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  1 / 228 MEDLINE  
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PMID:27739310
Autor:Heger Z; Eckschlager T; Stiborová M; Adam V
Título:[Glycine-N-methyltransferase and Malignant Diseases of the Prostate].
Título:Glycin-N-metyltransferáza a nádorová onemocnení prostaty..
Fuente:Klin Onkol; 29(5):331-335, 2016.
ISSN:0862-495X
País de publicación:Czech Republic
Idioma:cze
Resumen:BACKGROUND: Prostate cancer (PC) constitutes a heterogeneous group of diseases with high prevalence rates that are still increasing, particularly in western countries. Since 1980, prostate specific antigen (PSA) and other diagnostic approaches have been used for PC screening; however, some of these approaches are often deemed painful and cause invasive damage of tissue. Therefore, molecular approaches to PC diagnosis are attracting increasing attention, potentially providing patients with less stressful situations and providing better diagnoses and even prognostic information. Recent metabolomic and genomic studies have suggested that biomolecules can be used as diagnostic or prognostic markers or as targets for the development of novel therapeutic modalities. One of these molecules is glycine-N-methyltransferase (GNMT), an enzyme that plays a pivotal role in the biochemical conversion of glycine to sarcosine. The link between this molecule (encoded by homonymous gene - GNMT) and PC has been confirmed at several levels, and thus GNMT can be considered a promising target for the development of advanced diagnostic and/or prognostic approaches. AIM: The aim of this study was to analyse the physiological role of GNMT and to examine in greater detail its connection with PC at different levels, including gene structure, gene expression, and metabolism, in which GNMT plays an important role, not only in controlling the methylation status of cells, but also the metabolism of folic acid and methionine. Last but not least, we discuss the importance of cellular methylation processes and the link between their aberrations and PC development.Key words: glycine - folic acid - metabolism - methylation - sarcosineThis work was supported by GA CR 16-18917S, League against Cancer Prague (project 2022015) and Czech Ministry of Health - RVO, UH Motol 00064203.The authors declare they have no potential confl icts of interest concerning drugs, products, or services used in the study.The Editorial Board declares that the manuscript met the ICMJE recommendation for biomedical papers.Submitted: 9. 2. 2016Accepted: 20. 3. 2016.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Biomarkers, Tumor); 935E97BOY8 (Folic Acid); AE28F7PNPL (Methionine); EC 2.1.1.20 (Glycine N-Methyltransferase)


  2 / 228 MEDLINE  
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PMID:28383162
Autor:Mishra SK; Sankar K; Jernigan RL
Dirección:Bioinformatics and Computational Biology Program, Iowa State University, Ames, Iowa, 50011.
Título:Altered dynamics upon oligomerization corresponds to key functional sites.
Fuente:Proteins; 85(8):1422-1434, 2017 Aug.
ISSN:1097-0134
País de publicación:United States
Idioma:eng
Resumen:It is known that over half of the proteins encoded by most organisms function as oligomeric complexes. Oligomerization confers structural stability and dynamics changes in proteins. We investigate the effects of oligomerization on protein dynamics and its functional significance for a set of 145 multimeric proteins. Using coarse-grained elastic network models, we inspect the changes in residue fluctuations upon oligomerization and then compare with residue conservation scores to identify the functional significance of these changes. Our study reveals conservation of about ½ of the fluctuations, with » of the residues increasing in their mobilities and » having reduced fluctuations. The residues with dampened fluctuations are evolutionarily more conserved and can serve as orthosteric binding sites, indicating their importance. We also use triosephosphate isomerase as a test case to understand why certain enzymes function only in their oligomeric forms despite the monomer including all required catalytic residues. To this end, we compare the residue communities (groups of residues which are highly correlated in their fluctuations) in the monomeric and dimeric forms of the enzyme. We observe significant changes to the dynamical community architecture of the catalytic core of this enzyme. This relates to its functional mechanism and is seen only in the oligomeric form of the protein, answering why proteins are oligomeric structures. Proteins 2017; 85:1422-1434. © 2017 Wiley Periodicals, Inc.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:EC 1.4.1.2 (Glutamate Dehydrogenase); EC 1.4.3.- (Dao1 protein, mouse); EC 1.4.3.3 (D-Amino-Acid Oxidase); EC 2.1.1.20 (Glycine N-Methyltransferase); EC 3.5.3.1 (Arginase); EC 3.5.3.1 (arginase I, human); EC 5.3.1.1 (Triose-Phosphate Isomerase)


