RH; Massilamany C; Krishnan B; Gangaplara A; Kang G; Khalilzad-Sharghi V; Han Z; Othman S; Li Q; Riethoven JJ; Sobel RA; Steffen D; Reddy J
[Ad] Endereço:School of Veterinary Medicine and Biomedical Sciences, University of Nebraska-Lincoln, Lincoln, Nebraska.
[Ti] Título:Identification of an Epitope from Adenine Nucleotide Translocator 1 That Induces Inflammation in Heart in A/J Mice.
[So] Source:Am J Pathol;186(12):3160-3175, 2016 Dec.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Heart failure, a leading cause of death in humans, can emanate from myocarditis. Although most individuals with myocarditis recover spontaneously, some develop chronic dilated cardiomyopathy. Myocarditis may result from both infectious and noninfectious causes, including autoimmune responses to cardiac antigens. In support of this notion, intracellular cardiac antigens, like cardiac myosin heavy chain-α, cardiac troponin-I, and adenine nucleotide translocator 1 (ANT ), have been identified as autoantigens in cardiac autoimmunity. Herein, we demonstrate that ANT can induce autoimmune myocarditis in A/J mice by generating autoreactive T cells. We show that ANT encompasses multiple immunodominant epitopes (namely, ANT 21-40, ANT 31-50, ANT 171-190, and ANT 181-200). Although all four peptides induce comparable T-cell responses, only ANT 21-40 was found to be a major myocarditogenic epitope in immunized animals. The myocarditis-inducing ability of ANT 21-40 was associated with the generation of T cells producing predominantly IL-17A, and the antigen-sensitized T cells could transfer the disease to naïve recipients. These data indicate that cardiac mitochondrial proteins can be target autoantigens in myocarditis, supporting the notion that the antigens released as a result of primary damage may contribute to the persistence of chronic inflammation through autoimmunity.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/imunologia
Autoantígenos/imunologia
Cardiomiopatia Dilatada/fisiopatologia
Miocardite/imunologia
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Animais
Miosinas Cardíacas/metabolismo
Cardiomiopatia Dilatada/etiologia
Epitopos
Feminino
Coração/fisiopatologia
Seres Humanos
Inflamação
Interleucina-17/metabolismo
Camundongos
Proteínas Mitocondriais/imunologia
Proteínas Mitocondriais/metabolismo
Miocardite/complicações
Miocardite/fisiopatologia
Linfócitos T/imunologia
Troponina I/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Autoantigens); 0 (Epitopes); 0 (Interleukin-17); 0 (Mitochondrial Proteins); 0 (Troponin I); EC 3.6.1.- (Cardiac Myosins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE


  5 / 171 MEDLINE  
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[PMID]:27786441
[Au] Autor:Hedger G; Rouse SL; Domanski J; Chavent M; Koldsø H; Sansom MS
[Ad] Endereço:Department of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, U.K.
[Ti] Título:Lipid-Loving ANTs: Molecular Simulations of Cardiolipin Interactions and the Organization of the Adenine Nucleotide Translocase in Model Mitochondrial Membranes.
