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Pesquisa : D08.811.913.696.900.200 [Categoria DeCS]
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[PMID]:28314772
[Au] Autor:Kong P; Ufermann CM; Zimmermann DLM; Yin Q; Suo X; Helms JB; Brouwers JF; Gupta N
[Ad] Endereço:From the Department of Molecular Parasitology, Humboldt University, Berlin 10115, Germany.
[Ti] Título:Two phylogenetically and compartmentally distinct CDP-diacylglycerol synthases cooperate for lipid biogenesis in .
[So] Source:J Biol Chem;292(17):7145-7159, 2017 Apr 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is among the most prevalent protozoan parasites, which infects a wide range of organisms, including one-third of the human population. Its rapid intracellular replication within a vacuole requires efficient synthesis of glycerophospholipids. Cytidine diphosphate-diacylglycerol (CDP-DAG) serves as a major precursor for phospholipid synthesis. Given the peculiarities of lipid biogenesis, understanding the mechanism and physiological importance of CDP-DAG synthesis is particularly relevant in Here, we report the occurrence of two phylogenetically divergent CDP-DAG synthase (CDS) enzymes in the parasite. The eukaryotic-type CDS1 and the prokaryotic-type CDS2 reside in the endoplasmic reticulum and apicoplast, respectively. Conditional knockdown of CDS1 severely attenuated the parasite growth and resulted in a nearly complete loss of virulence in a mouse model. Moreover, mice infected with the CDS1 mutant became fully resistant to challenge infection with a hyper-virulent strain of The residual growth of the CDS1 mutant was abolished by consecutive deletion of CDS2. Lipidomic analyses of the two mutants revealed significant and specific declines in phosphatidylinositol and phosphatidylglycerol levels upon repression of CDS1 and after deletion of CDS2, respectively. Our data suggest a "division of labor" model of lipid biogenesis in in which two discrete CDP-DAG pools produced in the endoplasmic reticulum and apicoplast are subsequently used for the synthesis of phosphatidylinositol in the Golgi bodies and phosphatidylglycerol in the mitochondria. The essential and divergent nature of CDP-DAG synthesis in the parasite apicoplast offers a potential drug target to inhibit the asexual reproduction of .
[Mh] Termos MeSH primário: Diacilglicerol Colinofosfotransferase/genética
Glicerofosfolipídeos/biossíntese
Proteínas de Protozoários/genética
Toxoplasma/enzimologia
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Apicoplastos/enzimologia
Diacilglicerol Colinofosfotransferase/metabolismo
Retículo Endoplasmático/metabolismo
Fibroblastos/metabolismo
Técnica Indireta de Fluorescência para Anticorpo
Deleção de Genes
Complexo de Golgi/metabolismo
Seres Humanos
Camundongos
Mitocôndrias/metabolismo
Mutação
Fosfatidilgliceróis/química
Fosfatidilinositóis/química
Filogenia
Domínios Proteicos
Proteínas de Protozoários/metabolismo
Toxoplasma/genética
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophospholipids); 0 (Phosphatidylglycerols); 0 (Phosphatidylinositols); 0 (Protozoan Proteins); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.765487


  2 / 431 MEDLINE  
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[PMID]:28009086
[Au] Autor:Vences-Guzmán MÁ; Paula Goetting-Minesky M; Guan Z; Castillo-Ramirez S; Córdoba-Castro LA; López-Lara IM; Geiger O; Sohlenkamp C; Christopher Fenno J
[Ad] Endereço:Centro de Ciencias Genómicas, Universidad Nacional Autónoma de México, Av. Universidad s/n, Apdo. Postal 565-A, Cuernavaca, Morelos, CP62210, Mexico.
[Ti] Título:1,2-Diacylglycerol choline phosphotransferase catalyzes the final step in the unique Treponema denticola phosphatidylcholine biosynthesis pathway.
