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Pesquisa : D08.811.682.047.180 [Categoria DeCS]
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[PMID]:28663368
[Au] Autor:McClatchie T; Meredith M; Ouédraogo MO; Slow S; Lever M; Mann MRW; Zeisel SH; Trasler JM; Baltz JM
[Ad] Endereço:From the Ottawa Hospital Research Institute, Ottawa, Ontario K1H 8L6, Canada.
[Ti] Título:Betaine is accumulated via transient choline dehydrogenase activation during mouse oocyte meiotic maturation.
[So] Source:J Biol Chem;292(33):13784-13794, 2017 Aug 18.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Betaine ( -trimethylglycine) plays key roles in mouse eggs and preimplantation embryos first in a novel mechanism of cell volume regulation and second as a major methyl donor in blastocysts, but its origin is unknown. Here, we determined that endogenous betaine was present at low levels in germinal vesicle (GV) stage mouse oocytes before ovulation and reached high levels in the mature, ovulated egg. However, no betaine transport into oocytes was detected during meiotic maturation. Because betaine can be synthesized in mammalian cells via choline dehydrogenase (CHDH; EC 1.1.99.1), we assessed whether this enzyme was expressed and active. transcripts and CHDH protein were expressed in oocytes. No CHDH enzyme activity was detected in GV oocyte lysate, but CHDH became highly active during oocyte meiotic maturation. It was again inactive after fertilization. We then determined whether oocytes synthesized betaine and whether CHDH was required. Isolated maturing oocytes autonomously synthesized betaine in the presence of choline, whereas this failed to occur in oocytes, directly demonstrating a requirement for CHDH for betaine accumulation in oocytes. Overall, betaine accumulation is a previously unsuspected physiological process during mouse oocyte meiotic maturation whose underlying mechanism is the transient activation of CHDH.
[Mh] Termos MeSH primário: Betaína/metabolismo
Colina Desidrogenase/metabolismo
Oócitos/enzimologia
Oogênese
Regulação para Cima
[Mh] Termos MeSH secundário: Absorção Fisiológica
Animais
Blastocisto/citologia
Blastocisto/enzimologia
Blastocisto/metabolismo
Colina Desidrogenase/química
Colina Desidrogenase/genética
Cruzamentos Genéticos
Ativação Enzimática
Feminino
Regulação da Expressão Gênica no Desenvolvimento
Técnicas de Maturação in Vitro de Oócitos
Meiose
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Mórula/citologia
Mórula/enzimologia
Mórula/metabolismo
Oócitos/citologia
Oócitos/metabolismo
Trítio
Zigoto/citologia
Zigoto/enzimologia
Zigoto/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
10028-17-8 (Tritium); 3SCV180C9W (Betaine); EC 1.1.99.1 (Choline Dehydrogenase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.803080


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[PMID]:26910138
[Au] Autor:Scholz A; Stahl J; de Berardinis V; Müller V; Averhoff B
[Ad] Endereço:Department of Molecular Microbiology & Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt, Frankfurt am Main, Germany.
[Ti] Título:Osmotic stress response in Acinetobacter baylyi: identification of a glycine-betaine biosynthesis pathway and regulation of osmoadaptive choline uptake and glycine-betaine synthesis through a choline-responsive BetI repressor.
[So] Source:Environ Microbiol Rep;8(2):316-22, 2016 Apr.
[Is] ISSN:1758-2229
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acinetobacter baylyi, a ubiquitous soil bacterium, can cope with high salinity by uptake of choline as precursor of the compatible solute glycine betaine. Here, we report on the identification of a choline dehydrogenase (BetA) and a glycine betaine aldehyde dehydrogenase (BetB) mediating the oxidation of choline to glycine betaine. The betAB genes were found to form an operon together with the potential transcriptional regulator betI. The transcription of the betIBA operon and the two recently identified choline transporters was upregulated in response to choline and choline plus salt. The finding that the osmo-independent transporter BetT1 undergoes a higher upregulation in response to choline alone than betT2 suggests that BetT1 does not primarily function in osmoadaptation. Electrophoretic mobility shift assays led to the conclusion that BetI mediates transcriptional regulation of both, the betIBA gene operon and the choline transporters. BetI was released from the DNA in response to choline which together with the transcriptional upregulation of the bet genes in the presence of choline suggests that BetI is a choline sensing transcriptional repressor.