[So] Source:Biochemistry;55(45):6238-6249, 2016 Nov 15.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The exchange of ADP and ATP across the inner mitochondrial membrane is a fundamental cellular process. This exchange is facilitated by the adenine nucleotide translocase, the structure and function of which are critically dependent on the signature phospholipid of mitochondria, cardiolipin (CL). Here we employ multiscale molecular dynamics simulations to investigate CL interactions within a membrane environment. Using simulations at both coarse-grained and atomistic resolutions, we identify three CL binding sites on the translocase, in agreement with those seen in crystal structures and inferred from nuclear magnetic resonance measurements. Characterization of the free energy landscape for lateral lipid interaction via potential of mean force calculations demonstrates the strength of interaction compared to those of binding sites on other mitochondrial membrane proteins, as well as their selectivity for CL over other phospholipids. Extending the analysis to other members of the family, yeast Aac2p and mouse uncoupling protein 2, suggests a degree of conservation. Simulation of large patches of a model mitochondrial membrane containing multiple copies of the translocase shows that CL interactions persist in the presence of protein-protein interactions and suggests CL may mediate interactions between translocases. This study provides a key example of how computational microscopy may be used to shed light on regulatory lipid-protein interactions.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Cardiolipinas/metabolismo
Membranas Mitocondriais/metabolismo
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/química
Animais
Sítios de Ligação
Cardiolipinas/química
Bovinos
Cristalografia por Raios X
Espectroscopia de Ressonância Magnética
Camundongos
Translocases Mitocondriais de ADP e ATP/química
Translocases Mitocondriais de ADP e ATP/metabolismo
Ligação Proteica
Domínios Proteicos
Proteínas de Saccharomyces cerevisiae/química
Proteínas de Saccharomyces cerevisiae/metabolismo
Termodinâmica
Proteína Desacopladora 2/química
Proteína Desacopladora 2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Cardiolipins); 0 (PET9 protein, S cerevisiae); 0 (Saccharomyces cerevisiae Proteins); 0 (Uncoupling Protein 2); 9068-80-8 (Mitochondrial ADP, ATP Translocases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170522
[Lr] Data última revisão:
170522
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161028
[St] Status:MEDLINE


  6 / 171 MEDLINE  
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[PMID]:27717697
[Au] Autor:Song XB; Liu G; Wang ZY; Wang L
[Ad] Endereço:College of Animal Science and Veterinary Medicine, Shandong Agricultural University, Daizong Road No. 61, Tai'an 271018, People's Republic of China.
[Ti] Título:Puerarin protects against cadmium-induced proximal tubular cell apoptosis by restoring mitochondrial function.
[So] Source:Chem Biol Interact;260:219-231, 2016 Dec 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Puerarin (PU) is a potent free radical scavenger with a protective effect in nephrotoxin-mediated oxidative damage. Here, we show a novel molecular mechanism by which PU exerts its anti-apoptotic effects in cadmium (Cd)-exposed primary rat proximal tubular (rPT) cells. Morphological assessment and flow cytometric analysis revealed that PU significantly decreased Cd-induced apoptotic cell death of rPT cells. Administration of PU protected cells against Cd-induced depletion of mitochondrial membrane potential (ΔΨm) and lipid peroxidation. Cd-mediated mitochondrial permeability transition pore (MPTP) opening, disruption of mitochondrial ultrastructure, mitochondrial cytochrome c (cyt-c) release, caspase-3 activation and subsequently poly ADP-ribose polymerase (PARP) cleavage could be effectively blocked by the addition of PU. Moreover, up-regulation of Bcl-2 and down-regulation of Bax and hence increased Bcl-2/Bax ratio were observed with the PU administration. In addition, PU reversed Cd-induced ATP depletion by restoring ΔΨm to affect ATP production and by regulating expression levels of ANT-1 and ANT-2 to improve ATP transport. In summary, PU inhibited Cd-induced apoptosis in rPT cells by ameliorating the mitochondrial dysfunction.
[Mh] Termos MeSH primário: Cádmio/toxicidade
Isoflavonas/farmacologia
Túbulos Renais Proximais/patologia
Mitocôndrias/metabolismo
Substâncias Protetoras/farmacologia
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/genética
Translocador 1 do Nucleotídeo Adenina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Apoptose/efeitos dos fármacos
Caspase 3/metabolismo
Forma Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Citocromos c/metabolismo
Ativação Enzimática/efeitos dos fármacos
Espaço Intracelular/metabolismo
Isoflavonas/administração & dosagem
Túbulos Renais Proximais/efeitos dos fármacos
Túbulos Renais Proximais/ultraestrutura
Malondialdeído/metabolismo
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/ultraestrutura
Proteínas de Transporte da Membrana Mitocondrial/metabolismo
Modelos Biológicos
Poli(ADP-Ribose) Polimerases/metabolismo
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ratos Sprague-Dawley
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Isoflavones); 0 (Mitochondrial Membrane Transport Proteins); 0 (Protective Agents); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); 0 (Reactive Oxygen Species); 0 (mitochondrial permeability transition pore); 00BH33GNGH (Cadmium); 4Y8F71G49Q (Malondialdehyde); 8L70Q75FXE (Adenosine Triphosphate); 9007-43-6 (Cytochromes c); EC 2.4.2.30 (Poly(ADP-ribose) Polymerases); EC 3.4.22.- (Caspase 3); Z9W8997416 (puerarin)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161009
[St] Status:MEDLINE


  7 / 171 MEDLINE  
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[PMID]:27693233
[Au] Autor:Thompson K; Majd H; Dallabona C; Reinson K; King MS; Alston CL; He L; Lodi T; Jones SA; Fattal-Valevski A; Fraenkel ND; Saada A; Haham A; Isohanni P; Vara R; Barbosa IA; Simpson MA; Deshpande C; Puusepp S; Bonnen PE; Rodenburg RJ; Suomalainen A; Õunap K; Elpeleg O; Ferrero I; McFarland R; Kunji ER; Taylor RW
[Ad] Endereço:Wellcome Trust Centre for Mitochondrial Research, Institute of Neuroscience, Newcastle University, Newcastle upon Tyne NE2 4HH, UK.
