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Pesquisa : D08.811.913.225.650 [Categoria DeCS]
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[PMID]:29307522
[Au] Autor:Riberio DF; Cella PS; da Silva LECM; Jordao AA; Deminice R
[Ad] Endereço:Department of Physical Education, State University of Londrina, Londrina, PR, Brazil.
[Ti] Título:Acute exercise alters homocysteine plasma concentration in an intensity-dependent manner due increased methyl flux in liver of rats.
[So] Source:Life Sci;196:63-68, 2018 Mar 01.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:PURPOSE: We aimed to determine the effects of different intensities of acute exercise on Hcy plasma levels, and the exercise-induced changes in Hcy liver metabolism. METHOD: First, thirty-two Wistar rats were randomly submitted to an acute bout of swimming exercise carrying a load of 2% (n=8), 4% (n=8) and 6% (n=8) of their total body weight attached in their tail. Control rats remained rested (n=8). Blood samples were taken from tail vein for plasma S-containing amino acids determination before (Rest) and post, 1, 2, 3, 4, 6, and 10h after acute swimming exercise. Second, 56 exercised rats (4% loads) were euthanized before (Rest) and1, 2, 3, 4, 6, and 10h after acute swimming exercise. Blood and liver samples were collected for amino acids and keys genes involved in the Hcy metabolism assay. RESULTS: Acute exercise increases (P<0.05) plasma Hcy concentration in an intensity-dependent manner (rest 7.7±0.8; 6% load 13.8±3.6; 4% load 12.2±2.9±and 2% load 10.1±2.6, µmol/L); this increase is transient and does not promote hyperhomocysteinemia (<15µmol/L).Exercise-induced increased plasma Hcywas accompanied by the decreased liver S-adenosylmethionine/S-adenosylhomocysteine ratio and elevated MAT1a mRNA content. Acute exercise also caused elevated mRNA of key enzymes of transsulfuration (CBS) and remethylation (BHMT and the MTRR). CONCLUSION: Our data provided evidence that acute exercise increases plasma Hcy concentration due to the augmented requirement for methylated compounds that increases liver SAM consumption. Also, Hcy remethylation and transsulfuration are coordinately regulated to maintain methyl balance.
[Mh] Termos MeSH primário: Homocisteína/sangue
Fígado/metabolismo
Condicionamento Físico Animal/fisiologia
[Mh] Termos MeSH secundário: Animais
Peso Corporal/efeitos dos fármacos
Hiper-Homocisteinemia/metabolismo
Masculino
Metionina Adenosiltransferase/metabolismo
Metilação
Ratos
Ratos Wistar
S-Adenosil-Homocisteína/metabolismo
S-Adenosilmetionina/metabolismo
Natação/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0LVT1QZ0BA (Homocysteine); 7LP2MPO46S (S-Adenosylmethionine); 979-92-0 (S-Adenosylhomocysteine); EC 2.5.1.6 (Mat1a protein, rat); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29021282
[Au] Autor:Tang S; Fang Y; Huang G; Xu X; Padilla-Banks E; Fan W; Xu Q; Sanderson SM; Foley JF; Dowdy S; McBurney MW; Fargo DC; Williams CJ; Locasale JW; Guan Z; Li X
[Ad] Endereço:Signal Transduction Laboratory, National Institute of Environmental Health Sciences, Research Triangle Park, NC, USA.
[Ti] Título:Methionine metabolism is essential for SIRT1-regulated mouse embryonic stem cell maintenance and embryonic development.
