Base de dados : MEDLINE
Pesquisa : G04.655 [Categoria DeCS]
Referências encontradas : 130 [refinar]
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[PMID]:27876470
[Au] Autor:Aureille J; Belaadi N; Guilluy C
[Ad] Endereço:Institute for Advanced Biosciences, Inserm U1209, CNRS UMR 5309, Université Grenoble Alpes, 38000 Grenoble, France.
[Ti] Título:Mechanotransduction via the nuclear envelope: a distant reflection of the cell surface.
[So] Source:Curr Opin Cell Biol;44:59-67, 2017 Feb.
[Is] ISSN:1879-0410
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:As the largest and stiffest organelle in the cell, the nucleus can be subjected to significant forces generated by the cytoskeleton to adjust its shape and position, and accommodate the cellular machinery during cell migration, differentiation or division. As it was anticipated, recent work showed that mechanosensitive mechanisms exist in the nucleus and regulate its structure and function in response to mechanical force. While the molecular mechanisms that mediate this response are only beginning to be elucidated, the nuclear envelope seems to play a central role in this process. Here, we review these nuclear mechanosensitive mechanisms and highlight their functional homology with those located at the cell surface. Additionally, we discuss how these nuclear envelope mechanisms function during adhesion and migration, and how they participate in cytoskeletal organization, via direct physical contact or signaling event regulation.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Mecanotransdução Celular
Membrana Nuclear/metabolismo
[Mh] Termos MeSH secundário: Animais
Membrana Celular/química
Movimento Celular
Núcleo Celular/metabolismo
Citoesqueleto/metabolismo
Seres Humanos
Membrana Nuclear/química
Forma das Organelas
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161124
[St] Status:MEDLINE


  2 / 130 MEDLINE  
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[PMID]:27025901
[Au] Autor:Chou SJ; Tseng WL; Chen CT; Lai YF; Chien CS; Chang YL; Lee HC; Wei YH; Chiou SH
[Ad] Endereço:Institute of Pharmacology, Taipei, Taiwan.
[Ti] Título:Impaired ROS Scavenging System in Human Induced Pluripotent Stem Cells Generated from Patients with MERRF Syndrome.
[So] Source:Sci Rep;6:23661, 2016 Mar 30.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Myoclonus epilepsy associated with ragged-red fibers (MERRF) is a mitochondrial disorder characterized by myoclonus epilepsy, generalized seizures, ataxia and myopathy. MERRF syndrome is primarily due to an A to G mutation at mtDNA 8344 that disrupts the mitochondrial gene for tRNA(Lys). However, the detailed mechanism by which this tRNA(Lys) mutation causes mitochondrial dysfunction in cardiomyocytes or neurons remains unclear. In this study, we generated human induced pluripotent stem cells (hiPSCs) that carry the A8344G genetic mutation from patients with MERRF syndrome. Compared with mutation-free isogenic hiPSCs, MERRF-specific hiPSCs (MERRF-hiPSCs) exhibited reduced oxygen consumption, elevated reactive oxygen species (ROS) production, reduced growth, and fragmented mitochondrial morphology. We sought to investigate the induction ability and mitochondrial function of cardiomyocyte-like cells differentiated from MERRF-hiPSCs. Our data demonstrate that that cardiomyocyte-like cells (MERRF-CMs) or neural progenitor cells (MERRF-NPCs) differentiated from MERRF-iPSCs also exhibited increased ROS levels and altered antioxidant gene expression. Furthermore, MERRF-CMs or -NPCs contained fragmented mitochondria, as evidenced by MitoTracker Red staining and transmission electron microscopy. Taken together, these findings showed that MERRF-hiPSCs and MERRF-CM or -NPC harboring the A8344G genetic mutation displayed contained mitochondria with an abnormal ultrastructure, produced increased ROS levels, and expressed upregulated antioxidant genes.
