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[PMID]:29346429
[Au] Autor:Ferrigno A; Di Pasqua LG; Berardo C; Siciliano V; Rizzo V; Adorini L; Richelmi P; Vairetti M
[Ad] Endereço:Department of Internal Medicine and Therapeutics, University of Pavia, Pavia, Italy.
[Ti] Título:The farnesoid X receptor agonist obeticholic acid upregulates biliary excretion of asymmetric dimethylarginine via MATE-1 during hepatic ischemia/reperfusion injury.
[So] Source:PLoS One;13(1):e0191430, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: We previously showed that increased asymmetric dimethylarginine (ADMA) biliary excretion occurs during hepatic ischemia/reperfusion (I/R), prompting us to study the effects of the farnesoid X receptor (FXR) agonist obeticholic acid (OCA) on bile, serum and tissue levels of ADMA after I/R. MATERIAL AND METHODS: Male Wistar rats were orally administered 10mg/kg/day of OCA or vehicle for 5 days and were subjected to 60 min partial hepatic ischemia or sham-operated. After a 60 min reperfusion, serum, tissue and bile ADMA levels, liver mRNA and protein expression of ADMA transporters (CAT-1, CAT-2A, CAT-2B, OCT-1, MATE-1), and enzymes involved in ADMA synthesis (protein-arginine-N-methyltransferase-1, PRMT-1) and metabolism (dimethylarginine-dimethylaminohydrolase-1, DDAH-1) were measured. RESULTS: OCA administration induced a further increase in biliary ADMA levels both in sham and I/R groups, with no significant changes in hepatic ADMA content. A reduction in CAT-1, CAT-2A or CAT-2B transcripts was found in OCA-treated sham-operated rats compared with vehicle. Conversely, OCA administration did not change CAT-1, CAT-2A or CAT-2B expression, already reduced by I/R. However, a marked decrease in OCT-1 and increase in MATE-1 expression was observed. A similar trend occurred with protein expression. CONCLUSION: The reduced mRNA expression of hepatic CAT transporters suggests that the increase in serum ADMA levels is probably due to decreased liver uptake of ADMA from the systemic circulation. Conversely, the mechanism involved in further increasing biliary ADMA levels in sham and I/R groups treated with OCA appears to be MATE-1-dependent.
[Mh] Termos MeSH primário: Antiporters/metabolismo
Arginina/análogos & derivados
Sistema Biliar/efeitos dos fármacos
Ácido Quenodesoxicólico/análogos & derivados
Hepatopatias/metabolismo
Proteínas de Transporte de Cátions Orgânicos/metabolismo
Receptores Citoplasmáticos e Nucleares/antagonistas & inibidores
Traumatismo por Reperfusão/metabolismo
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Arginina/sangue
Arginina/metabolismo
Arginina/secreção
Sistema Biliar/metabolismo
Sistema Biliar/secreção
Western Blotting
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Ácido Quenodesoxicólico/farmacologia
Masculino
Óxido Nítrico Sintase/metabolismo
Proteína-Arginina N-Metiltransferases/genética
RNA Mensageiro/genética
Ratos
Ratos Wistar
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiporters); 0 (Carrier Proteins); 0 (MATE1 protein, rat); 0 (Organic Cation Transport Proteins); 0 (RNA, Messenger); 0 (Receptors, Cytoplasmic and Nuclear); 0 (farnesoid X-activated receptor); 0462Z4S4OZ (obeticholic acid); 0GEI24LG0J (Chenodeoxycholic Acid); 63CV1GEK3Y (N,N-dimethylarginine); 94ZLA3W45F (Arginine); EC 1.14.13.39 (Nitric Oxide Synthase); EC 2.1.1.319 (PRMT1 protein, rat); EC 2.1.1.319 (Protein-Arginine N-Methyltransferases)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180119
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191430


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[PMID]:28463667
[Au] Autor:Choudhury MA; Sidjabat HE; Rathnayake IU; Gavin N; Chan RJ; Marsh N; Banu S; Huygens F; Paterson DL; Rickard CM; McMillan DJ
[Ad] Endereço:2​Alliance for Vascular Access Teaching and Research, Griffith University, Brisbane, Australia.