  3 / 228 MEDLINE  
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PMID:28205209
Autor:Li CH; Yen CH; Chen YF; Lee KJ; Fang CC; Zhang X; Lai CC; Huang SF; Lin HK; Arthur Chen YM
Dirección:Center for Infectious Disease and Cancer Research (CICAR), Kaohsiung Medical University, Kaohsiung, 80708, Taiwan.
Título:Characterization of the GNMT-HectH9-PREX2 tripartite relationship in the pathogenesis of hepatocellular carcinoma.
Fuente:Int J Cancer; 140(10):2284-2297, 2017 May 15.
ISSN:1097-0215
País de publicación:United States
Idioma:eng
Resumen:The pathogenesis of hepatocellular carcinoma (HCC) involves many molecular pathways. Glycine N-methyltransferase (GNMT) is downregulated in almost all HCC and its gene knockout mice developed HCC with high penetrance. We identified PREX2, a novel PTEN inhibitor, as a GNMT-interacting protein. Such interaction enhanced degradation of PREX2 through an E3 ligase HectH9-mediated proteasomal ubiquitination pathway. Depletion of GNMT or HectH9 resulted in AKT activation in a PREX2 dependent manner and enhanced cell proliferation. An elevated PREX2 protein expression accompanied by activation of AKT was observed in the liver of Gnmt knockout mice. PREX2 protein expression was upregulated in 54.9% of human HCC samples, while its mRNA level was comparable in tumor and tumor-adjacent tissue, suggesting a post-translational alteration of PREX2 expression. Higher level of PREX2 in the tumor tissues was associated with poorer survival. These results reveal a novel mechanism in which GNMT participates in AKT signaling and HCC tumorigenesis by promoting HectH9-mediated PREX2 degradation.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Biomarkers, Tumor); 0 (Guanine Nucleotide Exchange Factors); 0 (PREX2 protein, human); 0 (RNA, Messenger); EC 2.1.1.20 (GNMT protein, human); EC 2.1.1.20 (Glycine N-Methyltransferase); EC 2.3.2.26 (HUWE1 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (PTEN protein, human)


  4 / 228 MEDLINE  
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PMID:28186605
Autor:Sun Y; Ma D; Wang Y; Yang B; Jiang T
Dirección:Center of Genetic Medicine, Obstetrics and Gynecology Hospital Affiliated to Nanjing Medical University, Jiangsu, Nanjing 210004, China. jiangzhang784@163.com.
Título:[Analysis of MAT1A gene mutations in a child affected with simple hypermethioninemia].
Fuente:Zhonghua Yi Xue Yi Chuan Xue Za Zhi; 34(1):98-101, 2017 Feb 10.
ISSN:1003-9406
País de publicación:China
Idioma:chi
Resumen: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.
Tipo de publicación:CASE REPORTS; JOURNAL ARTICLE
Nombre de substancia:EC 2.1.1.20 (Glycine N-Methyltransferase); EC 2.5.1.6 (MAT1A protein, human); EC 2.5.1.6 (Methionine Adenosyltransferase)