[So] Source:Mol Microbiol;103(5):896-912, 2017 Mar.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Treponema denticola synthesizes phosphatidylcholine through a licCA-dependent CDP-choline pathway identified only in the genus Treponema. However, the mechanism of conversion of CDP-choline to phosphatidylcholine remained unclear. We report here characterization of TDE0021 (herein designated cpt) encoding a 1,2-diacylglycerol choline phosphotransferase homologous to choline phosphotransferases that catalyze the final step of the highly conserved Kennedy pathway for phosphatidylcholine synthesis in eukaryotes. T. denticola Cpt catalyzed in vitro phosphatidylcholine formation from CDP-choline and diacylglycerol, and full activity required divalent manganese. Allelic replacement mutagenesis of cpt in T. denticola resulted in abrogation of phosphatidylcholine synthesis. T. denticola Cpt complemented a Saccharomyces cerevisiae CPT1 mutant, and expression of the entire T. denticola LicCA-Cpt pathway in E. coli resulted in phosphatidylcholine biosynthesis. Our findings show that T. denticola possesses a unique phosphatidylcholine synthesis pathway combining conserved prokaryotic choline kinase and CTP:phosphocholine cytidylyltransferase activities with a 1,2-diacylglycerol choline phosphotransferase that is common in eukaryotes. Other than in a subset of mammalian host-associated Treponema that includes T. pallidum, this pathway is found in neither bacteria nor Archaea. Molecular dating analysis of the Cpt gene family suggests that a horizontal gene transfer event introduced this gene into an ancestral Treponema well after its divergence from other spirochetes.
[Mh] Termos MeSH primário: Vias Biossintéticas
Diacilglicerol Colinofosfotransferase/metabolismo
Fosfatidilcolinas/biossíntese
Treponema denticola/metabolismo
[Mh] Termos MeSH secundário: Alelos
Vias Biossintéticas/genética
Vias Biossintéticas/fisiologia
Catálise
Cinética
Manganês/metabolismo
Mutagênese
Alinhamento de Sequência
Treponema denticola/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phosphatidylcholines); 42Z2K6ZL8P (Manganese); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161224
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13596


  3 / 431 MEDLINE  
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[PMID]:27706605
[Au] Autor:Sousa CS; Barros BA; Barh D; Ghosh P; Azevedo V; Barros EG; Moreira MA
[Ad] Endereço:Departamento de Bioquímica e Biologia Molecular - BIOAGRO, Universidade Federal de Viçosa, Viçosa, MG, Brasil cassissousa@gmail.com.
[Ti] Título:In silico characterization of 1,2-diacylglycerol cholinephosphotransferase and lysophospha-tidylcholine acyltransferase genes in Glycine max L. Merrill.
[So] Source:Genet Mol Res;15(3), 2016 Aug 26.
[Is] ISSN:1676-5680
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The enzymes 1,2-diacylglycerol cholinephosphotrans-ferase (CPT) and lysophosphatidylcholine acyltransferase (LPCAT) are important in lipid metabolism in soybean seeds. Thus, understand-ing the genes that encode these enzymes may enable their modification and aid the improvement of soybean oil quality. In soybean, the genes encoding these enzymes have not been completely described; there-fore, this study aimed to identify, characterize, and analyze the in silico expression of these genes in soybean. We identified two gene models encoding CPT and two gene models encoding LPCAT, one of which presented an alternative transcript. The sequences were positioned on the physical map of soybean and the promoter regions were analyzed. Cis-elements responsible for seed-specific expression and responses to biotic and abiotic stresses were identified. Virtual expression analysis of the gene models for CPT and LPCAT indicated that these genes are expressed under different stress conditions, in somatic embryos during differentiation, in immature seeds, root tissues, and calli. Putative ami-no acid sequences revealed the presence of transmembrane domains, and analysis of the cellular localization of these enzymes revealed they are located in the endoplasmic reticulum.