[So] Source:EMBO J;36(21):3175-3193, 2017 Nov 02.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Methionine metabolism is critical for epigenetic maintenance, redox homeostasis, and animal development. However, the regulation of methionine metabolism remains unclear. Here, we provide evidence that SIRT1, the most conserved mammalian NAD -dependent protein deacetylase, is critically involved in modulating methionine metabolism, thereby impacting maintenance of mouse embryonic stem cells (mESCs) and subsequent embryogenesis. We demonstrate that SIRT1-deficient mESCs are hypersensitive to methionine restriction/depletion-induced differentiation and apoptosis, primarily due to a reduced conversion of methionine to S-adenosylmethionine. This reduction markedly decreases methylation levels of histones, resulting in dramatic alterations in gene expression profiles. Mechanistically, we discover that the enzyme converting methionine to S-adenosylmethionine in mESCs, methionine adenosyltransferase 2a (MAT2a), is under control of Myc and SIRT1. Consistently, SIRT1 KO embryos display reduced expression and histone methylation and are sensitive to maternal methionine restriction-induced lethality, whereas maternal methionine supplementation increases the survival of SIRT1 KO newborn mice. Our findings uncover a novel regulatory mechanism for methionine metabolism and highlight the importance of methionine metabolism in SIRT1-mediated mESC maintenance and embryonic development.
[Mh] Termos MeSH primário: Desenvolvimento Embrionário/genética
Epigênese Genética
Metionina Adenosiltransferase/genética
Metionina/metabolismo
Células-Tronco Embrionárias Murinas/metabolismo
Sirtuína 1/genética
[Mh] Termos MeSH secundário: Acetilação
Animais
Apoptose
Diferenciação Celular
Embrião de Mamíferos
Histonas/genética
Histonas/metabolismo
Metabolômica
Metionina/administração & dosagem
Metionina Adenosiltransferase/metabolismo
Metilação
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Análise em Microsséries
Células-Tronco Embrionárias Murinas/citologia
Proteínas Proto-Oncogênicas c-myc/genética
Proteínas Proto-Oncogênicas c-myc/metabolismo
S-Adenosilmetionina/metabolismo
Sirtuína 1/deficiência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histones); 0 (Myc protein, mouse); 0 (Proto-Oncogene Proteins c-myc); 7LP2MPO46S (S-Adenosylmethionine); AE28F7PNPL (Methionine); EC 2.5.1.6 (Methionine Adenosyltransferase); EC 3.5.1.- (Sirt1 protein, mouse); EC 3.5.1.- (Sirtuin 1)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201796708


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[PMID]:28679590
[Au] Autor:Boddu R; Fan C; Rangarajan S; Sunil B; Bolisetty S; Curtis LM
[Ad] Endereço:Division of Nephrology, Nephrology Research and Training Center, Department of Medicine, University of Alabama at Birmingham, Birmingham, Alabama; and.
[Ti] Título:Unique sex- and age-dependent effects in protective pathways in acute kidney injury.
[So] Source:Am J Physiol Renal Physiol;313(3):F740-F755, 2017 Sep 01.
[Is] ISSN:1522-1466
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sex and age influence susceptibility to acute kidney injury (AKI), with young females exhibiting lowest incidence. In these studies, we investigated mechanisms which may underlie the sex/age-based dissimilarities. Cisplatin (Cp)-induced AKI resulted in morphological evidence of injury in all groups. A minimal rise in plasma creatinine (PCr) was seen in Young Females, whereas in Aged Females, PCr rose precipitously. Relative to Young Males, Aged Males showed significantly, but temporally, comparably elevated PCr. Notably, Aged Females showed significantly greater mortality, whereas Young Females exhibited none. Tissue KIM-1 and plasma NGAL were significantly lower in Young Females than all others. IGFBP7 levels were modestly increased in both Young groups. IGFBP7 levels in Aged Females were significantly elevated at baseline relative to Aged Males, and increased linearly through , when these levels were comparable in both Aged groups. Plasma cytokine levels similarly showed a pattern of protective effects preferentially in Young Females. Expression of the drug transporter MATE2 did not explain the sex/age distinctions. Heme oxygenase-1 (HO-1) levels (~28-kDa species) showed elevation at in all groups with highest levels seen in Young Males. Exclusively in Young Females, these levels returned to baseline on , suggestive of a more efficient recovery. In aggregate, we demonstrate, for the first time, a distinctive pattern of response to AKI in Young Females relative to males which appears to be significantly altered in aging. These distinctions may offer novel targets to exploit therapeutically in both females and males in the treatment of AKI.