[Mh] Termos MeSH primário: Células-Tronco Pluripotentes Induzidas/metabolismo
Síndrome MERRF/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Adolescente
Desdiferenciação Celular
Diferenciação Celular
Células Cultivadas
DNA Mitocondrial/genética
Feminino
Seres Humanos
Células-Tronco Pluripotentes Induzidas/patologia
Síndrome MERRF/patologia
Mitocôndrias Cardíacas/metabolismo
Mitocôndrias Cardíacas/patologia
Miócitos Cardíacos/metabolismo
Miócitos Cardíacos/patologia
Forma das Organelas
Consumo de Oxigênio
Mutação Puntual
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170217
[Lr] Data última revisão:
170217
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160331
[St] Status:MEDLINE
[do] DOI:10.1038/srep23661


  3 / 130 MEDLINE  
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[PMID]:26663076
[Au] Autor:Evans-Roberts KM; Mitchenall LA; Wall MK; Leroux J; Mylne JS; Maxwell A
[Ad] Endereço:From the Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
[Ti] Título:DNA Gyrase Is the Target for the Quinolone Drug Ciprofloxacin in Arabidopsis thaliana.
[So] Source:J Biol Chem;291(7):3136-44, 2016 Feb 12.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Arabidopsis thaliana genome contains four genes that were originally annotated as potentially encoding DNA gyrase: ATGYRA, ATGYRB1, ATGYRB2, and ATGYRB3. Although we subsequently showed that ATGYRB3 does not encode a gyrase subunit, the other three genes potentially encode subunits of a plant gyrase. We also showed evidence for the existence of supercoiling activity in A. thaliana and that the plant is sensitive to quinolone and aminocoumarin antibiotics, compounds that target DNA gyrase in bacteria. However, it was not possible at that time to show whether the A. thaliana genes encoded an active gyrase enzyme, nor whether that enzyme is indeed the target for the quinolone and aminocoumarin antibiotics. Here we show that an A. thaliana mutant resistant to the quinolone drug ciprofloxacin has a point mutation in ATGYRA. Moreover we show that, as in bacteria, the quinolone-sensitive (wild-type) allele is dominant to the resistant gene. Further we have heterologously expressed ATGYRA and ATGYRB2 in a baculovirus expression system and shown supercoiling activity of the partially purified enzyme. Expression/purification of the quinolone-resistant A. thaliana gyrase yields active enzyme that is resistant to ciprofloxacin. Taken together these experiments now show unequivocally that A. thaliana encodes an organelle-targeted DNA gyrase that is the target of the quinolone drug ciprofloxacin; this has important consequences for plant physiology and the development of herbicides.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Proteínas de Arabidopsis/antagonistas & inibidores
Arabidopsis/enzimologia
Cloroplastos/efeitos dos fármacos
Ciprofloxacino/farmacologia
DNA Girase/metabolismo
Inibidores da Topoisomerase II/farmacologia
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Arabidopsis/efeitos dos fármacos
Arabidopsis/genética
Arabidopsis/ultraestrutura
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Cloroplastos/enzimologia
Cloroplastos/ultraestrutura
DNA Girase/química
DNA Girase/genética
DNA Girase/isolamento & purificação
Resistência a Medicamentos
Técnicas de Inativação de Genes
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/enzimologia
Mitocôndrias/ultraestrutura
Forma das Organelas/efeitos dos fármacos
Folhas de Planta/efeitos dos fármacos
Folhas de Planta/enzimologia
Folhas de Planta/genética
Folhas de Planta/ultraestrutura
Plantas Geneticamente Modificadas/efeitos dos fármacos
Plantas Geneticamente Modificadas/enzimologia
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/ultraestrutura
Mutação Puntual
Conformação Proteica
Subunidades Proteicas/antagonistas & inibidores
Subunidades Proteicas/genética
Subunidades Proteicas/isolamento & purificação
Subunidades Proteicas/metabolismo
Interferência de RNA
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Células Sf9
Spodoptera
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Arabidopsis Proteins); 0 (Protein Subunits); 0 (Recombinant Proteins); 0 (Topoisomerase II Inhibitors); 5E8K9I0O4U (Ciprofloxacin); EC 5.99.1.3 (DNA Gyrase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.689554


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[PMID]:26546679
[Au] Autor:Hanna MG; Mela I; Wang L; Henderson RM; Chapman ER; Edwardson JM; Audhya A
[Ad] Endereço:From the Department of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, Wisconsin 53706.
[Ti] Título:Sar1 GTPase Activity Is Regulated by Membrane Curvature.