[Mh] Termos MeSH primário: Acinetobacter/fisiologia
Betaína/metabolismo
Vias Biossintéticas/genética
Colina/metabolismo
Regulação Bacteriana da Expressão Gênica
Osmorregulação
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Acinetobacter/genética
Acinetobacter/metabolismo
Colina Desidrogenase/genética
Colina Desidrogenase/metabolismo
Ensaio de Desvio de Mobilidade Eletroforética
Glicina Desidrogenase/genética
Glicina Desidrogenase/metabolismo
Proteínas de Membrana Transportadoras/genética
Proteínas de Membrana Transportadoras/metabolismo
Óperon
Oxirredução
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Transport Proteins); 0 (Repressor Proteins); 3SCV180C9W (Betaine); EC 1.1.99.1 (Choline Dehydrogenase); EC 1.4.1.10 (Glycine Dehydrogenase); N91BDP6H0X (Choline)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160225
[St] Status:MEDLINE
[do] DOI:10.1111/1758-2229.12382


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[PMID]:26058574
[Au] Autor:Lidbury I; Kimberley G; Scanlan DJ; Murrell JC; Chen Y
[Ad] Endereço:School of Life Sciences, University of Warwick, Coventry, CV4 7AL, UK.
[Ti] Título:Comparative genomics and mutagenesis analyses of choline metabolism in the marine Roseobacter clade.
[So] Source:Environ Microbiol;17(12):5048-62, 2015 Dec.
[Is] ISSN:1462-2920
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Choline is ubiquitous in marine eukaryotes and appears to be widely distributed in surface marine waters; however, its metabolism by marine bacteria is poorly understood. Here, using comparative genomics and molecular genetic approaches, we reveal that the capacity for choline catabolism is widespread in marine heterotrophs of the marine Roseobacter clade (MRC). Using the model bacterium Ruegeria pomeroyi, we confirm that the betA, betB and betC genes, encoding choline dehydrogenase, betaine aldehyde dehydrogenase and choline sulfatase, respectively, are involved in choline metabolism. The betT gene, encoding an organic solute transporter, was essential for the rapid uptake of choline but not glycine betaine (GBT). Growth of choline and GBT as a sole carbon source resulted in the re-mineralization of these nitrogen-rich compounds into ammonium. Oxidation of the methyl groups from choline requires formyltetrahydrofolate synthetase encoded by fhs in R. pomeroyi, deletion of which resulted in incomplete degradation of GBT. We demonstrate that this was due to an imbalance in the supply of reducing equivalents required for choline catabolism, which can be alleviated by the addition of formate. Together, our results demonstrate that choline metabolism is ubiquitous in the MRC and reveal the role of Fhs in methyl group oxidation in R. pomeroyi.
[Mh] Termos MeSH primário: Colina/metabolismo
Roseobacter/genética
Roseobacter/metabolismo
[Mh] Termos MeSH secundário: Organismos Aquáticos/genética
Organismos Aquáticos/metabolismo
Betaína/metabolismo
Betaína-Aldeído Desidrogenase/genética
Colina Desidrogenase/genética
Formiato-Tetra-Hidrofolato Ligase/genética
Genômica
Mutagênese
Sulfatases/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
3SCV180C9W (Betaine); EC 1.1.99.1 (Choline Dehydrogenase); EC 1.2.1.8 (Betaine-Aldehyde Dehydrogenase); EC 3.1.6.- (Sulfatases); EC 3.1.6.6 (choline-sulfatase); EC 6.3.4.3 (Formate-Tetrahydrofolate Ligase); N91BDP6H0X (Choline)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150611
[St] Status:MEDLINE
[do] DOI:10.1111/1462-2920.12943


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[PMID]:25921832
[Au] Autor:Silver MJ; Corbin KD; Hellenthal G; da Costa KA; Dominguez-Salas P; Moore SE; Owen J; Prentice AM; Hennig BJ; Zeisel SH
[Ad] Endereço:*Medical Research Council International Nutrition Group, London School of Hygiene and Tropical Medicine, London, United Kingdom; Medical Research Council Unit, Banjul, The Gambia; Nutrition Research Institute, North Carolina Research Campus, Kannapolis, North Carolina, USA; Department of Nutrition,
[Ti] Título:Evidence for negative selection of gene variants that increase dependence on dietary choline in a Gambian cohort.