[Ti] Título:Recurrent De Novo Dominant Mutations in SLC25A4 Cause Severe Early-Onset Mitochondrial Disease and Loss of Mitochondrial DNA Copy Number.
[So] Source:Am J Hum Genet;99(4):860-876, 2016 10 06.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutations in SLC25A4 encoding the mitochondrial ADP/ATP carrier AAC1 are well-recognized causes of mitochondrial disease. Several heterozygous SLC25A4 mutations cause adult-onset autosomal-dominant progressive external ophthalmoplegia associated with multiple mitochondrial DNA deletions, whereas recessive SLC25A4 mutations cause childhood-onset mitochondrial myopathy and cardiomyopathy. Here, we describe the identification by whole-exome sequencing of seven probands harboring dominant, de novo SLC25A4 mutations. All affected individuals presented at birth, were ventilator dependent and, where tested, revealed severe combined mitochondrial respiratory chain deficiencies associated with a marked loss of mitochondrial DNA copy number in skeletal muscle. Strikingly, an identical c.239G>A (p.Arg80His) mutation was present in four of the seven subjects, and the other three case subjects harbored the same c.703C>G (p.Arg235Gly) mutation. Analysis of skeletal muscle revealed a marked decrease of AAC1 protein levels and loss of respiratory chain complexes containing mitochondrial DNA-encoded subunits. We show that both recombinant AAC1 mutant proteins are severely impaired in ADP/ATP transport, affecting most likely the substrate binding and mechanics of the carrier, respectively. This highly reduced capacity for transport probably affects mitochondrial DNA maintenance and in turn respiration, causing a severe energy crisis. The confirmation of the pathogenicity of these de novo SLC25A4 mutations highlights a third distinct clinical phenotype associated with mutation of this gene and demonstrates that early-onset mitochondrial disease can be caused by recurrent de novo mutations, which has significant implications for the application and analysis of whole-exome sequencing data in mitochondrial disease.
[Mh] Termos MeSH primário: Translocador 1 do Nucleotídeo Adenina/genética
Variações do Número de Cópias de DNA/genética
DNA Mitocondrial/genética
Genes Dominantes/genética
Doenças Mitocondriais/genética
Mutação
[Mh] Termos MeSH secundário: Difosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Idade de Início
Arilamina N-Acetiltransferase/genética
Criança
Pré-Escolar
Transporte de Elétrons/genética
Exoma/genética
Feminino
Seres Humanos
Lactente
Recém-Nascido
Isoenzimas/genética
Masculino
Doenças Mitocondriais/patologia
Músculo Esquelético/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (DNA, Mitochondrial); 0 (Isoenzymes); 0 (SLC25A4 protein, human); 61D2G4IYVH (Adenosine Diphosphate); 8L70Q75FXE (Adenosine Triphosphate); EC 2.3.1.5 (Arylamine N-Acetyltransferase); EC 2.3.1.5 (N-acetyltransferase 1)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171125
[Lr] Data última revisão:
171125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


  8 / 171 MEDLINE  
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[PMID]:27658776
[Au] Autor:Dong YY; Zhuang YH; Cai WJ; Liu Y; Zou WB
[Ad] Endereço:Department of Surgical Oncology, First Hospital of Quanzhou Affiliated to Fujian Medical University, Quanzhou, Fujian, 362000, China. yangyangfuzhou59@126.com.
[Ti] Título:The mitochondrion interfering compound NPC-26 exerts potent anti-pancreatic cancer cell activity in vitro and in vivo.