[Mh] Termos MeSH primário: Lesão Renal Aguda/prevenção & controle
Envelhecimento/metabolismo
Rim/metabolismo
[Mh] Termos MeSH secundário: Lesão Renal Aguda/induzido quimicamente
Lesão Renal Aguda/metabolismo
Lesão Renal Aguda/patologia
Fatores Etários
Envelhecimento/patologia
Animais
Autofagia
Proliferação Celular
Cisplatino
Creatinina/sangue
Citocinas/sangue
Modelos Animais de Doenças
Feminino
Heme Oxigenase-1/metabolismo
Receptor Celular 1 do Vírus da Hepatite A/metabolismo
Proteínas de Ligação a Fator de Crescimento Semelhante a Insulina/metabolismo
Rim/patologia
Lipocalina-2/sangue
Masculino
Proteínas de Membrana/metabolismo
Metionina Adenosiltransferase/metabolismo
Camundongos Endogâmicos C57BL
Fatores Sexuais
Transdução de Sinais
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Havcr1 protein, mouse); 0 (Hepatitis A Virus Cellular Receptor 1); 0 (Insulin-Like Growth Factor Binding Proteins); 0 (Lipocalin-2); 0 (Membrane Proteins); 0 (insulin-like growth factor binding protein-related protein 1); 126469-30-5 (Lcn2 protein, mouse); AYI8EX34EU (Creatinine); EC 1.14.14.18 (Heme Oxygenase-1); EC 1.14.14.18 (Hmox1 protein, mouse); EC 2.5.1.6 (Methionine Adenosyltransferase); Q20Q21Q62J (Cisplatin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1152/ajprenal.00049.2017


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[PMID]:28553945
[Au] Autor:Quinlan CL; Kaiser SE; Bolaños B; Nowlin D; Grantner R; Karlicek-Bryant S; Feng JL; Jenkinson S; Freeman-Cook K; Dann SG; Wang X; Wells PA; Fantin VR; Stewart AE; Grant SK
[Ad] Endereço:Oncology Research and Development, Pfizer Inc., San Diego, California, USA.
[Ti] Título:Targeting S-adenosylmethionine biosynthesis with a novel allosteric inhibitor of Mat2A.
[So] Source:Nat Chem Biol;13(7):785-792, 2017 Jul.
[Is] ISSN:1552-4469
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:S-Adenosyl-L-methionine (SAM) is an enzyme cofactor used in methyl transfer reactions and polyamine biosynthesis. The biosynthesis of SAM from ATP and L-methionine is performed by the methionine adenosyltransferase enzyme family (Mat; EC 2.5.1.6). Human methionine adenosyltransferase 2A (Mat2A), the extrahepatic isoform, is often deregulated in cancer. We identified a Mat2A inhibitor, PF-9366, that binds an allosteric site on Mat2A that overlaps with the binding site for the Mat2A regulator, Mat2B. Studies exploiting PF-9366 suggested a general mode of Mat2A allosteric regulation. Allosteric binding of PF-9366 or Mat2B altered the Mat2A active site, resulting in increased substrate affinity and decreased enzyme turnover. These data support a model whereby Mat2B functions as an inhibitor of Mat2A activity when methionine or SAM levels are high, yet functions as an activator of Mat2A when methionine or SAM levels are low. The ramification of Mat2A activity modulation in cancer cells is also described.
[Mh] Termos MeSH primário: Metionina Adenosiltransferase/antagonistas & inibidores
Quinolinas/farmacologia
S-Adenosilmetionina/metabolismo
Triazóis/farmacologia
[Mh] Termos MeSH secundário: Sítio Alostérico/efeitos dos fármacos
Linhagem Celular Tumoral
Relação Dose-Resposta a Droga
Seres Humanos
Cinética
Metionina Adenosiltransferase/isolamento & purificação
Metionina Adenosiltransferase/metabolismo
Quinolinas/química
Relação Estrutura-Atividade
Triazóis/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PF-9366); 0 (Quinolines); 0 (Triazoles); 7LP2MPO46S (S-Adenosylmethionine); EC 2.5.1.6 (MAT2A protein, human); EC 2.5.1.6 (Methionine Adenosyltransferase)
[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:170530
[St] Status:MEDLINE
[do] DOI:10.1038/nchembio.2384


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[PMID]:28525753
[Au] Autor:Pendleton KE; Chen B; Liu K; Hunter OV; Xie Y; Tu BP; Conrad NK
[Ad] Endereço:Department of Microbiology, UT Southwestern Medical Center, Dallas, TX 75390, USA.