[So] Source:FASEB J;29(8):3426-35, 2015 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Choline is an essential nutrient, and the amount needed in the diet is modulated by several factors. Given geographical differences in dietary choline intake and disparate frequencies of single-nucleotide polymorphisms (SNPs) in choline metabolism genes between ethnic groups, we tested the hypothesis that 3 SNPs that increase dependence on dietary choline would be under negative selection pressure in settings where choline intake is low: choline dehydrogenase (CHDH) rs12676, methylenetetrahydrofolate reductase 1 (MTHFD1) rs2236225, and phosphatidylethanolamine-N-methyltransferase (PEMT) rs12325817. Evidence of negative selection was assessed in 2 populations: one in The Gambia, West Africa, where there is historic evidence of a choline-poor diet, and the other in the United States, with a comparatively choline-rich diet. We used 2 independent methods, and confirmation of our hypothesis was sought via a comparison with SNP data from the Maasai, an East African population with a genetic background similar to that of Gambians but with a traditional diet that is higher in choline. Our results show that frequencies of SNPs known to increase dependence on dietary choline are significantly reduced in the low-choline setting of The Gambia. Our findings suggest that adequate intake levels of choline may have to be reevaluated in different ethnic groups and highlight a possible approach for identifying novel functional SNPs under the influence of dietary selective pressure.
[Mh] Termos MeSH primário: Colina/genética
Colina/metabolismo
Grupos Étnicos/genética
Polimorfismo de Nucleotídeo Único/genética
[Mh] Termos MeSH secundário: Colina Desidrogenase/genética
Colina Desidrogenase/metabolismo
Dieta/métodos
Feminino
Genótipo
Seres Humanos
Masculino
Metilenotetra-Hidrofolato Redutase (NADPH2)/genética
Metilenotetra-Hidrofolato Redutase (NADPH2)/metabolismo
Fosfatidiletanolamina N-Metiltransferase/genética
Fosfatidiletanolamina N-Metiltransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 1.1.99.1 (Choline Dehydrogenase); EC 1.5.1.20 (Methylenetetrahydrofolate Reductase (NADPH2)); EC 2.1.1.17 (Phosphatidylethanolamine N-Methyltransferase); N91BDP6H0X (Choline)
[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:150430
[St] Status:MEDLINE
[do] DOI:10.1096/fj.15-271056


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[PMID]:25483962
[Au] Autor:Park S; Choi SG; Yoo SM; Son JH; Jung YK
[Ad] Endereço:a Global Research Laboratory; School of Biological Science/Bio-MAX Institute ; Seoul National University ; Seoul , Korea.
[Ti] Título:Choline dehydrogenase interacts with SQSTM1/p62 to recruit LC3 and stimulate mitophagy.
[So] Source:Autophagy;10(11):1906-20, 2014.
[Is] ISSN:1554-8635
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:CHDH (choline dehydrogenase) is an enzyme catalyzing the dehydrogenation of choline to betaine aldehyde in mitochondria. Apart from this well-known activity, we report here a pivotal role of CHDH in mitophagy. Knockdown of CHDH expression impairs CCCP-induced mitophagy and PARK2/parkin-mediated clearance of mitochondria in mammalian cells, including HeLa cells and SN4741 dopaminergic neuronal cells. Conversely, overexpression of CHDH accelerates PARK2-mediated mitophagy. CHDH is found on both the outer and inner membranes of mitochondria in resting cells. Interestingly, upon induction of mitophagy, CHDH accumulates on the outer membrane in a mitochondrial potential-dependent manner. We found that CHDH is not a substrate of PARK2 but interacts with SQSTM1 independently of PARK2 to recruit SQSTM1 into depolarized mitochondria. The FB1 domain of CHDH is exposed to the cytosol and is required for the interaction with SQSTM1, and overexpression of the FB1 domain only in cytosol reduces CCCP-induced mitochondrial degradation via competitive interaction with SQSTM1. In addition, CHDH, but not the CHDH FB1 deletion mutant, forms a ternary protein complex with SQSTM1 and MAP1LC3 (LC3), leading to loading of LC3 onto the damaged mitochondria via SQSTM1. Further, CHDH is crucial to the mitophagy induced by MPP+ in SN4741 cells. Overall, our results suggest that CHDH is required for PARK2-mediated mitophagy for the recruitment of SQSTM1 and LC3 onto the mitochondria for cargo recognition.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Colina Desidrogenase/metabolismo
Proteínas Associadas aos Microtúbulos/metabolismo
Degradação Mitocondrial
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Cromatografia Líquida
Citosol/metabolismo
DNA Mitocondrial/metabolismo
Dopamina/química
Endopeptidase K/metabolismo
Citometria de Fluxo
Deleção de Genes
Proteínas de Fluorescência Verde/metabolismo
Células HEK293
Células HeLa
Seres Humanos
Espectrometria de Massas
Mitocôndrias/metabolismo
Neurônios/metabolismo
Ligação Proteica
RNA Interferente Pequeno/metabolismo
Proteína Sequestossoma-1
Ubiquitina-Proteína Ligases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (DNA, Mitochondrial); 0 (Microtubule-Associated Proteins); 0 (RNA, Small Interfering); 0 (SQSTM1 protein, human); 0 (Sequestosome-1 Protein); 0 (light chain 3, human); 147336-22-9 (Green Fluorescent Proteins); EC 1.1.99.1 (Choline Dehydrogenase); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (parkin protein); EC 3.4.21.64 (Endopeptidase K); VTD58H1Z2X (Dopamine)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141209
[St] Status:MEDLINE
[do] DOI:10.4161/auto.32177


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[PMID]:24444367
[Au] Autor:Gao J; Sampson NS
[Ad] Endereço:Department of Chemistry, Stony Brook University , Stony Brook, New York 11794-3400, United States.