[Mh] Termos MeSH primário: 1-Acilglicerofosfocolina O-Aciltransferase/genética
Diacilglicerol Colinofosfotransferase/genética
Retículo Endoplasmático/enzimologia
Proteínas de Plantas/genética
Feijão de Soja/genética
[Mh] Termos MeSH secundário: 1-Acilglicerofosfocolina O-Aciltransferase/química
1-Acilglicerofosfocolina O-Aciltransferase/metabolismo
Processamento Alternativo
Sequência de Aminoácidos
Simulação por Computador
Diacilglicerol Colinofosfotransferase/química
Diacilglicerol Colinofosfotransferase/metabolismo
Retículo Endoplasmático/química
Retículo Endoplasmático/ultraestrutura
Expressão Gênica
Metabolismo dos Lipídeos/genética
Modelos Genéticos
Mapeamento Físico do Cromossomo
Células Vegetais/enzimologia
Células Vegetais/ultraestrutura
Proteínas de Plantas/química
Proteínas de Plantas/metabolismo
Raízes de Plantas/citologia
Raízes de Plantas/enzimologia
Regiões Promotoras Genéticas
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Sementes/citologia
Sementes/enzimologia
Alinhamento de Sequência
Feijão de Soja/citologia
Feijão de Soja/enzimologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (RNA, Messenger); EC 2.3.1.23 (1-Acylglycerophosphocholine O-Acyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170224
[Lr] Data última revisão:
170224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE
[do] DOI:10.4238/gmr.15038974


  4 / 431 MEDLINE  
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[PMID]:27457520
[Au] Autor:Jia M; Andreassen T; Jensen L; Bathen TF; Sinha I; Gao H; Zhao C; Haldosen LA; Cao Y; Girnita L; Moestue SA; Dahlman-Wright K
[Ad] Endereço:Department of Biosciences and Nutrition, Novum, Karolinska Institutet, Huddinge, Sweden. min.jia@ki.se Karin.Dahlman-Wright@ki.se.
[Ti] Título:Estrogen Receptor α Promotes Breast Cancer by Reprogramming Choline Metabolism.
[So] Source:Cancer Res;76(19):5634-5646, 2016 Oct 01.
[Is] ISSN:1538-7445
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Estrogen receptor α (ERα) is a key regulator of breast growth and breast cancer development. Here, we report how ERα impacts these processes by reprogramming metabolism in malignant breast cells. We employed an integrated approach, combining genome-wide mapping of chromatin-bound ERα with estrogen-induced transcript and metabolic profiling, to demonstrate that ERα reprograms metabolism upon estrogen stimulation, including changes in aerobic glycolysis, nucleotide and amino acid synthesis, and choline (Cho) metabolism. Cho phosphotransferase CHPT1, identified as a direct ERα-regulated gene, was required for estrogen-induced effects on Cho metabolism, including increased phosphatidylcholine synthesis. CHPT1 silencing inhibited anchorage-independent growth and cell proliferation, also suppressing early-stage metastasis of tamoxifen-resistant breast cancer cells in a zebrafish xenograft model. Our results showed that ERα promotes metabolic alterations in breast cancer cells mediated by its target CHPT1, which this study implicates as a candidate therapeutic target. Cancer Res; 76(19); 5634-46. ©2016 AACR.