[Ti] Título:Culture-independent detection of chlorhexidine resistance genes qacA/B and smr in bacterial DNA recovered from body sites treated with chlorhexidine-containing dressings.
[So] Source:J Med Microbiol;66(4):447-453, 2017 Apr.
[Is] ISSN:1473-5644
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Dressings containing chlorhexidine gluconate (CHG) are increasingly used in clinical environments for prevention of infection at central venous catheter insertion sites. Increased tolerance to this biocide in staphylococci is primarily associated with the presence of qacA/B and smr genes. METHODOLOGY: We used a culture-independent method to assess the prevalence of these genes in 78 DNA specimens recovered from the skin of 43 patients at catheter insertion sites in the arm that were covered with CHG dressings. RESULTS: Of the 78 DNA specimens analysed, 52 (67 %) possessed qacA/B and 14 (18 %) possessed smr; all samples positive for smr were also positive for qacA/B. These prevalence rates were not statistically greater than those observed in a subsample of specimens taken from non-CHG treated contralateral arms and non-CHG-dressing exposed arms. A statistically greater proportion of specimens with greater than 72 h exposure to CHG dressings were qac-positive (P=0.04), suggesting that the patients were contaminated with bacteria or DNA containing qacA/B during their hospital stay. The presence of qac genes was not positively associated with the presence of DNA specific for Staphylococcusepidermidis and Staphylococcusaureus in these specimens. CONCLUSION: Our results show that CHG genes are highly prevalent on hospital patients' skin, even in the absence of viable bacteria.
[Mh] Termos MeSH primário: Antiporters/genética
Proteínas de Bactérias/genética
Clorexidina/análogos & derivados
Desinfetantes/farmacologia
Proteínas de Membrana Transportadoras/genética
Staphylococcus aureus/genética
Staphylococcus epidermidis/genética
[Mh] Termos MeSH secundário: Bandagens/microbiologia
Cateterismo Venoso Central
Clorexidina/farmacologia
DNA Bacteriano/genética
Farmacorresistência Bacteriana/genética
Feminino
Seres Humanos
Masculino
Testes de Sensibilidade Microbiana
Meia-Idade
Pele/microbiologia
Infecções Estafilocócicas/prevenção & controle
Staphylococcus aureus/efeitos dos fármacos
Staphylococcus aureus/isolamento & purificação
Staphylococcus epidermidis/efeitos dos fármacos
Staphylococcus epidermidis/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiporters); 0 (Bacterial Proteins); 0 (DNA, Bacterial); 0 (Disinfectants); 0 (Membrane Transport Proteins); 0 (QacB protein, Staphylococcus aureus); 0 (small multidrug-resistance pump, Staphylococcus aureus); 134773-66-3 (qacA protein, Staphylococcus aureus); MOR84MUD8E (chlorhexidine gluconate); R4KO0DY52L (Chlorhexidine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1099/jmm.0.000463


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[PMID]:28747715
[Au] Autor:Tomita A; Zhang M; Jin F; Zhuang W; Takeda H; Maruyama T; Osawa M; Hashimoto KI; Kawasaki H; Ito K; Dohmae N; Ishitani R; Shimada I; Yan Z; Hattori M; Nureki O
[Ad] Endereço:Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo, 113-0032, Japan.
[Ti] Título:ATP-dependent modulation of MgtE in Mg homeostasis.