[Ti] Título:A GMC oxidoreductase homologue is required for acetylation of glycopeptidolipid in Mycobacterium smegmatis.
[So] Source:Biochemistry;53(4):611-3, 2014 Feb 04.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Mycobacterium tuberculosis Rv3409c gene is required for modulation of the Toll-like receptor 2 (TLR-2) signaling response in infected macrophages. Although each is annotated as encoding a cholesterol oxidase, neither Rv3409c nor its ortholog MSMEG1604 is required for the metabolism of cholesterol in mycobacteria. Here we report that a unique lipid, L1334, accumulates in a MSMEG1604 transposon mutant in the Mycobacterium smegmatis cell envelope. L1334 is a polar glycopeptidolipid that is hyperrhamnosylated and in which the 6-deoxytalose moiety is not acetylated. The alteration of L1334 acetylation is consistent with a reduced level of interference with TLR-2 signaling in mutant infected macrophages.
[Mh] Termos MeSH primário: Oxirredutases do Álcool/metabolismo
Glicopeptídeos/metabolismo
Mycobacterium smegmatis/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Colina Desidrogenase/metabolismo
Glucose Desidrogenase/metabolismo
Mutação
Mycobacterium smegmatis/genética
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Glycopeptides); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.1.- (Glucose Dehydrogenases); EC 1.1.99.1 (Choline Dehydrogenase)
[Em] Mês de entrada:1404
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140122
[St] Status:MEDLINE
[do] DOI:10.1021/bi4015083


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[PMID]:23906661
[Au] Autor:Salvi F; Gadda G
[Ad] Endereço:Department of Chemistry, Georgia State University, Atlanta, GA 30302-3965, United States.
[Ti] Título:Human choline dehydrogenase: medical promises and biochemical challenges.
[So] Source:Arch Biochem Biophys;537(2):243-52, 2013 Sep 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Human choline dehydrogenase (CHD) is located in the inner membrane of mitochondria primarily in liver and kidney and catalyzes the oxidation of choline to glycine betaine. Its physiological role is to regulate the concentrations of choline and glycine betaine in the blood and cells. Choline is important for regulation of gene expression, the biosynthesis of lipoproteins and membrane phospholipids and for the biosynthesis of the neurotransmitter acetylcholine; glycine betaine plays important roles as a primary intracellular osmoprotectant and as methyl donor for the biosynthesis of methionine from homocysteine, a required step for the synthesis of the ubiquitous methyl donor S-adenosyl methionine. Recently, CHD has generated considerable medical attention due to its association with various human pathologies, including male infertility, homocysteinuria, breast cancer and metabolic syndrome. Despite the renewed interest, the biochemical characterization of the enzyme has lagged behind due to difficulties in the obtainment of purified, active and stable enzyme. This review article summarizes the medical relevance and the physiological roles of human CHD, highlights the biochemical knowledge on the enzyme, and provides an analysis based on the comparison of the protein sequence with that of bacterial choline oxidase, for which structural and biochemical information is available.