[Ti] Título:The U6 snRNA m A Methyltransferase METTL16 Regulates SAM Synthetase Intron Retention.
[So] Source:Cell;169(5):824-835.e14, 2017 May 18.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Maintenance of proper levels of the methyl donor S-adenosylmethionine (SAM) is critical for a wide variety of biological processes. We demonstrate that the N -adenosine methyltransferase METTL16 regulates expression of human MAT2A, which encodes the SAM synthetase expressed in most cells. Upon SAM depletion by methionine starvation, cells induce MAT2A expression by enhanced splicing of a retained intron. Induction requires METTL16 and its methylation substrate, a vertebrate conserved hairpin (hp1) in the MAT2A 3' UTR. Increasing METTL16 occupancy on the MAT2A 3' UTR is sufficient to induce efficient splicing. We propose that, under SAM-limiting conditions, METTL16 occupancy on hp1 increases due to inefficient enzymatic turnover, which promotes MAT2A splicing. We further show that METTL16 is the long-unknown methyltransferase for the U6 spliceosomal small nuclear RNA (snRNA). These observations suggest that the conserved U6 snRNA methyltransferase evolved an additional function in vertebrates to regulate SAM homeostasis.
[Mh] Termos MeSH primário: Íntrons
Metionina Adenosiltransferase/genética
Metiltransferases/metabolismo
Processamento de RNA
S-Adenosilmetionina/metabolismo
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Regulação Enzimológica da Expressão Gênica
Células HEK293
Seres Humanos
Sequências Repetidas Invertidas
Metionina Adenosiltransferase/química
Metilação
Metiltransferases/química
Schizosaccharomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
7LP2MPO46S (S-Adenosylmethionine); EC 2.1.1.- (METTL16 protein, human); EC 2.1.1.- (Methyltransferases); EC 2.1.1.- (U6 small nuclear RNA methyltransferase); EC 2.5.1.6 (MAT2A protein, human); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170520
[St] Status:MEDLINE


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[PMID]:28420190
[Au] Autor:Ma C; Wang Y; Gu D; Nan J; Chen S; Li H
[Ad] Endereço:Key Laboratory of Molecular Biology, College of Heilongjiang Province, College of Life Sciences, Heilongjiang University, Harbin 150080, China. chqm0913@163.com.
[Ti] Título:Overexpression of S-Adenosyl-l-Methionine Synthetase 2 from Sugar Beet M14 Increased Arabidopsis Tolerance to Salt and Oxidative Stress.
[So] Source:Int J Mol Sci;18(4), 2017 Apr 18.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The sugar beet monosomic addition line M14 is a unique germplasm that contains genetic materials from L. and Zoss, and shows tolerance to salt stress. Our study focuses on exploring the molecular mechanism of the salt tolerance of the sugar beet M14. In order to identify differentially expressed genes in M14 under salt stress, a subtractive cDNA library was generated by suppression subtractive hybridization (SSH). A total of 36 unique sequences were identified in the library and their putative functions were analyzed. One of the genes, -adenosylmethionine synthetase ( ), is the key enzyme involved in the biosynthesis of -adenosylmethionine (SAM), a precursor of polyamines. To determine the potential role of in salt tolerance, we isolated from the salt-tolerant sugar beet M14. The expression of in leaves and roots was greatly induced by salt stress. Overexpression of in resulted in enhanced salt and H2O2 tolerance. Furthermore, we obtained a knock-down T-DNA insertion mutant of , which shares the highest homology with . Interestingly, the mutant showed sensitivity to salt and H2O2 stress. We also found that the antioxidant system and polyamine metabolism play an important role in salt and H2O2 tolerance in the -overexpressed plants. To our knowledge, the function of the sugar beet SAMS has not been reported before. Our results have provided new insights into SAMS functions in sugar beet.