[So] Source:Nat Commun;8(1):148, 2017 07 27.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Magnesium is an essential ion for numerous physiological processes. MgtE is a Mg selective channel involved in the maintenance of intracellular Mg homeostasis, whose gating is regulated by intracellular Mg levels. Here, we report that ATP binds to MgtE, regulating its Mg -dependent gating. Crystal structures of MgtE-ATP complex show that ATP binds to the intracellular CBS domain of MgtE. Functional studies support that ATP binding to MgtE enhances the intracellular domain affinity for Mg within physiological concentrations of this divalent cation, enabling MgtE to function as an in vivo Mg sensor. ATP dissociation from MgtE upregulates Mg influx at both high and low intracellular Mg concentrations. Using site-directed mutagenesis and structure based-electrophysiological and biochemical analyses, we identify key residues and main structural changes involved in the process. This work provides the molecular basis of ATP-dependent modulation of MgtE in Mg homeostasis.MgtE is an Mg transporter involved in Mg homeostasis. Here, the authors report that ATP regulates the Mg -dependent gating of MgtE and use X-ray crystallography combined with functional studies to propose the molecular mechanisms involved in this process.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Antiporters/metabolismo
Proteínas de Bactérias/metabolismo
Homeostase
Magnésio/metabolismo
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/química
Sequência de Aminoácidos
Antiporters/química
Antiporters/genética
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Cristalografia por Raios X
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Homologia de Sequência de Aminoácidos
Thermus thermophilus/genética
Thermus thermophilus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiporters); 0 (Bacterial Proteins); 0 (MgtE protein, bacteria); 8L70Q75FXE (Adenosine Triphosphate); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-00082-w


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[PMID]:29100094
[Au] Autor:Writzl K; Maver A; Kovacic L; Martinez-Valero P; Contreras L; Satrustegui J; Castori M; Faivre L; Lapunzina P; van Kuilenburg ABP; Radovic S; Thauvin-Robinet C; Peterlin B; Del Arco A; Hennekam RC
[Ad] Endereço:Clinical Institute of Medical Genetics, University Medical Centre, 1000 Ljubljana, Slovenia. Electronic address: karinwritzl@gmail.com.
[Ti] Título:De Novo Mutations in SLC25A24 Cause a Disorder Characterized by Early Aging, Bone Dysplasia, Characteristic Face, and Early Demise.
[So] Source:Am J Hum Genet;101(5):844-855, 2017 Nov 02.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A series of simplex cases have been reported under various diagnoses sharing early aging, especially evident in congenitally decreased subcutaneous fat tissue and sparse hair, bone dysplasia of the skull and fingers, a distinctive facial gestalt, and prenatal and postnatal growth retardation. For historical reasons, we suggest naming the entity Fontaine syndrome. Exome sequencing of four unrelated affected individuals showed that all carried the de novo missense variant c.649C>T (p.Arg217Cys) or c.650G>A (p.Arg217His) in SLC25A24, a solute carrier 25 family member coding for calcium-binding mitochondrial carrier protein (SCaMC-1, also known as SLC25A24). SLC25A24 allows an electro-neutral and reversible exchange of ATP-Mg and phosphate between the cytosol and mitochondria, which is required for maintaining optimal adenine nucleotide levels in the mitochondrial matrix. Molecular dynamic simulation studies predict that p.Arg217Cys and p.Arg217His narrow the substrate cavity of the protein and disrupt transporter dynamics. SLC25A24-mutant fibroblasts and cells expressing p.Arg217Cys or p.Arg217His variants showed altered mitochondrial morphology, a decreased proliferation rate, increased mitochondrial membrane potential, and decreased ATP-linked mitochondrial oxygen consumption. The results suggest that the SLC25A24 mutations lead to impaired mitochondrial ATP synthesis and cause hyperpolarization and increased proton leak in association with an impaired energy metabolism. Our findings identify SLC25A24 mutations affecting codon 217 as the underlying genetic cause of human progeroid Fontaine syndrome.