[Mh] Termos MeSH primário: Neoplasias da Mama/etiologia
Colina/metabolismo
Receptor alfa de Estrogênio/fisiologia
[Mh] Termos MeSH secundário: Animais
Neoplasias da Mama/tratamento farmacológico
Neoplasias da Mama/metabolismo
Colina-Fosfato Citidililtransferase/fisiologia
Diacilglicerol Colinofosfotransferase/fisiologia
Resistência a Medicamentos Antineoplásicos
Feminino
Seres Humanos
Células MCF-7
Metástase Neoplásica
Tamoxifeno/uso terapêutico
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Estrogen Receptor alpha); 0 (estrogen receptor alpha, human); 094ZI81Y45 (Tamoxifen); EC 2.7.7.15 (CTP phosphocholine cytidylyltransferase, alpha isoform, human); EC 2.7.7.15 (Choline-Phosphate Cytidylyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase); N91BDP6H0X (Choline)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE


  5 / 431 MEDLINE  
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[PMID]:27404583
[Au] Autor:Gavriljuk K; Schartner J; Seidel H; Dickhut C; Zahedi RP; Hedberg C; Kötting C; Gerwert K
[Ad] Endereço:Department of Biophysics, Ruhr-Universität Bochum , Universitätsstrasse 150, 44801 Bochum, Germany.
[Ti] Título:Unraveling the Phosphocholination Mechanism of the Legionella pneumophila Enzyme AnkX.
[So] Source:Biochemistry;55(31):4375-85, 2016 Aug 09.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intracellular pathogen Legionella pneumophila infects lung macrophages and injects numerous effector proteins into the host cell to establish a vacuole for proliferation. The necessary interference with vesicular trafficking of the host is achieved by modulation of the function of Rab GTPases. The effector protein AnkX chemically modifies Rab1b and Rab35 by covalent phosphocholination of serine or threonine residues using CDP-choline as a donor. So far, the phosphoryl transfer mechanism and the relevance of observed autophosphocholination of AnkX remained disputable. We designed tailored caged compounds to make this type of enzymatic reaction accessible for time-resolved Fourier transform infrared difference spectroscopy. By combining spectroscopic and biochemical methods, we determined that full length AnkX is autophosphocholinated at Ser521, Thr620, and Thr943. However, autophosphocholination loses specificity for these sites in shortened constructs and does not appear to be relevant for the catalysis of the phosphoryl transfer. In contrast, transient phosphocholination of His229 in the conserved catalytic motif might exist as a short-lived reaction intermediate. Upon substrate binding, His229 is deprotonated and locked in this state, being rendered capable of a nucleophilic attack on the pyrophosphate moiety of the substrate. The proton that originated from His229 is transferred to a nearby carboxylic acid residue. Thus, our combined findings support a ping-pong mechanism involving phosphocholination of His229 and subsequent transfer of phosphocholine to the Rab GTPase. Our approach can be extended to the investigation of further nucleotidyl transfer reactions, which are currently of reemerging interest in regulatory pathways of host-pathogen interactions.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Proteínas de Bactérias/metabolismo
Diacilglicerol Colinofosfotransferase/química
Diacilglicerol Colinofosfotransferase/metabolismo
Legionella pneumophila/enzimologia
[Mh] Termos MeSH secundário: Repetição de Anquirina
Proteínas de Bactérias/genética
Biocatálise
Domínio Catalítico
Diacilglicerol Colinofosfotransferase/genética
Interações Hospedeiro-Patógeno
Seres Humanos
Legionella pneumophila/genética
Legionella pneumophila/patogenicidade
Modelos Moleculares
Fosforilcolina/metabolismo
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Espectroscopia de Infravermelho com Transformada de Fourier
Proteínas rab de Ligação ao GTP/metabolismo
Proteínas rab1 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Recombinant Proteins); 107-73-3 (Phosphorylcholine); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase); EC 3.6.1.- (RAB35 protein, human); EC 3.6.1.- (Rab1B protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab1 GTP-Binding Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160713
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00524


  6 / 431 MEDLINE  
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[PMID]:27073147
[Au] Autor:Arlauckas SP; Popov AV; Delikatny EJ
[Ad] Endereço:Department of Radiology, 317 Anatomy-Chemistry Building, 3620 Hamilton Walk, University of Pennsylvania, Philadelphia, PA 19104, USA.
[Ti] Título:Choline kinase alpha-Putting the ChoK-hold on tumor metabolism.