[Mh] Termos MeSH primário: Arabidopsis/genética
Arabidopsis/metabolismo
Regulação da Expressão Gênica de Plantas
Metionina Adenosiltransferase/genética
Estresse Oxidativo/genética
Tolerância a Sal/genética
[Mh] Termos MeSH secundário: Antioxidantes/metabolismo
Clonagem Molecular
Biologia Computacional/métodos
Perfilação da Expressão Gênica
Ontologia Genética
Poliaminas/metabolismo
Estresse Fisiológico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Polyamines); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE


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[PMID]:28337758
[Au] Autor:Hao X; Zhou M; Li H; Angres IA
[Ad] Endereço:Arthus Biosystems, Richmond, CA, USA.
[Ti] Título:Novel immunoassays to detect methionine adenosyltransferase activity and quantify S-adenosylmethionine.
[So] Source:FEBS Lett;591(8):1114-1125, 2017 Apr.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We present a novel real-time immunoassay to measure methionine adenosyltransferase (MAT) activity that integrates the MAT-catalyzed reaction of Met and adenosine triphosphate to produce S-adenosylmethionine (SAM) and a highly sensitive immunoassay to specifically quantify SAM simultaneously. The cellular localization of SAM and S-adenosylhomocysteine varies with cell proliferation status: in normal cells, they are found mostly in the cytoplasm, but localize to the nucleus in proliferating cells. MAT-I/III activity is stimulated by Met, but inhibited by S-nitrosoglutathione, and the methylation index (MI) increases after Met stimulation of L02 cells. Met and S-nitrosoglutathione inhibit MAT-II activity, and the MI decreases after Met stimulation of HepG2 cells. The method described provides a significant advancement in the field for the measurement of MAT activity under various conditions.
[Mh] Termos MeSH primário: Hepatócitos/metabolismo
Metionina Adenosiltransferase/metabolismo
S-Adenosil-Homocisteína/metabolismo
S-Adenosilmetionina/metabolismo
[Mh] Termos MeSH secundário: Transporte Ativo do Núcleo Celular/efeitos dos fármacos
Animais
Especificidade de Anticorpos
Linhagem Celular
Núcleo Celular/efeitos dos fármacos
Núcleo Celular/enzimologia
Núcleo Celular/metabolismo
Proliferação Celular/efeitos dos fármacos
Células Cultivadas
Citoplasma/efeitos dos fármacos
Citoplasma/enzimologia
Citoplasma/metabolismo
Inibidores Enzimáticos/farmacologia
Ensaio de Imunoadsorção Enzimática
Citometria de Fluxo
Células Hep G2
Hepatócitos/citologia
Hepatócitos/efeitos dos fármacos
Seres Humanos
Metionina Adenosiltransferase/antagonistas & inibidores
Metilação/efeitos dos fármacos
Camundongos
Microscopia de Fluorescência
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 7LP2MPO46S (S-Adenosylmethionine); 979-92-0 (S-Adenosylhomocysteine); EC 2.5.1.6 (Methionine Adenosyltransferase)
[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:170325
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12631


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[PMID]:28186605
[Au] Autor:Sun Y; Ma D; Wang Y; Yang B; Jiang T
[Ad] Endereço:Center of Genetic Medicine, Obstetrics and Gynecology Hospital Affiliated to Nanjing Medical University, Jiangsu, Nanjing 210004, China. jiangzhang784@163.com.
[Ti] Título:[Analysis of MAT1A gene mutations in a child affected with simple hypermethioninemia].
[So] Source:Zhonghua Yi Xue Yi Chuan Xue Za Zhi;34(1):98-101, 2017 Feb 10.