  5 / 228 MEDLINE  
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PMID:28036340
Autor:Lai SJ; Deng YC; Lai MC
Dirección:Department of Life Sciences, National Chung Hsing University, Taichung, Taiwan.
Título:Comparison of Enzymatic Traits between Native and Recombinant Glycine Sarcosine N-Methyltransferase from Methanohalophilus portucalensis FDF1T.
Fuente:PLoS One; 11(12):e0168666, 2016.
ISSN:1932-6203
País de publicación:United States
Idioma:eng
Resumen:The halophilic methanoarchaeon Methanohalophilus portucalensis FDF1T possesses the ability to synthesize the osmolyte betaine from its precursor, glycine, in response to extracellular salt stress through a three-step transmethylation process. Analysis of recombinant glycine sarcosine N-methyltransferase (rGSMT) and recombinant sarcosine dimethylglycine N-methyltransferase (rSDMT) from Escherichia coli indicated that betaine synthesis is rate-limited by rGSMT and is constitutively activated by rSDMT. Therefore, it is of interest to purify native GSMT from Methanohalophilus portucalensis to further compare its enzymatic characteristics and kinetics with rGSMT. In this study, native GSMT was purified through DEAE ion exchange and gel filtration chromatography with 95% purity. The enzymatic characteristics of GSMT and rGSMT showed similar trends of activities that were activated by high concentrations of monovalent cations. Both were feedback-inhibited by the end product, betaine, and competitively inhibited by S-adenosylhomocysteine (SAH). Native GSMT was 2-fold more sensitive to SAH than rGSMT. Notably, comparison of the kinetic parameters illustrated that the turnover rate of glycine methylation of GSMT was promoted by potassium ions, whereas rGSMT was activated by increasing protein-glycine binding affinity. These results suggest that GSMT and rGSMT may have different levels of post-translational modifications. Our preliminary mass spectrometry evidence indicated that there was no detectable phosphosite on GSMT after the complicated purification processes, whereas purified rGSMT still possessed 23.1% of its initial phosphorylation level. We believe that a phosphorylation-mediated modification may be involved in the regulation of this energy consuming betaine synthesis pathway during the stress response in halophilic methanoarchaea.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Archaeal Proteins); 3SCV180C9W (Betaine); 7797M4CPPA (dimethylglycine); 979-92-0 (S-Adenosylhomocysteine); EC 2.1.1.20 (Glycine N-Methyltransferase); TE7660XO1C (Glycine); Z711V88R5F (Sarcosine)


  6 / 228 MEDLINE  
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PMID:27824899
Autor:Heger Z; Merlos Rodrigo MA; Michalek P; Polanska H; Masarik M; Vit V; Plevova M; Pacik D; Eckschlager T; Stiborova M; Adam V
Dirección:Department of Chemistry and Biochemistry, Mendel University in Brno, Zemedelska 1, CZ-613 00, Brno, Czech Republic.
Título:Sarcosine Up-Regulates Expression of Genes Involved in Cell Cycle Progression of Metastatic Models of Prostate Cancer.
Fuente:PLoS One; 11(11):e0165830, 2016.
ISSN:1932-6203
País de publicación:United States
Idioma:eng
Resumen:The effects of sarcosine on the processes driving prostate cancer (PCa) development remain still unclear. Herein, we show that a supplementation of metastatic PCa cells (androgen independent PC-3 and androgen dependent LNCaP) with sarcosine stimulates cells proliferation in vitro. Similar stimulatory effects were observed also in PCa murine xenografts, in which sarcosine treatment induced a tumor growth and significantly reduced weight of treated mice (p < 0.05). Determination of sarcosine metabolism-related amino acids and enzymes within tumor mass revealed significantly increased glycine, serine and sarcosine concentrations after treatment accompanied with the increased amount of sarcosine dehydrogenase. In both tumor types, dimethylglycine and glycine-N-methyltransferase were affected slightly, only. To identify the effects of sarcosine treatment on the expression of genes involved in any aspect of cancer development, we further investigated expression profiles of excised tumors using cDNA electrochemical microarray followed by validation using the semi-quantitative PCR. We found 25 differentially expressed genes in PC-3, 32 in LNCaP tumors and 18 overlapping genes. Bioinformatical processing revealed strong sarcosine-related induction of genes involved particularly in a cell cycle progression. Our exploratory study demonstrates that sarcosine stimulates PCa metastatic cells irrespectively of androgen dependence. Overall, the obtained data provides valuable information towards understanding the role of sarcosine in PCa progression and adds another piece of puzzle into a picture of sarcosine oncometabolic potential.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:EC 1.5.8.3 (Sarcosine Dehydrogenase); EC 2.1.1.20 (Glycine N-Methyltransferase); Z711V88R5F (Sarcosine)