[Mh] Termos MeSH primário: Envelhecimento/genética
Antiporters/genética
Doenças do Desenvolvimento Ósseo/genética
Proteínas de Ligação ao Cálcio/genética
Proteínas Mitocondriais/genética
Mutação/genética
[Mh] Termos MeSH secundário: Adenina/metabolismo
Trifosfato de Adenosina/metabolismo
Citosol/metabolismo
Feminino
Morte Fetal
Fibroblastos/metabolismo
Seres Humanos
Lactente
Recém-Nascido
Masculino
Potencial da Membrana Mitocondrial/genética
Mitocôndrias/genética
Mitocôndrias/metabolismo
Proteínas Mitocondriais/metabolismo
Simulação de Dinâmica Molecular
Oxigênio/metabolismo
Fosfatos/metabolismo
Síndrome
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiporters); 0 (Calcium-Binding Proteins); 0 (Mitochondrial Proteins); 0 (Phosphates); 0 (SLC25A24 protein, human); 8L70Q75FXE (Adenosine Triphosphate); JAC85A2161 (Adenine); S88TT14065 (Oxygen)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171104
[St] Status:MEDLINE


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[PMID]:29100093
[Au] Autor:Ehmke N; Graul-Neumann L; Smorag L; Koenig R; Segebrecht L; Magoulas P; Scaglia F; Kilic E; Hennig AF; Adolphs N; Saha N; Fauler B; Kalscheuer VM; Hennig F; Altmüller J; Netzer C; Thiele H; Nürnberg P; Yigit G; Jäger M; Hecht J; Krüger U; Mielke T; Krawitz PM; Horn D; Schuelke M; Mundlos S; Bacino CA; Bonnen PE; Wollnik B; Fischer-Zirnsak B; Kornak U
[Ad] Endereço:Institute of Medical and Human Genetics, Charité - Universitätsmedizin Berlin, 13353 Berlin, Germany; Berlin Institute of Health, 10117 Berlin, Germany; Max Planck Institute for Molecular Genetics, Development and Disease Group, 14195 Berlin, Germany. Electronic address: nadja.ehmke@charite.de.
[Ti] Título:De Novo Mutations in SLC25A24 Cause a Craniosynostosis Syndrome with Hypertrichosis, Progeroid Appearance, and Mitochondrial Dysfunction.
[So] Source:Am J Hum Genet;101(5):833-843, 2017 Nov 02.
[Is] ISSN:1537-6605
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Gorlin-Chaudhry-Moss syndrome (GCMS) is a dysmorphic syndrome characterized by coronal craniosynostosis and severe midface hypoplasia, body and facial hypertrichosis, microphthalmia, short stature, and short distal phalanges. Variable lipoatrophy and cutis laxa are the basis for a progeroid appearance. Using exome and genome sequencing, we identified the recurrent de novo mutations c.650G>A (p.Arg217His) and c.649C>T (p.Arg217Cys) in SLC25A24 in five unrelated girls diagnosed with GCMS. Two of the girls had pronounced neonatal progeroid features and were initially diagnosed with Wiedemann-Rautenstrauch syndrome. SLC25A24 encodes a mitochondrial inner membrane ATP-Mg/P carrier. In fibroblasts from affected individuals, the mutated SLC25A24 showed normal stability. In contrast to control cells, the probands' cells showed mitochondrial swelling, which was exacerbated upon treatment with hydrogen peroxide (H O ). The same effect was observed after overexpression of the mutant cDNA. Under normal culture conditions, the mitochondrial membrane potential of the probands' fibroblasts was intact, whereas ATP content in the mitochondrial matrix was lower than that in control cells. However, upon H O exposure, the membrane potential was significantly elevated in cells harboring the mutated SLC25A24. No reduction of mitochondrial DNA copy number was observed. These findings demonstrate that mitochondrial dysfunction with increased sensitivity to oxidative stress is due to the SLC25A24 mutations. Our results suggest that the SLC25A24 mutations induce a gain of pathological function and link mitochondrial ATP-Mg/P transport to the development of skeletal and connective tissue.