[So] Source:Prog Lipid Res;63:28-40, 2016 07.
[Is] ISSN:1873-2194
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:It is well established that lipid metabolism is drastically altered during tumor development and response to therapy. Choline kinase alpha (ChoKα) is a key mediator of these changes, as it represents the first committed step in the Kennedy pathway of phosphatidylcholine biosynthesis and ChoKα expression is upregulated in many human cancers. ChoKα activity is associated with drug resistant, metastatic, and malignant phenotypes, and represents a robust biomarker and therapeutic target in cancer. Effective ChoKα inhibitors have been developed and have recently entered clinical trials. ChoKα's clinical relevance was, until recently, attributed solely to its production of second messenger intermediates of phospholipid synthesis. The recent discovery of a non-catalytic scaffolding function of ChoKα may link growth receptor signaling to lipid biogenesis and requires a reinterpretation of the design and validation of ChoKα inhibitors. Advances in positron emission tomography, magnetic resonance spectroscopy, and optical imaging methods now allow for a comprehensive understanding of ChoKα expression and activity in vivo. We will review the current understanding of ChoKα metabolism, its role in tumor biology and the development and validation of targeted therapies and companion diagnostics for this important regulatory enzyme. This comes at a critical time as ChoKα-targeting programs receive more clinical interest.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Colina Quinase/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Neoplasias Encefálicas/diagnóstico por imagem
Neoplasias Encefálicas/tratamento farmacológico
Neoplasias Encefálicas/patologia
Colina Quinase/antagonistas & inibidores
Colina Quinase/genética
Diacilglicerol Colinofosfotransferase/metabolismo
Inibidores Enzimáticos/metabolismo
Inibidores Enzimáticos/uso terapêutico
Inibidores Enzimáticos/toxicidade
Hemicolínio 3/metabolismo
Hemicolínio 3/uso terapêutico
Hemicolínio 3/toxicidade
Seres Humanos
Espectroscopia de Ressonância Magnética
Tomografia por Emissão de Pósitrons
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; REVIEW
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 312-45-8 (Hemicholinium 3); EC 2.7.1.32 (Choline Kinase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170701
[Lr] Data última revisão:
170701
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160414
[St] Status:MEDLINE


  7 / 431 MEDLINE  
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[PMID]:26946540
[Au] Autor:Qi Y; Kapterian TS; Du X; Ma Q; Fei W; Zhang Y; Huang X; Dawes IW; Yang H
[Ad] Endereço:School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney 2052, Australia.
[Ti] Título:CDP-diacylglycerol synthases regulate the growth of lipid droplets and adipocyte development.
[So] Source:J Lipid Res;57(5):767-80, 2016 May.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The expansion of lipid droplets (LDs) and the differentiation of preadipocytes are two important aspects of mammalian lipid storage. In this study, we examined the role of CDP-diacylglycerol (DAG) synthases (CDSs), encoded by CDS1 and CDS2 genes in mammals, in lipid storage. CDS enzymes catalyze the formation of CDP-DAG from phosphatidic acid (PA). Knocking down either CDS1 or CDS2 resulted in the formation of giant or supersized LDs in cultured cells. Moreover, depleting CDS1 almost completely blocked the differentiation of 3T3-L1 preadipocytes, whereas depleting CDS2 had a moderate inhibitory effect on adipocyte differentiation. The levels of many PA species were significantly increased upon knocking down CDS1 In contrast, only a small number of PA species were increased upon depleting CDS2 Importantly, the amount of PA in the endoplasmic reticulum was dramatically increased upon knocking down CDS1 or CDS2 Our results suggest that the changes in PA level and localization may underlie the formation of giant LDs as well as the block in adipogenesis in CDS-deficient cells. We have therefore identified CDS1 and CDS2 as important novel regulators of lipid storage, and these results highlight the crucial role of phospholipids in mammalian lipid storage.