[So] Source:J Biol Chem;291(3):1014-27, 2016 Jan 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The majority of biosynthetic secretory proteins initiate their journey through the endomembrane system from specific subdomains of the endoplasmic reticulum. At these locations, coated transport carriers are generated, with the Sar1 GTPase playing a critical role in membrane bending, recruitment of coat components, and nascent vesicle formation. How these events are appropriately coordinated remains poorly understood. Here, we demonstrate that Sar1 acts as the curvature-sensing component of the COPII coat complex and highlight the ability of Sar1 to bind more avidly to membranes of high curvature. Additionally, using an atomic force microscopy-based approach, we further show that the intrinsic GTPase activity of Sar1 is necessary for remodeling lipid bilayers. Consistent with this idea, Sar1-mediated membrane remodeling is dramatically accelerated in the presence of its guanine nucleotide-activating protein (GAP), Sec23-Sec24, and blocked upon addition of guanosine-5'-[(ß,γ)-imido]triphosphate, a poorly hydrolysable analog of GTP. Our results also indicate that Sar1 GTPase activity is stimulated by membranes that exhibit elevated curvature, potentially enabling Sar1 membrane scission activity to be spatially restricted to highly bent membranes that are characteristic of a bud neck. Taken together, our data support a stepwise model in which the amino-terminal amphipathic helix of GTP-bound Sar1 stably penetrates the endoplasmic reticulum membrane, promoting local membrane deformation. As membrane bending increases, Sar1 membrane binding is elevated, ultimately culminating in GTP hydrolysis, which may destabilize the bilayer sufficiently to facilitate membrane fission.
[Mh] Termos MeSH primário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/fisiologia
Retículo Endoplasmático/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Guanosina Trifosfato/metabolismo
Modelos Biológicos
Proteínas Monoméricas de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Animais
Vesículas Revestidas pelo Complexo de Proteína do Envoltório/efeitos dos fármacos
Vesículas Revestidas pelo Complexo de Proteína do Envoltório/ultraestrutura
Caenorhabditis elegans/efeitos dos fármacos
Caenorhabditis elegans/enzimologia
Caenorhabditis elegans/ultraestrutura
Proteínas de Caenorhabditis elegans/antagonistas & inibidores
Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/genética
Retículo Endoplasmático/ultraestrutura
Inibidores Enzimáticos/farmacologia
GTP Fosfo-Hidrolases/antagonistas & inibidores
GTP Fosfo-Hidrolases/química
GTP Fosfo-Hidrolases/genética
Proteínas Ativadoras de GTPase/antagonistas & inibidores
Proteínas Ativadoras de GTPase/genética
Proteínas Ativadoras de GTPase/metabolismo
Guanilil Imidodifosfato/farmacologia
Seres Humanos
Bicamadas Lipídicas/química
Bicamadas Lipídicas/metabolismo
Microdomínios da Membrana/efeitos dos fármacos
Microdomínios da Membrana/metabolismo
Microdomínios da Membrana/ultraestrutura
Microscopia de Força Atômica
Proteínas Monoméricas de Ligação ao GTP/antagonistas & inibidores
Proteínas Monoméricas de Ligação ao GTP/química
Proteínas Monoméricas de Ligação ao GTP/genética
Mutação
Forma das Organelas/efeitos dos fármacos
Interferência de RNA
Receptores Proteína Tirosina Quinases/genética
Receptores Proteína Tirosina Quinases/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteínas de Transporte Vesicular/antagonistas & inibidores
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
Proteínas Ativadoras de ras GTPase/genética
Proteínas Ativadoras de ras GTPase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Enzyme Inhibitors); 0 (GAP-1 protein, C elegans); 0 (GTPase-Activating Proteins); 0 (Lipid Bilayers); 0 (Recombinant Proteins); 0 (SEC-24 protein, C elegans); 0 (Vesicular Transport Proteins); 0 (ras GTPase-Activating Proteins); 0 (sec-23 protein, C elegans); 34273-04-6 (Guanylyl Imidodiphosphate); 86-01-1 (Guanosine Triphosphate); EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (SAR1B protein, human); EC 3.6.1.- (Sar1 protein, C elegans); EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151108
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.672287


  5 / 130 MEDLINE  
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[PMID]:26325352
[Au] Autor:Kawano-Kawada M; Pongcharoen P; Kawahara R; Yasuda M; Yamasaki T; Akiyama K; Sekito T; Kakinuma Y
[Ad] Endereço:a Laboratory of Molecular Physiology and Genetics, Faculty of Agriculture , Ehime University , Matsuyama , Japan.