[Mh] Termos MeSH primário: Anormalidades Múltiplas/genética
Antiporters/genética
Proteínas de Ligação ao Cálcio/genética
Anormalidades Craniofaciais/genética
Craniossinostoses/genética
Permeabilidade do Canal Arterial/genética
Hipertricose/genética
Mitocôndrias/genética
Proteínas Mitocondriais/genética
Mutação/genética
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/genética
Adolescente
Criança
Pré-Escolar
Cútis Laxa/genética
DNA Mitocondrial/genética
Exoma/genética
Feminino
Retardo do Crescimento Fetal/genética
Fibroblastos/patologia
Seres Humanos
Peróxido de Hidrogênio/farmacologia
Lactente
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Potencial da Membrana Mitocondrial/genética
Mitocôndrias/efeitos dos fármacos
Estresse Oxidativo/genética
Progéria/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP-Mg-Pi carrier proteins, mitochondria); 0 (Antiporters); 0 (Calcium-Binding Proteins); 0 (DNA, Mitochondrial); 0 (Mitochondrial Proteins); 0 (SLC25A24 protein, human); 8L70Q75FXE (Adenosine Triphosphate); BBX060AN9V (Hydrogen Peroxide)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171104
[St] Status:MEDLINE


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[PMID]:29025768
[Au] Autor:Sirish P; Ledford HA; Timofeyev V; Thai PN; Ren L; Kim HJ; Park S; Lee JH; Dai G; Moshref M; Sihn CR; Chen WC; Timofeyeva MV; Jian Z; Shimkunas R; Izu LT; Chiamvimonvat N; Chen-Izu Y; Yamoah EN; Zhang XD
[Ad] Endereço:From the Division of Cardiovascular Medicine, Department of Internal Medicine (P.S., H.A.L., V.T., P.N.T., L.R., S.P., G.D., M.M., C.-R.S., W.C.C., M.V.T., N.C., Y.C.-I., X.-D.Z.), Center for Neuroscience (H.J.K.), Department of Pharmacology (Z.J., R.S., L.T.I., N.C., Y.C.-I.) and Department of Biom
[Ti] Título:Action Potential Shortening and Impairment of Cardiac Function by Ablation of .
[So] Source:Circ Arrhythm Electrophysiol;10(10), 2017 Oct.
[Is] ISSN:1941-3084
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Intracellular pH (pH ) is critical to cardiac excitation and contraction; uncompensated changes in pH impair cardiac function and trigger arrhythmia. Several ion transporters participate in cardiac pH regulation. Our previous studies identified several isoforms of a solute carrier Slc26a6 to be highly expressed in cardiomyocytes. We show that Slc26a6 mediates electrogenic Cl /HCO exchange activities in cardiomyocytes, suggesting the potential role of Slc26a6 in regulation of not only pH , but also cardiac excitability. METHODS AND RESULTS: To test the mechanistic role of Slc26a6 in the heart, we took advantage of knockout ( ) mice using both in vivo and in vitro analyses. Consistent with our prediction of its electrogenic activities, ablation of results in action potential shortening. There are reduced Ca transient and sarcoplasmic reticulum Ca load, together with decreased sarcomere shortening in cardiomyocytes. These abnormalities translate into reduced fractional shortening and cardiac contractility at the in vivo level. Additionally, pH is elevated in cardiomyocytes with slower recovery kinetics from intracellular alkalization, consistent with the Cl /HCO exchange activities of Slc26a6. Moreover, mice show evidence of sinus bradycardia and fragmented QRS complex, supporting the critical role of Slc26a6 in cardiac conduction system. CONCLUSIONS: Our study provides mechanistic insights into Slc26a6, a unique cardiac electrogenic Cl /HCO transporter in ventricular myocytes, linking the critical roles of Slc26a6 in regulation of pH , excitability, and contractility. pH is a critical regulator of other membrane and contractile proteins. Future studies are needed to investigate possible changes in these proteins in mice.