[So] Source:Tumour Biol;37(11):15053-15063, 2016 Nov.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The development of novel anti-pancreatic cancer agents is extremely important. Here, we investigated the anti-pancreatic cancer activity by NPC-26, a novel mitochondrion interfering compound. We showed that NPC-26 was anti-proliferative and cytotoxic to human pancreatic cancer cells, possibly via inducing caspase-9-dependent cell apoptosis. Pharmacological inhibition or shRNA-mediated silence of caspase-9 attenuated NPC-26-induced pancreatic cancer cell death and apoptosis. Further, NPC-26 treatment led to mitochondrial permeability transition pore (mPTP) opening in the cancer cells, which was evidenced by mitochondrial depolarization, ANT-1(adenine nucleotide translocator-1)-Cyp-D (cyclophilin-D) association and oxidative phosphorylation disturbance. mPTP blockers (cyclosporin and sanglifehrin A) or shRNA-mediated knockdown of key mPTP components (Cyp-D and ANT-1) dramatically attenuated NPC-26-induced pancreatic cancer cell apoptosis. Importantly, we showed that NPC-26, at a low concentration, potentiated gemcitabine-induced mPTP opening and subsequent pancreatic cancer cell apoptosis. In vivo, NPC-26 intraperitoneal injection significantly suppressed the growth of PANC-1 xenograft tumors in nude mice. Meanwhile, NPC-26 sensitized gemcitabine-mediated anti-pancreatic cancer activity in vivo. In summary, the results of this study suggest that NPC-26, alone or together with gemcitabine, potently inhibits pancreatic cancer cells possibly via disrupting mitochondrion.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Apoptose/efeitos dos fármacos
Desoxicitidina/análogos & derivados
Mitocôndrias/efeitos dos fármacos
Proteínas de Transporte da Membrana Mitocondrial/efeitos dos fármacos
Neoplasias Pancreáticas/patologia
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/metabolismo
Monofosfato de Adenosina/metabolismo
Trifosfato de Adenosina/metabolismo
Adulto
Animais
Western Blotting
Proliferação Celular/efeitos dos fármacos
Ciclofilinas/metabolismo
Desoxicitidina/farmacologia
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Técnicas Imunoenzimáticas
Técnicas In Vitro
Camundongos
Camundongos Nus
Meia-Idade
Mitocôndrias/metabolismo
Neoplasias Pancreáticas/tratamento farmacológico
Neoplasias Pancreáticas/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Células Tumorais Cultivadas
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Antineoplastic Agents); 0 (Mitochondrial Membrane Transport Proteins); 0 (Reactive Oxygen Species); 0 (SLC25A4 protein, human); 0 (mitochondrial permeability transition pore); 0W860991D6 (Deoxycytidine); 415SHH325A (Adenosine Monophosphate); 8L70Q75FXE (Adenosine Triphosphate); B76N6SBZ8R (gemcitabine); EC 5.2.1.- (Cyclophilins); EC 5.2.1.8 (cyclophilin D)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160924
[St] Status:MEDLINE


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[PMID]:27067366
[Au] Autor:Dulermo R; Gamboa-Meléndez H; Ledesma-Amaro R; Thevenieau F; Nicaud JM
[Ad] Endereço:Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350, Jouy-en-Josas, France. Electronic address: remi.dulermo@grignon.inra.fr.
[Ti] Título:Yarrowia lipolytica AAL genes are involved in peroxisomal fatty acid activation.