[Mh] Termos MeSH primário: Colina Desidrogenase/química
Colina Desidrogenase/metabolismo
Homocistinúria/enzimologia
Infertilidade Masculina/enzimologia
Síndrome Metabólica/enzimologia
Mitocôndrias/enzimologia
[Mh] Termos MeSH secundário: Estabilidade Enzimática
Seres Humanos
Masculino
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
EC 1.1.99.1 (Choline Dehydrogenase)
[Em] Mês de entrada:1310
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130803
[St] Status:MEDLINE


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[PMID]:23684804
[Au] Autor:Ash JA; Jiang X; Malysheva OV; Fiorenza CG; Bisogni AJ; Levitsky DA; Strawderman MS; Caudill MA; Stover PJ; Strupp BJ
[Ad] Endereço:Division of Nutritional Sciences, Cornell University, Ithaca, NY 14853, United States. jessica.ash@nih.gov
[Ti] Título:Dietary and genetic manipulations of folate metabolism differentially affect neocortical functions in mice.
[So] Source:Neurotoxicol Teratol;38:79-91, 2013 Jul-Aug.
[Is] ISSN:1872-9738
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Converging evidence suggests that folate-mediated one-carbon metabolism may modulate cognitive functioning throughout the lifespan, but few studies have directly tested this hypothesis. This study examined the separate and combined effects of dietary and genetic manipulations of folate metabolism on neocortical functions in mice, modeling a common genetic variant in the MTHFD1 gene in humans. Mutant (Mthfd1(gt/+)) and wildtype (WT) male mice were assigned to a folate sufficient or deficient diet at weaning and continued on these diets throughout testing on a series of visual attention tasks adapted from the 5-choice serial reaction time task. WT mice on a deficient diet exhibited impulsive responding immediately following a change in task parameters that increased demands on attention and impulse control, and on trials following an error. This pattern of findings indicates a heightened affective response to stress and/or an inability to regulate negative emotions. In contrast, Mthfd1(gt/+) mice (regardless of diet) exhibited attentional dysfunction and a blunted affective response to committing an error. The Mthfd1(gt/+) mice also showed significantly decreased expression levels for genes encoding choline dehydrogenase and the alpha 7 nicotinic cholinergic receptor. The effects of the MTHFD1 mutation were less pronounced when combined with a deficient diet, suggesting a compensatory mechanism to the combined genetic and dietary perturbation of folate metabolism. These data demonstrate that common alterations in folate metabolism can produce functionally distinct cognitive and affective changes, and highlight the importance of considering genotype when making dietary folate recommendations.
[Mh] Termos MeSH primário: Deficiência de Ácido Fólico/genética
Deficiência de Ácido Fólico/psicologia
Ácido Fólico/metabolismo
Comportamento Impulsivo/genética
Comportamento Impulsivo/metabolismo
Metilenotetra-Hidrofolato Desidrogenase (NADP)/genética
Neocórtex/metabolismo
[Mh] Termos MeSH secundário: Animais
Atenção
Colina Desidrogenase/biossíntese
Dieta
Discriminação (Psicologia)
Ácido Fólico/sangue
Expressão Gênica/genética
Masculino
Camundongos
Mutação
Receptor Nicotínico de Acetilcolina alfa7/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (alpha7 Nicotinic Acetylcholine Receptor); 935E97BOY8 (Folic Acid); EC 1.1.99.1 (Choline Dehydrogenase); EC 1.5.1.5 (Methylenetetrahydrofolate Dehydrogenase (NADP))
[Em] Mês de entrada:1411
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130521
[St] Status:MEDLINE


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[PMID]:23110363
[Au] Autor:Sheen TR; O'Callaghan M; Smalley DJ; Ronson CW; Hurst MR
[Ad] Endereço:Innovative Farm Systems, AgResearch, Lincoln Research Centre, Christchurch, New Zealand.
[Ti] Título:Serratia entomophila bet gene induction and the impact of glycine betaine accumulation on desiccation tolerance.
[So] Source:J Appl Microbiol;114(2):470-81, 2013 Feb.