[Mh] Termos MeSH primário: Potenciais de Ação
Antiporters/deficiência
Acoplamento Excitação-Contração
Frequência Cardíaca
Contração Miocárdica
Miócitos Cardíacos/metabolismo
[Mh] Termos MeSH secundário: Animais
Antiporters/genética
Bradicardia/genética
Bradicardia/metabolismo
Bradicardia/fisiopatologia
Células CHO
Cricetulus
Genótipo
Concentração de Íons de Hidrogênio
Cinética
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Camundongos da Linhagem 129
Camundongos Knockout
Fenótipo
Sarcômeros/metabolismo
Retículo Sarcoplasmático/metabolismo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiporters); 0 (Membrane Transport Proteins); 0 (SLC26A6 protein, human); 0 (Slc26a6 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171101
[Lr] Data última revisão:
171101
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE


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[PMID]:28931644
[Au] Autor:Hamilton EMC; Bertini E; Kalaydjieva L; Morar B; Dojcáková D; Liu J; Vanderver A; Curiel J; Persoon CM; Diodato D; Pinelli L; van der Meij NL; Plecko B; Blaser S; Wolf NI; Waisfisz Q; Abbink TEM; van der Knaap MS; Recessive H-ABC Research Group
[Ad] Endereço:From the Department of Child Neurology (E.M.C.H., N.I.W., T.E.M.A., M.S.v.d.K.), Amsterdam Neuroscience (E.M.C.H., N.I.W., T.E.M.A., M.S.v.d.K.), Department of Clinical Genetics (C.M.P., Q.W.), Department of Functional Genomics, Center for Neurogenomics and Cognitive Research (M.S.v.d.K.), VU Univer
[Ti] Título: founder mutation in the Roma population causes recessive variant of H-ABC.
[So] Source:Neurology;89(17):1821-1828, 2017 Oct 24.
[Is] ISSN:1526-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To identify the gene defect in patients with hypomyelination with atrophy of the basal ganglia and cerebellum (H-ABC) who are negative for mutations. METHODS: We performed homozygosity mapping and whole exome sequencing (WES) to detect the disease-causing variant. We used a Taqman assay for population screening. We developed a luciferase reporter construct to investigate the effect of the promoter mutation on expression. RESULTS: Sixteen patients from 14 families from different countries fulfilling the MRI criteria for H-ABC exhibited a similar, severe clinical phenotype, including lack of development and a severe epileptic encephalopathy. The majority of patients had a known Roma ethnic background. Single nucleotide polymorphism array analysis in 5 patients identified one large overlapping homozygous region on chromosome 13. WES in 2 patients revealed a homozygous deletion in the promoter region of . Sanger sequencing confirmed homozygosity for this variant in all 16 patients. All patients shared a common haplotype, indicative of a founder effect. Screening of 1,000 controls from different European Roma panels demonstrated an overall carrier rate of the mutation of 3%-25%. Transfection assays showed that the deletion significantly reduced expression in specific CNS cell lines. CONCLUSIONS: encodes ubiquitin-fold modifier 1 (UFM1), a member of the ubiquitin-like family involved in posttranslational modification of proteins. Its exact biological role is unclear. This study associates a gene defect with a disease and sheds new light on possible UFM1 functional networks.