[Mh] Termos MeSH primário: Adipócitos/enzimologia
Diacilglicerol Colinofosfotransferase/fisiologia
Gotículas Lipídicas/enzimologia
[Mh] Termos MeSH secundário: Células 3T3-L1
Animais
Diferenciação Celular
Expressão Gênica
Células HeLa
Seres Humanos
Metabolismo dos Lipídeos
Camundongos
Fosfatidato Fosfatase/genética
Fosfatidato Fosfatase/metabolismo
Fosfolipídeos/metabolismo
Transporte Proteico
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phospholipids); 0 (Triglycerides); EC 2.7.8.2 (CDS1 protein, human); EC 2.7.8.2 (CDS2 protein, human); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase); EC 3.1.3.4 (LPIN1 protein, human); EC 3.1.3.4 (Phosphatidate Phosphatase)
[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:160307
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M060574


  8 / 431 MEDLINE  
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[PMID]:26791243
[Au] Autor:Laurinyecz B; Péter M; Vedelek V; Kovács AL; Juhász G; Maróy P; Vígh L; Balogh G; Sinka R
[Ad] Endereço:Department of Genetics, University of Szeged, Szeged, Hungary.
[Ti] Título:Reduced expression of CDP-DAG synthase changes lipid composition and leads to male sterility in Drosophila.
[So] Source:Open Biol;6(1):50169, 2016 Jan.
[Is] ISSN:2046-2441
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Drosophila spermatogenesis is an ideal system to study the effects of changes in lipid composition, because spermatid elongation and individualization requires extensive membrane biosynthesis and remodelling. The bulk of transcriptional activity is completed with the entry of cysts into meiotic division, which makes post-meiotic stages of spermatogenesis very sensitive to even a small reduction in gene products. In this study, we describe the effect of changes in lipid composition during spermatogenesis using a hypomorphic male sterile allele of the Drosophila CDP-DAG synthase (CdsA) gene. We find that the CdsA mutant shows defects in spermatid individualization and enlargement of mitochondria and the axonemal sheath of the spermatids. Furthermore, we could genetically rescue the male sterile phenotype by overexpressing Phosphatidylinositol synthase (dPIS) in a CdsA mutant background. The results of lipidomic and genetic analyses of the CdsA mutant highlight the importance of correct lipid composition during sperm development and show that phosphatidic acid levels are crucial in late stages of spermatogenesis.
[Mh] Termos MeSH primário: Proteínas de Drosophila/metabolismo
Drosophila melanogaster/enzimologia
Drosophila melanogaster/fisiologia
Infertilidade Masculina/enzimologia
Lipídeos/química
Nucleotidiltransferases/metabolismo
[Mh] Termos MeSH secundário: Alelos
Animais
Diacilglicerol Colinofosfotransferase
Genes de Insetos
Infertilidade Masculina/patologia
Lipídeos/biossíntese
Masculino
Mitocôndrias
Mutação/genética
Ácidos Fosfatídicos/metabolismo
Fosfatidilinositóis/metabolismo
Espermátides/metabolismo
Espermátides/ultraestrutura
Espermatogênese
Testículo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Lipids); 0 (Phosphatidic Acids); 0 (Phosphatidylinositols); EC 2.7.7.- (Nucleotidyltransferases); EC 2.7.8.2 (CdsA protein, Drosophila); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160122
[St] Status:MEDLINE


  9 / 431 MEDLINE  
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[PMID]:26358846
[Au] Autor:Vlachogianni IC; Fragopoulou E; Stamatakis GM; Kostakis IK; Antonopoulou S
[Ad] Endereço:Department of Nutritional Science and Dietetics, Harokopio University, Athens, Greece.
[Ti] Título:Platelet Activating Factor (PAF) biosynthesis is inhibited by phenolic compounds in U-937 cells under inflammatory conditions.
[So] Source:Prostaglandins Other Lipid Mediat;121(Pt B):176-83, 2015 Sep.