[Ti] Título:Vba4p, a vacuolar membrane protein, is involved in the drug resistance and vacuolar morphology of Saccharomyces cerevisiae.
[So] Source:Biosci Biotechnol Biochem;80(2):279-87, 2016.
[Is] ISSN:1347-6947
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In the vacuolar basic amino acid (VBA) transporter family of Saccharomyces cerevisiae, VBA4 encodes a vacuolar membrane protein with 14 putative transmembrane helices. Transport experiments with isolated vacuolar membrane vesicles and estimation of the amino acid contents in vacuoles showed that Vba4p is not likely involved in the transport of amino acids. We found that the vba4Δ cells, as well as vba1Δ and vba2Δ cells, showed increased susceptibility to several drugs, particularly to azoles. Although disruption of the VBA4 gene did not affect the salt tolerance of the cells, vacuolar fragmentation observed under high salt conditions was less prominent in vba4Δ cells than in wild type, vba1Δ, and vba2Δ cells. Vba4p differs from Vba1p and Vba2p as a vacuolar transporter but is important for the drug resistance and vacuolar morphology of S. cerevisiae.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Básicos/metabolismo
Antifúngicos/farmacologia
Farmacorresistência Fúngica/genética
Membranas Intracelulares/metabolismo
Saccharomyces cerevisiae/metabolismo
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Sistemas de Transporte de Aminoácidos Básicos/genética
Aminoácidos/metabolismo
Transporte Biológico
Fluconazol/farmacologia
Expressão Gênica
Membranas Intracelulares/efeitos dos fármacos
Membranas Intracelulares/ultraestrutura
Cetoconazol/farmacologia
Miconazol/farmacologia
Forma das Organelas
Isoformas de Proteínas/genética
Isoformas de Proteínas/metabolismo
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Saccharomyces cerevisiae/efeitos dos fármacos
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/ultraestrutura
Tolerância a Sal
Cloreto de Sódio/farmacologia
Vacúolos/efeitos dos fármacos
Vacúolos/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acid Transport Systems, Basic); 0 (Amino Acids); 0 (Antifungal Agents); 0 (Protein Isoforms); 451W47IQ8X (Sodium Chloride); 7NNO0D7S5M (Miconazole); 8VZV102JFY (Fluconazole); R9400W927I (Ketoconazole)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150902
[St] Status:MEDLINE
[do] DOI:10.1080/09168451.2015.1083401


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[PMID]:26053100
[Au] Autor:Leduc-Gaudet JP; Picard M; St-Jean Pelletier F; Sgarioto N; Auger MJ; Vallée J; Robitaille R; St-Pierre DH; Gouspillou G
[Ad] Endereço:Département des Sciences de l'Activité Physique, Faculté des Sciences, UQAM, Montréal, Canada.
[Ti] Título:Mitochondrial morphology is altered in atrophied skeletal muscle of aged mice.
[So] Source:Oncotarget;6(20):17923-37, 2015 Jul 20.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Skeletal muscle aging is associated with a progressive decline in muscle mass and strength, a process termed sarcopenia. Evidence suggests that accumulation of mitochondrial dysfunction plays a causal role in sarcopenia, which could be triggered by impaired mitophagy. Mitochondrial function, mitophagy and mitochondrial morphology are interconnected aspects of mitochondrial biology, and may coordinately be altered with aging. However, mitochondrial morphology has remained challenging to characterize in muscle, and whether sarcopenia is associated with abnormal mitochondrial morphology remains unknown. Therefore, we assessed the morphology of SubSarcolemmal (SS) and InterMyoFibrillar (IMF) mitochondria in skeletal muscle of young (8-12wk-old) and old (88-96wk-old) mice using a quantitative 2-dimensional transmission electron microscopy approach. We show that sarcopenia is associated with larger and less circular SS mitochondria. Likewise, aged IMF mitochondria were longer and more branched, suggesting increased fusion and/or decreased fission. Accordingly, although no difference in the content of proteins regulating mitochondrial dynamics (Mfn1, Mfn2, Opa1 and Drp1) was observed, a mitochondrial fusion index (Mfn2-to-Drp1 ratio) was significantly increased in aged muscles. Our results reveal that sarcopenia is associated with complex changes in mitochondrial morphology that could interfere with mitochondrial function and mitophagy, and thus contribute to aging-related accumulation of mitochondrial dysfunction and sarcopenia.