[Mh] Termos MeSH primário: Sistemas de Transporte de Aminoácidos Acídicos/deficiência
Antiporters/deficiência
Gânglios da Base/patologia
Cerebelo/patologia
Doenças Desmielinizantes Hereditárias do Sistema Nervoso Central/genética
Doenças Mitocondriais/genética
Polimorfismo de Nucleotídeo Único/genética
Proteínas/genética
Transtornos Psicomotores/genética
[Mh] Termos MeSH secundário: Adolescente
Adulto
Sistemas de Transporte de Aminoácidos Acídicos/genética
Antiporters/genética
Atrofia/etiologia
Gânglios da Base/diagnóstico por imagem
Linhagem Celular Tumoral/patologia
Cerebelo/diagnóstico por imagem
Criança
Pré-Escolar
Análise Mutacional de DNA
Saúde da Família
Feminino
Células HeLa
Doenças Desmielinizantes Hereditárias do Sistema Nervoso Central/complicações
Doenças Desmielinizantes Hereditárias do Sistema Nervoso Central/diagnóstico por imagem
Seres Humanos
Processamento de Imagem Assistida por Computador
Itália
Imagem por Ressonância Magnética
Masculino
Doenças Mitocondriais/complicações
Doenças Mitocondriais/diagnóstico por imagem
Transtornos Psicomotores/complicações
Transtornos Psicomotores/diagnóstico por imagem
Transfecção
Tubulina (Proteína)/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acid Transport Systems, Acidic); 0 (Antiporters); 0 (Proteins); 0 (TUBB4A protein, human); 0 (Tubulin); 0 (UFM1 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171105
[Lr] Data última revisão:
171105
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1212/WNL.0000000000004578


  8 / 3254 MEDLINE  
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[PMID]:28847924
[Au] Autor:Chakravarty S; Melton CN; Bailin A; Yahr TL; Anderson GG
[Ad] Endereço:Department of Biology, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana, USA.
[Ti] Título:Pseudomonas aeruginosa Magnesium Transporter MgtE Inhibits Type III Secretion System Gene Expression by Stimulating Transcription.
[So] Source:J Bacteriol;199(23), 2017 Dec 01.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:causes numerous acute and chronic opportunistic infections in humans. One of its most formidable weapons is a type III secretion system (T3SS), which injects powerful toxins directly into host cells. The toxins lead to cell dysfunction and, ultimately, cell death. Identification of regulatory pathways that control T3SS gene expression may lead to the discovery of novel therapeutics to treat infections. In a previous study, we found that expression of the magnesium transporter gene inhibits T3SS gene transcription. MgtE-dependent inhibition appeared to interfere with the synthesis or function of the master T3SS transcriptional activator ExsA, although the exact mechanism was unclear. We now demonstrate that expression acts through the GacAS two-component system to activate and transcription. This event ultimately leads to inhibition of translation. This inhibitory effect is specific to as translation of other genes in the operon is not inhibited by Moreover, our data reveal that MgtE acts solely through this pathway to regulate T3SS gene transcription. Our study reveals an important mechanism that may allow to fine-tune T3SS activity in response to certain environmental stimuli. The type III secretion system (T3SS) is a critical virulence factor utilized by numerous Gram-negative bacteria, including , to intoxicate and kill host cells. Elucidating T3SS regulatory mechanisms may uncover targets for novel anti- therapeutics and provide deeper understanding of bacterial pathogenesis. We previously found that the magnesium transporter MgtE inhibits T3SS gene transcription in In this study, we describe the mechanism of MgtE-dependent inhibition of the T3SS. Our report also illustrates how MgtE might respond to environmental cues, such as magnesium levels, to fine-tune T3SS gene expression.
[Mh] Termos MeSH primário: Antiporters/metabolismo
Proteínas de Bactérias/metabolismo
Sistemas de Secreção Bacterianos/metabolismo
Regulação Bacteriana da Expressão Gênica/fisiologia
Magnésio/metabolismo
Pseudomonas aeruginosa/metabolismo
Transcrição Genética/fisiologia
Sistemas de Secreção Tipo III/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Membrana Transportadoras/metabolismo
Óperon/fisiologia
Transdução de Sinais/fisiologia
Transativadores/metabolismo
Fatores de Virulência/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiporters); 0 (Bacterial Proteins); 0 (Bacterial Secretion Systems); 0 (Membrane Transport Proteins); 0 (MgtE protein, bacteria); 0 (Trans-Activators); 0 (Type III Secretion Systems); 0 (Virulence Factors); I38ZP9992A (Magnesium)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE


  9 / 3254 MEDLINE  
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[PMID]:28774891
[Au] Autor:Murley A; Yamada J; Niles BJ; Toulmay A; Prinz WA; Powers T; Nunnari J
[Ad] Endereço:Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.
[Ti] Título:Sterol transporters at membrane contact sites regulate TORC1 and TORC2 signaling.