[So] Source:Biochim Biophys Acta;1861(7):555-65, 2016 Jul.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:In yeast, ß-oxidation of fatty acids (FAs) essentially takes place in peroxisomes, and FA activation must precede FA oxidation. In Saccharomyces cerevisiae, a single fatty-acyl­CoA-synthetase, ScFaa2p, mediates peroxisomal FA activation. We have previously shown that this reaction also exists in the oleaginous yeast Yarrowia lipolytica; however, the protein involved in this process remains unknown. Here, we found that proteins, named Aal proteins (Acyl/Aryl-CoA-ligases), resembling the 4-coumarate­CoA-ligase-like enzymes found in plants are involved in peroxisomal FA activation in Y. lipolytica; Y. lipolytica has 10 AAL genes, eight of which are upregulated by oleate. All the Aal proteins contain a PTS1-type peroxisomal targeting sequence (A/SKL), suggesting a peroxisomal localization. The function of the Aal proteins was analyzed using the faa1Δant1Δ mutant strain, which demonstrates neither cytoplasmic FA activation (direct result of FAA1 deletion) nor peroxisomal FA activation (indirect result of ANT1 deletion, a gene coding an ATP transporter). This strain is thus highly sensitive to external FA levels and unable to store external FAs in lipid bodies (LBs). Whereas the overexpression of (cytoplasmic) AAL1ΔPTS1 was able to partially complement the growth defect observed in the faa1Δant1Δ mutant on short-, medium- and long-chain FA media, the presence of Aal2p to Aal10p only allowed growth on the short-chain FA medium. Additionally, partial LB formation was observed in the oleate medium for strains overexpressing Aal1ΔPTS1p, Aal4ΔPTS1p, Aal7ΔPTS1p, and Aal8ΔPTS1p. Finally, an analysis of the FA content of cells grown in the oleate medium suggested that Aal4p and Aal6p present substrate specificity for C16:1 and/or C18:0.
[Mh] Termos MeSH primário: Coenzima A Ligases/genética
Ácidos Graxos/metabolismo
Proteínas Fúngicas/genética
Regulação Fúngica da Expressão Gênica
Peroxissomos/enzimologia
Yarrowia/genética
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/deficiência
Translocador 1 do Nucleotídeo Adenina/genética
Sequência de Aminoácidos
Transporte Biológico
Coenzima A Ligases/metabolismo
Proteínas Fúngicas/metabolismo
Isoenzimas
Gotículas Lipídicas/química
Gotículas Lipídicas/enzimologia
Dados de Sequência Molecular
Oxirredução
Receptor 1 de Sinal de Orientação para Peroxissomos
Peroxissomos/química
Filogenia
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/genética
Alinhamento de Sequência
Transdução de Sinais
Especificidade por Substrato
Yarrowia/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1); 0 (Fatty Acids); 0 (Fungal Proteins); 0 (Isoenzymes); 0 (Peroxisome-Targeting Signal 1 Receptor); 0 (Receptors, Cytoplasmic and Nuclear); EC 6.2.1.- (Coenzyme A Ligases)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160413
[St] Status:MEDLINE


  10 / 171 MEDLINE  
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[PMID]:27050514
[Au] Autor:Lin-Hendel EG; McManus MJ; Wallace DC; Anderson SA; Golden JA
[Ad] Endereço:School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA; Developmental, Regenerative and Stem Cell Biology, Biomedical Graduate Group, University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Título:Differential Mitochondrial Requirements for Radially and Non-radially Migrating Cortical Neurons: Implications for Mitochondrial Disorders.
[So] Source:Cell Rep;15(2):229-37, 2016 Apr 12.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial dysfunction has been increasingly linked to neurodevelopmental disorders such as intellectual disability, childhood epilepsy, and autism spectrum disorder, conditions also associated with cortical GABAergic interneuron dysfunction. Although interneurons have some of the highest metabolic demands in the postnatal brain, the importance of mitochondria during interneuron development is unknown. We find that interneuron migration from the basal forebrain to the neocortex is highly sensitive to perturbations in oxidative phosphorylation. Both pharmacologic and genetic inhibition of adenine nucleotide transferase 1 (Ant1) disrupts the non-radial migration of interneurons, but not the radial migration of cortical projection neurons. The selective dependence of cortical interneuron migration on oxidative phosphorylation may be a mechanistic pathway upon which multiple developmental and metabolic pathologies converge.
[Mh] Termos MeSH primário: Movimento Celular
Córtex Cerebral/patologia
Mitocôndrias/metabolismo
Doenças Mitocondriais/patologia
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Translocador 1 do Nucleotídeo Adenina/deficiência
Translocador 1 do Nucleotídeo Adenina/metabolismo
Animais
Centrossomo/metabolismo
Embrião de Mamíferos/patologia
Feminino
Interneurônios/patologia
Masculino
Camundongos Endogâmicos C57BL
Mutação/genética
Fosforilação Oxidativa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adenine Nucleotide Translocator 1)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160407
[St] Status:MEDLINE



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