[Is] ISSN:1098-8823
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Interleukin 1 beta (IL-1ß) induced platelet activating factor (PAF) synthesis in U-937 cells through stimulation of acetyl-CoA:lysoPAF-acetyltransferase (lyso PAF-AT) at 3 h and DTT-independentCDP-choline-1-alkyl-2-acetyl-sn-glycerol cholinophosphotransferase (PAF-CPT) at 0.5 h. The aim of this study was to investigate the effect of tyrosol (T), resveratrol (R) and their acetylated derivatives(AcDs) which exhibit enhanced bioavailability, on PAF synthesis in U-937 after IL-1ß stimulation. The specific activity of PAF enzymes and intracellular levels were measured in cell homogenates. T and R concentration capable of inducing 50% inhibition in IL-1ß effect on lyso PAF-AT was 48 µΜ ± 11 and 157 µΜ ± 77, for PAF-CPT 246 µΜ ± 61 and 294 µΜ ± 102, respectively. The same order of concentration was also observed on inhibiting PAF levels produced by IL-1ß. T was more potent inhibitor than R (p<0.05). AcDs of T retain parent compound inhibitory activity, while in the case of R only two AcDs retain the activity. The observed inhibitory effect by T,R and their AcDs, may partly explain their already reported beneficial role.
[Mh] Termos MeSH primário: Anti-Inflamatórios não Esteroides/farmacologia
Antioxidantes/farmacologia
Regulação para Baixo/efeitos dos fármacos
Monócitos/efeitos dos fármacos
Álcool Feniletílico/análogos & derivados
Fator de Ativação de Plaquetas/antagonistas & inibidores
Estilbenos/farmacologia
[Mh] Termos MeSH secundário: 1-Alquil-2-acetilglicerofosfocolina Esterase/antagonistas & inibidores
1-Alquil-2-acetilglicerofosfocolina Esterase/química
1-Alquil-2-acetilglicerofosfocolina Esterase/metabolismo
Acetilação
Acetiltransferases/antagonistas & inibidores
Acetiltransferases/química
Acetiltransferases/metabolismo
Anti-Inflamatórios não Esteroides/síntese química
Anti-Inflamatórios não Esteroides/química
Antioxidantes/síntese química
Antioxidantes/química
Linhagem Celular
Diacilglicerol Colinofosfotransferase/antagonistas & inibidores
Diacilglicerol Colinofosfotransferase/química
Diacilglicerol Colinofosfotransferase/metabolismo
Ativação Enzimática/efeitos dos fármacos
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Inibidores Enzimáticos/farmacologia
Seres Humanos
Interleucina-1beta/antagonistas & inibidores
Interleucina-1beta/genética
Interleucina-1beta/metabolismo
Monócitos/imunologia
Monócitos/metabolismo
Concentração Osmolar
Álcool Feniletílico/farmacologia
Fator de Ativação de Plaquetas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Estilbenos/química
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents, Non-Steroidal); 0 (Antioxidants); 0 (Enzyme Inhibitors); 0 (IL1B protein, human); 0 (Interleukin-1beta); 0 (Platelet Activating Factor); 0 (Recombinant Proteins); 0 (Stilbenes); 1AK4MU3SNX (4-hydroxyphenylethanol); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.67 (1-alkylglycerophosphocholine acetyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase); EC 3.1.1.47 (1-Alkyl-2-acetylglycerophosphocholine Esterase); ML9LGA7468 (Phenylethyl Alcohol); Q369O8926L (resveratrol)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150912
[St] Status:MEDLINE


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[PMID]:24639073
[Au] Autor:Detopoulou P; Fragopoulou E; Nomikos T; Yannakoulia M; Stamatakis G; Panagiotakos DB; Antonopoulou S
[Ad] Endereço:Department of Nutrition-Dietetics, Harokopio University, 70 El. Venizelou Street, 17671, Athens, Greece.