[Mh] Termos MeSH primário: Envelhecimento/patologia
Mitocôndrias Musculares/ultraestrutura
Músculo Esquelético/ultraestrutura
Sarcopenia/patologia
[Mh] Termos MeSH secundário: Fatores Etários
Envelhecimento/metabolismo
Animais
Modelos Animais de Doenças
Dinaminas/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Masculino
Camundongos
Microscopia Eletrônica de Transmissão
Mitocôndrias Musculares/metabolismo
Dinâmica Mitocondrial
Tamanho Mitocondrial
Músculo Esquelético/metabolismo
Forma das Organelas
Sarcopenia/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (Mfn1 protein, mouse); EC 3.6.1.- (Mfn2 protein, mouse); EC 3.6.1.- (Opa1 protein (GTPase), mouse); EC 3.6.5.5 (Dnm1l protein, mouse); EC 3.6.5.5 (Dynamins)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:151112
[Lr] Data última revisão:
151112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150609
[St] Status:MEDLINE


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[PMID]:26010263
[Au] Autor:Held NM; Houtkooper RH
[Ad] Endereço:Laboratory Genetic Metabolic Diseases, Academic Medical Center, Amsterdam, the Netherlands.
[Ti] Título:Mitochondrial quality control pathways as determinants of metabolic health.
[So] Source:Bioessays;37(8):867-76, 2015 Aug.
[Is] ISSN:1521-1878
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial function is key for maintaining cellular health, while mitochondrial failure is associated with various pathologies, including inherited metabolic disorders and age-related diseases. In order to maintain mitochondrial quality, several pathways of mitochondrial quality control have evolved. These systems monitor mitochondrial integrity through antioxidants, DNA repair systems, and chaperones and proteases involved in the mitochondrial unfolded protein response. Additional regulation of mitochondrial function involves dynamic exchange of components through mitochondrial fusion and fission. Sustained stress induces a selective autophagy - termed mitophagy - and ultimately leads to apoptosis. Together, these systems form a network that acts on the molecular, organellar, and cellular level. In this review, we highlight how these systems are regulated in an integrated context- and time-dependent network of mitochondrial quality control that is implicated in healthy aging.
[Mh] Termos MeSH primário: Mitocôndrias/fisiologia
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
Seres Humanos
Degradação Mitocondrial
Dinâmica Mitocondrial
Proteínas Mitocondriais/metabolismo
Forma das Organelas
Proteólise
Resposta a Proteínas não Dobradas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150527
[St] Status:MEDLINE
[do] DOI:10.1002/bies.201500013


  8 / 130 MEDLINE  
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[PMID]:25743185
[Au] Autor:Zhu M; Li X; Tian X; Wu C
[Ad] Endereço:Neuroscience Center of Excellence, Department of Cell Biology and Anatomy, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA.
[Ti] Título:Mask loss-of-function rescues mitochondrial impairment and muscle degeneration of Drosophila pink1 and parkin mutants.