[So] Source:J Cell Biol;216(9):2679-2689, 2017 Sep 04.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane contact sites (MCSs) function to facilitate the formation of membrane domains composed of specialized lipids, proteins, and nucleic acids. In cells, membrane domains regulate membrane dynamics and biochemical and signaling pathways. We and others identified a highly conserved family of sterol transport proteins (Ltc/Lam) localized at diverse MCSs. In this study, we describe data indicating that the yeast family members Ltc1 and Ltc3/4 function at the vacuole and plasma membrane, respectively, to create membrane domains that partition upstream regulators of the TORC1 and TORC2 signaling pathways to coordinate cellular stress responses with sterol homeostasis.
[Mh] Termos MeSH primário: Antiporters/metabolismo
Microdomínios da Membrana/enzimologia
Complexos Multiproteicos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
Esteróis/metabolismo
Serina-Treonina Quinases TOR/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Antiporters/genética
Transporte Biológico
Proteínas de Transporte/genética
Proteínas de Transporte/metabolismo
Retículo Endoplasmático/enzimologia
Alvo Mecanístico do Complexo 2 de Rapamicina
Complexos Multiproteicos/genética
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Transdução de Sinais
Serina-Treonina Quinases TOR/genética
Fatores de Transcrição/genética
Vacúolos/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antiporters); 0 (Carrier Proteins); 0 (LTC1 protein, S cerevisiae); 0 (Multiprotein Complexes); 0 (RNA-Binding Proteins); 0 (Saccharomyces cerevisiae Proteins); 0 (Slm1 protein, S cerevisiae); 0 (Slm2 protein, S cerevisiae); 0 (Sterols); 0 (TORC1 protein complex, S cerevisiae); 0 (Transcription Factors); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201610032


  10 / 3254 MEDLINE  
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[PMID]:28719630
[Au] Autor:Ryu YS; Chandran SP; Kim K; Lee SK
[Ad] Endereço:School of Energy and Chemical Engineering, Ulsan National Institute of Science and Technology (UNIST), Ulsan, Republic of Korea.
[Ti] Título:Oligo- and dsDNA-mediated genome editing using a tetA dual selection system in Escherichia coli.
[So] Source:PLoS One;12(7):e0181501, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The ability to precisely and seamlessly modify a target genome is needed for metabolic engineering and synthetic biology techniques aimed at creating potent biosystems. Herein, we report on a promising method in Escherichia coli that relies on the insertion of an optimized tetA dual selection cassette followed by replacement of the same cassette with short, single-stranded DNA (oligos) or long, double-stranded DNA and the isolation of recombinant strains by negative selection using NiCl2. This method could be rapidly and successfully used for genome engineering, including deletions, insertions, replacements, and point mutations, without inactivation of the methyl-directed mismatch repair (MMR) system and plasmid cloning. The method we describe here facilitates positive genome-edited recombinants with selection efficiencies ranging from 57 to 92%. Using our method, we increased lycopene production (3.4-fold) by replacing the ribosome binding site (RBS) of the rate-limiting gene (dxs) in the 1-deoxy-D-xylulose-5-phosphate (DXP) biosynthesis pathway with a strong RBS. Thus, this method could be used to achieve scarless, proficient, and targeted genome editing for engineering E. coli strains.
[Mh] Termos MeSH primário: Antiporters/metabolismo
Proteínas de Bactérias/metabolismo
DNA de Cadeia Simples/genética
Escherichia coli/genética
Edição de Genes/métodos
Genômica
[Mh] Termos MeSH secundário: Sequência de Bases
Cromossomos Bacterianos/genética
Engenharia Metabólica
Pentosefosfatos/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-deoxylulose 5-phosphate); 0 (Antiporters); 0 (Bacterial Proteins); 0 (DNA, Single-Stranded); 0 (Pentosephosphates); 0 (tetA protein, Bacteria)
[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:170719
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181501



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