[Is] ISSN:1003-9406
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To detect potential mutations of MAT1A gene in a child suspected with simple hypermethioninemia by MS/MS neonatal screening. METHODS: Clinical data of the child was collected. Genomic DNA was extracted by a standard method and subjected to targeted sequencing using an Ion Ampliseq Inherited Disease Panel. Detected mutations were verified by Sanger sequencing. RESULTS: The child showed no clinical features except evaluated methionine. A novel compound mutation of the MAT1A gene, i.e., c.345delA and c.529C>T, was identified in the child. His father and mother were found to be heterozygous for the c.345delA mutation and c.529C>T mutation, respectively. CONCLUSION: The compound mutation c.345delA and c.529C>T of the MAT1A gene probably underlie the disease in the child. The semi-conductor sequencing has provided an important means for the diagnosis of hereditary diseases.
[Mh] Termos MeSH primário: Erros Inatos do Metabolismo dos Aminoácidos/genética
Predisposição Genética para Doença/genética
Glicina N-Metiltransferase/deficiência
Doenças do Recém-Nascido/genética
Metionina Adenosiltransferase/genética
Mutação
[Mh] Termos MeSH secundário: Erros Inatos do Metabolismo dos Aminoácidos/patologia
Sequência de Bases
Análise Mutacional de DNA/métodos
Saúde da Família
Pai
Feminino
Glicina N-Metiltransferase/genética
Heterozigoto
Seres Humanos
Recém-Nascido
Doenças do Recém-Nascido/patologia
Masculino
Mães
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.1.1.20 (Glycine N-Methyltransferase); EC 2.5.1.6 (MAT1A protein, human); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170211
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1003-9406.2017.01.023


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[PMID]:28132890
[Au] Autor:Alonso C; Fernández-Ramos D; Varela-Rey M; Martínez-Arranz I; Navasa N; Van Liempd SM; Lavín Trueba JL; Mayo R; Ilisso CP; de Juan VG; Iruarrizaga-Lejarreta M; delaCruz-Villar L; Mincholé I; Robinson A; Crespo J; Martín-Duce A; Romero-Gómez M; Sann H; Platon J; Van Eyk J; Aspichueta P; Noureddin M; Falcón-Pérez JM; Anguita J; Aransay AM; Martínez-Chantar ML; Lu SC; Mato JM
[Ad] Endereço:OWL Metabolomics, Parque Tecnológico de Bizkaia, Derio, Spain.
[Ti] Título:Metabolomic Identification of Subtypes of Nonalcoholic Steatohepatitis.
[So] Source:Gastroenterology;152(6):1449-1461.e7, 2017 May.
[Is] ISSN:1528-0012
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND & AIMS: Nonalcoholic fatty liver disease (NAFLD) is a consequence of defects in diverse metabolic pathways that involve hepatic accumulation of triglycerides. Features of these aberrations might determine whether NAFLD progresses to nonalcoholic steatohepatitis (NASH). We investigated whether the diverse defects observed in patients with NAFLD are caused by different NAFLD subtypes with specific serum metabolomic profiles, and whether these can distinguish patients with NASH from patients with simple steatosis. METHODS: We collected liver and serum from methionine adenosyltransferase 1a knockout (MAT1A-KO) mice, which have chronically low levels of hepatic S-adenosylmethionine (SAMe) and spontaneously develop steatohepatitis, as well as C57Bl/6 mice (controls); the metabolomes of all samples were determined. We also analyzed serum metabolomes of 535 patients with biopsy-proven NAFLD (353 with simple steatosis and 182 with NASH) and compared them with serum metabolomes of mice. MAT1A-KO mice were also given SAMe (30 mg/kg/day for 8 weeks); liver samples were collected and analyzed histologically for steatohepatitis. RESULTS: Livers of MAT1A-KO mice were characterized by high levels of triglycerides, diglycerides, fatty acids, ceramides, and oxidized fatty acids, as well as low levels of SAMe and downstream metabolites. There was a correlation between liver and serum metabolomes. We identified a serum metabolomic signature associated with MAT1A-KO mice that also was present in 49% of the patients; based on this signature, we identified 2 NAFLD subtypes. We identified specific panels of markers that could distinguish patients with NASH from patients with simple steatosis for each subtype of NAFLD. Administration of SAMe reduced features of steatohepatitis in MAT1A-KO mice. CONCLUSIONS: In an analysis of serum metabolomes of patients with NAFLD and MAT1A-KO mice with steatohepatitis, we identified 2 major subtypes of NAFLD and markers that differentiate steatosis from NASH in each subtype. These might be used to monitor disease progression and identify therapeutic targets for patients.