[So] Source:Hum Mol Genet;24(11):3272-85, 2015 Jun 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PTEN-induced kinase 1 (Pink1) and ubiquitin E3 ligase Parkin function in a linear pathway to maintain healthy mitochondria via regulating mitochondrial clearance and trafficking. Mutations in the two enzymes cause the familial form of Parkinson's disease (PD) in humans, as well as accumulation of defective mitochondria and cellular degeneration in flies. Here, we show that loss of function of a scaffolding protein Mask, also known as ANKHD1 (Ankyrin repeats and KH domain containing protein 1) in humans, rescues the behavioral, anatomical and cellular defects caused by pink1 or parkin mutations in a cell-autonomous manner. Moreover, similar rescue can also be achieved if Mask knock-down is induced in parkin adult flies when the mitochondrial dystrophy is already manifested. We found that Mask genetically interacts with Parkin to modulate mitochondrial morphology and negatively regulates the recruitment of Parkin to mitochondria. We also provide evidence that loss of Mask activity promotes co-localization of the autophagosome marker with mitochondria in developing larval muscle, and that an intact autophagy pathway is required for the rescue of parkin mutant defects by mask loss of function. Together, our data strongly suggest that Mask/ANKHD1 activity can be inhibited in a tissue- and timely-controlled fashion to restore mitochondrial integrity under PD-linked pathological conditions.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/genética
Proteínas de Drosophila/genética
Doença de Parkinson/genética
Proteínas Serina-Treonina Quinases/genética
Ubiquitina-Proteína Ligases/genética
[Mh] Termos MeSH secundário: Animais
Neurônios Dopaminérgicos/metabolismo
Neurônios Dopaminérgicos/patologia
Drosophila melanogaster
Feminino
Estudos de Associação Genética
Seres Humanos
Masculino
Mitocôndrias/enzimologia
Forma das Organelas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Drosophila Proteins); 0 (Mask protein, Drosophila); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (PINK1 protein, Drosophila); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 6.3.2.- (parkin protein, Drosophila)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150307
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddv081


  9 / 130 MEDLINE  
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[PMID]:25665438
[Au] Autor:Kilpatrick BS; Eden ER; Hockey LN; Futter CE; Patel S
[Ad] Endereço:Department of Cell and Developmental Biology, University College London, London, UK.
[Ti] Título:Methods for monitoring lysosomal morphology.
[So] Source:Methods Cell Biol;126:1-19, 2015.
[Is] ISSN:0091-679X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysosomes are abundant organelles best known for their crucial role in macromolecule turnover. Lysosome dysfunction features in several diseases exemplified by the lysosomal storage disorders and is often associated with marked changes in lysosome structure. Lysosomal morphology may therefore serve as a sensitive readout of endocytic well-being. Here we describe methods for monitoring lysosome morphology in fixed and live cells using fluorescent probes and electron microscopy.
[Mh] Termos MeSH primário: Lisossomos/ultraestrutura
[Mh] Termos MeSH secundário: Células Cultivadas
Microscopia Crioeletrônica
Técnica Indireta de Fluorescência para Anticorpo
Corantes Fluorescentes/química
Seres Humanos
Microscopia Eletrônica
Microscopia Eletrônica de Transmissão
Microscopia de Fluorescência
Forma das Organelas
Análise de Célula Única
Coloração e Rotulagem
Fixação de Tecidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluorescent Dyes)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150211
[St] Status:MEDLINE


  10 / 130 MEDLINE  
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[PMID]:25619254
[Au] Autor:Spang A
[Ad] Endereço:*Growth & Development, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
[Ti] Título:A small GTPase involved in mitochondrial morphology and function.
[So] Source:Biochem Soc Trans;43(1):108-10, 2015 Feb.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mitochondria are the powerhouse of cells as they produce the bulk of ATP which is consumed by the cell. They form a highly interconnected network that is governed by fission and fusion processes. In addition, mitochondria and the endoplasmic reticulum (ER) are found in close proximity to each other and it is thought that they maintain contact sites to exchange molecules. The regulation and the function of these contact sites need to be further explored. The small GTPase Arf1 (ADP-ribosylation factor 1), which is best known for its essential role in the generation of coatomer protein I (COPI)-coated vesicles at the Golgi complex appears to be also essential for the dynamics and maintenance of mitochondrial function, presumably at ER-mitochondrial contact sites.
[Mh] Termos MeSH primário: Fator 1 de Ribosilação do ADP/fisiologia
Mitocôndrias/enzimologia
[Mh] Termos MeSH secundário: Animais
Retículo Endoplasmático/metabolismo
Seres Humanos
Mitocôndrias/ultraestrutura
Forma das Organelas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 3.6.5.2 (ADP-Ribosylation Factor 1)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:150126
[Lr] Data última revisão:
150126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150127
[St] Status:MEDLINE
[do] DOI:10.1042/BST20140284



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