  7 / 228 MEDLINE  
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PMID:27716281
Autor:Liao YJ; Lee TS; Twu YC; Hsu SM; Yang CP; Wang CK; Liang YC; Chen YA
Dirección:School of Medical Laboratory Science and Biotechnology, College of Medical Science and Technology, Taipei Medical University, Taipei, Taiwan.
Título:Glycine N-methyltransferase deficiency in female mice impairs insulin signaling and promotes gluconeogenesis by modulating the PI3K/Akt pathway in the liver.
Fuente:J Biomed Sci; 23(1):69, 2016 Oct 04.
ISSN:1423-0127
País de publicación:England
Idioma:eng
Resumen:BACKGROUND: Glycine N-methyltransferase (GNMT) is abundantly expressed in the normal liver but is down-regulated in liver cancer tissues. GNMT knockout (Gnmt-/-) mice can spontaneously develop chronic hepatitis, fatty liver, and liver cancer. We previously demonstrated that hepatic GNMT is decreased in high-fat-diet-induced type 2 diabetes mellitus, but its contribution to metabolic syndrome is unclear. Here we show that GNMT modulates key aspects of metabolic syndrome in mice. METHODS: Eleven-week-old Gnmt-/- and wild-type (WT) mice with a C57BL/6 genetic background were used in this study. The metabolic defects of GNMT deficiency were measured by glucose and insulin tolerance tests, lipid homeostasis, gluconeogenesis, and insulin signaling. RESULTS: Gnmt-/- mice, especially females, exhibited glucose intolerance and insulin resistance. However, their body fat and lean mass, food and water intakes, and energy expenditure did not differ from those of WT mice. In addition, glucose-stimulated insulin secretion and insulin-stimulated glucagon secretion were normal in the serum and pancreatic islets of Gnmt-/- mice. Importantly, we found that GNMT deficiency increased lipogenesis and triglycerides in the liver. The elevated triglycerides disrupted the ability of insulin to induce Akt and S6 ribosomal protein phosphorylation, and then triggered insulin resistance and gluconeogenesis in female Gnmt-/- mice. CONCLUSIONS: Our data indicate that hepatic GNMT regulates lipid and glucose homeostasis, and provide insight into the development of insulin resistance through modulating the PI3K/Akt pathway.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Insulin); EC 2.1.1.20 (Glycine N-Methyltransferase); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)


  8 / 228 MEDLINE  
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PMID:27648945
Autor:Jia Y; Ling M; Zhang L; Jiang S; Sha Y; Zhao R
Dirección:Key Laboratory of Animal Physiology & Biochemistry, College of Veterinary Medicine, Nanjing Agricultural University , Nanjing 210095, People's Republic of China.
Título:Downregulation of miR-150 Expression by DNA Hypermethylation Is Associated with High 2-Hydroxy-(4-methylthio)butanoic Acid-Induced Hepatic Cholesterol Accumulation in Nursery Piglets.
Fuente:J Agric Food Chem; 64(40):7530-7539, 2016 Oct 12.
ISSN:1520-5118
País de publicación:United States
Idioma:eng
Resumen:Excess 2-hydroxy-(4-methylthio)butanoic acid (HMB) supplementation induces hyperhomocysteinemia, which contributes to hepatic cholesterol accumulation. However, it is unclear whether and how high levels of HMB break hepatic cholesterol homeostasis in nursery piglets. In this study, HMB oversupplementation suppressed food intake and decreased body weight in nursery piglets. Hyperhomocysteinemia and higher hepatic cholesterol accumulation were observed in HMB groups. Accordingly, HMB significantly increased the protein content of 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR) and glycine N-methyltransferase (GNMT) but decreased that of acyl-coenzyme A:cholesterol acyltransferase-1 (ACAT1). Significant downregulation of miR-150, miR-181d-5p, and miR-296-3p targeting the 3'-untranslated regions (UTRs) of GNMT and HMGCR was detected in the liver of HMB-treated piglets, and their functional validation was confirmed by dual-luciferase reporter assay. Furthermore, hypermethylation of miR-150 promoter was detected in association with suppressed miR-150 expression in the livers of HMB-treated piglets. This study indicated a new mechanism of hepatic cholesterol unhomeostasis by dietary methyl donor supplementation.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (3' Untranslated Regions); 0 (MicroRNAs); 583-91-5 (alpha-hydroxy-gamma-methylmercaptobutyric acid); 97C5T2UQ7J (Cholesterol); AE28F7PNPL (Methionine); EC 1.1.1.- (Hydroxymethylglutaryl CoA Reductases); EC 2.1.1.20 (Glycine N-Methyltransferase); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)