[Is] ISSN:1365-2672
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIMS: The genes involved in choline transport and oxidation to glycine betaine in the biopesticidal bacterium Serratia entomophila were characterized, and the potential of osmoprotectants, coupled with increased NaCl concentrations, to improve the desiccation tolerance of this species was investigated. METHODS AND RESULTS: Serratia entomophila carries sequences similar to the Escherichia coli betTIBA genes encoding a choline transporter and dehydrogenase, a betaine aldehyde dehydrogenase and a regulatory protein. Disruption of betA abolished the ability of Ser. entomophila to utilize choline as a carbon source. Quantitative reverse-transcriptase PCR analysis revealed that betA transcription was reduced compared to that of the upstream genes in the operon, and that NaCl and choline induced bet gene expression. Glycine betaine and choline increased the NaCl tolerance of Ser. entomophila, and osmotically preconditioned cultures survived better than control cultures following desiccation and immediately after application to agricultural soil. CONCLUSIONS: Addition of glycine betaine and NaCl to growth medium can greatly enhance the desiccation survival of Ser. entomophila, and its initial survival in soil. SIGNIFICANCE AND IMPACT OF THE STUDY: Serratia entomophila is sensitive to desiccation and does not persist under low soil moisture conditions. Techniques described here for enhancing the desiccation survival of Ser. entomophila can be used to improve formulations of this bacterium, and allow its application under a wider range of environmental conditions.
[Mh] Termos MeSH primário: Betaína/metabolismo
Regulação Bacteriana da Expressão Gênica
Serratia/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Betaína-Aldeído Desidrogenase/biossíntese
Betaína-Aldeído Desidrogenase/genética
Colina/metabolismo
Colina/farmacologia
Colina Desidrogenase/biossíntese
Colina Desidrogenase/genética
Colina Desidrogenase/fisiologia
Dessecação
Genes Bacterianos
Dados de Sequência Molecular
Concentração Osmolar
Análise de Sequência de DNA
Serratia/efeitos dos fármacos
Serratia/metabolismo
Cloreto de Sódio/farmacologia
Microbiologia do Solo
Fatores de Transcrição/biossíntese
Fatores de Transcrição/genética
Transcrição Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transcription Factors); 3SCV180C9W (Betaine); 451W47IQ8X (Sodium Chloride); EC 1.1.99.1 (Choline Dehydrogenase); EC 1.2.1.8 (Betaine-Aldehyde Dehydrogenase); N91BDP6H0X (Choline)
[Em] Mês de entrada:1312
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:121101
[St] Status:MEDLINE
[do] DOI:10.1111/jam.12052


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[PMID]:22558321
[Au] Autor:Johnson AR; Lao S; Wang T; Galanko JA; Zeisel SH
[Ad] Endereço:Department of Nutrition, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina, USA.
[Ti] Título:Choline dehydrogenase polymorphism rs12676 is a functional variation and is associated with changes in human sperm cell function.
[So] Source:PLoS One;7(4):e36047, 2012.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Approximately 15% of couples are affected by infertility and up to half of these cases arise from male factor infertility. Unidentified genetic aberrations such as chromosomal deletions, translocations and single nucleotide polymorphisms (SNPs) may be the underlying cause of many cases of idiopathic male infertility. Deletion of the choline dehydrogenase (Chdh) gene in mice results in decreased male fertility due to diminished sperm motility; sperm from Chdh(-/-) males have decreased ATP concentrations likely stemming from abnormal sperm mitochondrial morphology and function in these cells. Several SNPs have been identified in the human CHDH gene that may result in altered CHDH enzymatic activity. rs12676 (G233T), a non-synonymous SNP located in the CHDH coding region, is associated with increased susceptibility to dietary choline deficiency and risk of breast cancer. We now report evidence that this SNP is also associated with altered sperm motility patterns and dysmorphic mitochondrial structure in sperm. Sperm produced by men who are GT or TT for rs12676 have 40% and 73% lower ATP concentrations, respectively, in their sperm. rs12676 is associated with decreased CHDH protein in sperm and hepatocytes. A second SNP located in the coding region of IL17BR, rs1025689, is linked to altered sperm motility characteristics and changes in choline metabolite concentrations in sperm.
[Mh] Termos MeSH primário: Colina Desidrogenase/genética
Polimorfismo de Nucleotídeo Único/genética
Espermatozoides/citologia
Espermatozoides/enzimologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Adolescente
Adulto
Idoso
Alelos
Animais
Colina/sangue
Metabolismo Energético/genética
Frequência do Gene/genética
Genótipo
Homozigoto
Seres Humanos
Masculino
Camundongos
Meia-Idade
Mitocôndrias/ultraestrutura
Sêmen/metabolismo
Motilidade Espermática/genética
Espermatozoides/ultraestrutura
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
8L70Q75FXE (Adenosine Triphosphate); EC 1.1.99.1 (Choline Dehydrogenase); N91BDP6H0X (Choline)
[Em] Mês de entrada:1209
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:120505
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0036047



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