[Ti] Título:The relation of diet with PAF and its metabolic enzymes in healthy volunteers.
[So] Source:Eur J Nutr;54(1):25-34, 2015 Feb.
[Is] ISSN:1436-6215
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Platelet-activating factor (PAF), a potent inflammatory mediator, is implicated in atherosclerosis. Its key biosynthetic enzymes are lyso-PAF acetyltransferases (lyso-PAF-AT), responsible for PAF synthesis through the remodeling route and a specific CDP-choline:1-alkyl-2-acetyl-sn-glycerol cholinephosphotransferase (PAF-CPT), responsible for its de novo biosynthesis. PAF acetylhydrolase (PAF-AH) and its extracellular isoform lipoprotein-associated phospholipase A2 catabolize PAF. The impact of diet on PAF metabolism is ill-defined. The aim was to investigate associations between PAF, its enzymes and dietary factors. METHODS: One-hundred and six (n = 106) healthy volunteers were recruited. Food-frequency questionnaires, dietary recalls, lifestyle and biochemical variables were collected. Food groups, macronutrient intake, a priori (MedDietScore) and a posteriori defined food patterns with PCA analysis, dietary antioxidant capacity (DAC), glycemic index (GI) and glycemic load were assessed. RESULTS: PAF was inversely correlated with antioxidant-rich foods (herbal drinks and coffee), the DAC as well as a dietary pattern characterized by legumes, vegetables, poultry and fish (all Ps < 0.05). PAF was positively correlated to % fat intake. Lyso-PAF-AT was also negatively associated with healthy patterns (fruits, nuts and herbal drinks, and a pattern rich in olive oil and whole-wheat products), as well as the DAC and % monounsaturated fatty acids. PAF-CPT was negatively associated with GI and coffee intake and positively with dietary cholesterol. PAF-AH was negatively associated with coffee and positively associated with alcohol consumption (all Ps < 0.05). CONCLUSIONS: In conclusion, the DAC and healthy dietary patterns were inversely associated with PAF or its biosynthetic enzymes, suggesting potential new mechanisms of the diet-disease associations.
[Mh] Termos MeSH primário: Acetiltransferases/sangue
Doenças Cardiovasculares/etiologia
Diacilglicerol Colinofosfotransferase/sangue
Dieta Hiperlipídica/efeitos adversos
Fator de Ativação de Plaquetas/análise
Regulação para Cima
[Mh] Termos MeSH secundário: 1-Alquil-2-acetilglicerofosfocolina Esterase/sangue
1-Alquil-2-acetilglicerofosfocolina Esterase/metabolismo
Acetiltransferases/metabolismo
Adulto
Consumo de Bebidas Alcoólicas/efeitos adversos
Antioxidantes/uso terapêutico
Doenças Cardiovasculares/epidemiologia
Doenças Cardiovasculares/metabolismo
Doenças Cardiovasculares/prevenção & controle
Estudos Transversais
Diacilglicerol Colinofosfotransferase/metabolismo
Carboidratos da Dieta/efeitos adversos
Feminino
Índice Glicêmico
Grécia/epidemiologia
Seres Humanos
Leucócitos/enzimologia
Leucócitos/imunologia
Masculino
Meia-Idade
Fator de Ativação de Plaquetas/metabolismo
Análise de Componente Principal
Risco
Caracteres Sexuais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antioxidants); 0 (Dietary Carbohydrates); 0 (Platelet Activating Factor); EC 2.3.1.- (Acetyltransferases); EC 2.3.1.67 (1-alkylglycerophosphocholine acetyltransferase); EC 2.7.8.2 (Diacylglycerol Cholinephosphotransferase); EC 3.1.1.47 (1-Alkyl-2-acetylglycerophosphocholine Esterase)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140319
[St] Status:MEDLINE
[do] DOI:10.1007/s00394-014-0682-3



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