  9 / 228 MEDLINE  
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PMID:27177696
Autor:Levy HL
Dirección:Division of Genetics and Genomics, Boston Children's Hospital, Boston, MA, United States; Harvard Medical School, Boston, MA, United States. Electronic address: harvey.levy@childrens.harvard.edu.
Título:The remarkable S. Harvey Mudd - A reminiscence.
Fuente:Mol Genet Metab; 118(3):143-4, 2016 Jul.
ISSN:1096-7206
País de publicación:United States
Idioma:eng
Resumen:Harvey Mudd was the father of methionine metabolic disorders. Beginning with his identification of the enzyme defect in homocystinuria, he co-discovered cobalamin C disorder as the first known human disorder of vitamin B12 metabolism, thereby extending our concept of homocystinuria as a key feature of related disorders rather than a single disease, and identified new disorders that produce hypermethioninemia. He had no equal in our understanding of how critical methionine metabolism is to human homeostasis.
Tipo de publicación:BIOGRAPHY; HISTORICAL ARTICLE; JOURNAL ARTICLE
Nombre personal como asunto:Mudd H
Nombre de substancia:AE28F7PNPL (Methionine); EC 2.1.1.20 (Glycine N-Methyltransferase)


  10 / 228 MEDLINE  
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PMID:27153064
Autor:Kant R; Yen CH; Lu CK; Lin YC; Li JH; Chen YM
Dirección:Institute of Microbiology and Immunology, National Yang-Ming University, Taipei 11221, Taiwan. rajnihpmicro@gmail.com.
Título:Identification of 1,2,3,4,6-Penta-O-galloyl-ß-d-glucopyranoside as a Glycine N-Methyltransferase Enhancer by High-Throughput Screening of Natural Products Inhibits Hepatocellular Carcinoma.
Fuente:Int J Mol Sci; 17(5), 2016 May 04.
ISSN:1422-0067
País de publicación:Switzerland
Idioma:eng
Resumen:Glycine N-methyltransferase (GNMT) expression is vastly downregulated in hepatocellular carcinomas (HCC). High rates of GNMT knockout mice developed HCC, while overexpression of GNMT prevented aflatoxin-induced carcinogenicity and inhibited liver cancer cell proliferation. Therefore, in this study, we aimed for the identification of a GNMT inducer for HCC therapy. We established a GNMT promoter-driven luciferase reporter assay as a drug screening platform. Screening of 324 pure compounds and 480 crude extracts from Chinese medicinal herbs resulted in the identification of Paeonia lactiflora Pall (PL) extract and the active component 1,2,3,4,6-penta-O-galloyl-ß-d-glucopyranoside (PGG) as a GNMT inducer. Purified PL extract and PGG induced GNMT mRNA and protein expression in Huh7 human hepatoma cells and in xenograft tumors. PGG and PL extract had potent anti-HCC effects both in vitro and in vivo. Furthermore, PGG treatment induced apoptosis in Huh7 cells. Moreover, PGG treatment sensitized Huh7 cells to sorafenib treatment. Therefore, these results indicated that identifying a GNMT enhancer using the GNMT promoter-based assay might be a useful approach to find drugs for HCC. These data also suggested that PGG has therapeutic potential for the treatment of HCC.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (1,2,3,4,6-penta-O-galloylglucopyranoside); 0 (Antineoplastic Agents); 0 (Glucosides); 0 (Plant Extracts); EC 2.1.1.20 (Glycine N-Methyltransferase)



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