[Mh] Termos MeSH primário: Metabolismo dos Lipídeos
Metaboloma
Metionina Adenosiltransferase/genética
Hepatopatia Gordurosa não Alcoólica/sangue
Hepatopatia Gordurosa não Alcoólica/classificação
[Mh] Termos MeSH secundário: Adulto
Animais
Biomarcadores/sangue
Ceramidas/metabolismo
Diglicerídeos/metabolismo
Ácidos Graxos/metabolismo
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Meia-Idade
Hepatopatia Gordurosa não Alcoólica/metabolismo
S-Adenosilmetionina/metabolismo
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Ceramides); 0 (Diglycerides); 0 (Fatty Acids); 0 (Triglycerides); 7LP2MPO46S (S-Adenosylmethionine); EC 2.5.1.6 (Mat1a protein, mouse); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170131
[St] Status:MEDLINE


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[PMID]:27994052
[Au] Autor:Thweatt JL; Ferlez BH; Golbeck JH; Bryant DA
[Ad] Endereço:From the Departments of Biochemistry and Molecular Biology and.
[Ti] Título:BciD Is a Radical S-Adenosyl-l-methionine (SAM) Enzyme That Completes Bacteriochlorophyllide e Biosynthesis by Oxidizing a Methyl Group into a Formyl Group at C-7.
[So] Source:J Biol Chem;292(4):1361-1373, 2017 Jan 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Green bacteria are chlorophotorophs that synthesize bacteriochlorophyll (BChl) c, d, or e, which assemble into supramolecular, nanotubular structures in large light-harvesting structures called chlorosomes. The biosynthetic pathways of these chlorophylls are known except for one reaction. Null mutants of bciD, which encodes a putative radical S-adenosyl-l-methionine (SAM) protein, are unable to synthesize BChl e but accumulate BChl c; however, it is unknown whether BciD is sufficient to convert BChl c (or its precursor, bacteriochlorophyllide (BChlide) c) into BChl e (or BChlide e). To determine the function of BciD, we expressed the bciD gene of Chlorobaculum limnaeum strain DSMZ 1677 in Escherichia coli and purified the enzyme under anoxic conditions. Electron paramagnetic resonance spectroscopy of BciD indicated that it contains a single [4Fe-4S] cluster. In assays containing SAM, BChlide c or d, and sodium dithionite, BciD catalyzed the conversion of SAM into 5'-deoxyadenosine and BChlide c or d into BChlide e or f, respectively. Our analyses also identified intermediates that are proposed to be 7 -OH-BChlide c and d Thus, BciD is a radical SAM enzyme that converts the methyl group of BChlide c or d into the formyl group of BChlide e or f This probably occurs by a mechanism involving consecutive hydroxylation reactions of the C-7 methyl group to form a geminal diol intermediate, which spontaneously dehydrates to produce the final products, BChlide e or BChlide f The demonstration that BciD is sufficient to catalyze the conversion of BChlide c into BChlide e completes the biosynthetic pathways for all "Chlorobium chlorophylls."
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Bacterioclorofilas/biossíntese
Chlorobi/enzimologia
Proteínas com Ferro-Enxofre/metabolismo
Metionina Adenosiltransferase/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Bacterioclorofilas/genética
Chlorobi/genética
Proteínas com Ferro-Enxofre/genética
Metionina Adenosiltransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Bacteriochlorophylls); 0 (Iron-Sulfur Proteins); EC 2.5.1.6 (Methionine Adenosyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161221
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.767665



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