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  1 / 1990 MEDLINE  
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[PMID]:28471688
[Au] Autor:Dobiásová M
[Ad] Endereço:Institute of Physiology of the Czech Academy of Sciences, Prague, Czech Republic. milada.dobiasova@fgu.cas.cz.
[Ti] Título:Atherogenic impact of lecithin-cholesterol acyltransferase and its relation to cholesterol esterification rate in HDL (FER(HDL)) and AIP [log(TG/HDL-C)] biomarkers: the butterfly effect?
[So] Source:Physiol Res;66(2):193-203, 2017 May 04.
[Is] ISSN:1802-9973
[Cp] País de publicação:Czech Republic
[La] Idioma:eng
[Ab] Resumo:The atherogenic impact and functional capacity of LCAT was studied and discussed over a half century. This review aims to clarify the key points that may affect the final decision on whether LCAT is an anti-atherogenic or atherogenic factor. There are three main processes involving the efflux of free cholesterol from peripheral cells, LCAT action in intravascular pool where cholesterol esterification rate is under the control of HDL, LDL and VLDL subpopulations, and finally the destination of newly produced cholesteryl esters either to the catabolism in liver or to a futile cycle with apoB lipoproteins. The functionality of LCAT substantially depends on its mass together with the composition of the phospholipid bilayer as well as the saturation and the length of fatty acyls and other effectors about which we know yet nothing. Over the years, LCAT puzzle has been significantly supplemented but yet not so satisfactory as to enable how to manipulate LCAT in order to prevent cardiometabolic events. It reminds the butterfly effect when only a moderate change in the process of transformation free cholesterol to cholesteryl esters may cause a crucial turn in the intended target. On the other hand, two biomarkers - FER(HDL) (fractional esterification rate in HDL) and AIP [log(TG/HDL-C)] can offer a benefit to identify the risk of cardiovascular disease (CVD). They both reflect the rate of cholesterol esterification by LCAT and the composition of lipoprotein subpopulations that controls this rate. In clinical practice, AIP can be calculated from the routine lipid profile with help of AIP calculator www.biomed.cas.cz/fgu/aip/calculator.php.
[Mh] Termos MeSH primário: Aterosclerose/metabolismo
Biomarcadores/metabolismo
Colesterol/metabolismo
Ácidos Graxos/metabolismo
Lipoproteínas HDL/metabolismo
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
[Mh] Termos MeSH secundário: Animais
Aterosclerose/sangue
Esterificação
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); 0 (Fatty Acids); 0 (Lipoproteins, HDL); 97C5T2UQ7J (Cholesterol); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE


  2 / 1990 MEDLINE  
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[PMID]:28746818
[Au] Autor:Khalil A; Kamtchueng Simo O; Ikhlef S; Berrougui H
[Ad] Endereço:a Research Centre on Aging, Sherbrooke, QC J1H 4C4, Canada.
[Ti] Título:The role of paraoxonase 1 in regulating high-density lipoprotein functionality during aging.
[So] Source:Can J Physiol Pharmacol;95(10):1254-1262, 2017 Oct.
[Is] ISSN:1205-7541
[Cp] País de publicação:Canada
[La] Idioma:eng
[Ab] Resumo:Pharmacological interventions to increase the concentration of high-density lipoprotein (HDL) have led to disappointing results and have contributed to the emergence of the concept of HDL functionality. The anti-atherogenic activity of HDLs can be explained by their functionality or quality. The capacity of HDLs to maintain cellular cholesterol homeostasis and to transport cholesterol from peripheral cells to the liver for elimination is one of their principal anti-atherogenic activities. However, HDLs possess several other attributes that contribute to their protective effect against cardiovascular diseases. HDL functionality is regulated by various proteins and lipids making up HDL particles. However, several studies investigated the role of paraoxonase 1 (PON1) and suggest a significant role of this protein in the regulation of the functionality of HDLs. Moreover, research on PON1 attracted much interest following several studies indicating that it is involved in cardiovascular protection. However, the mechanisms by which PON1 exerts these effects remain to be elucidated.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Arildialquilfosfatase/metabolismo
Doenças Cardiovasculares/prevenção & controle
HDL-Colesterol/metabolismo
[Mh] Termos MeSH secundário: Fatores Etários
Animais
Doenças Cardiovasculares/enzimologia
Doenças Cardiovasculares/etiologia
Proteínas de Transferência de Ésteres de Colesterol/metabolismo
Seres Humanos
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CETP protein, human); 0 (Cholesterol Ester Transfer Proteins); 0 (Cholesterol, HDL); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON1 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1139/cjpp-2017-0117


  3 / 1990 MEDLINE  
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[PMID]:28795592
[Au] Autor:Zaher NH; Rashed ER; El-Ghazaly MA
[Ad] Endereço:Department of Drug Radiation Research, National Center for Radiation Research & Technology, Technology (NCRRT), Egyptian Atomic Energy Authority (EAEA), PO box 29, Nasr City, Cairo, Egypt.
[Ti] Título:Semi-synthetic thymoquinone analogs: new prototypes as potential antihyperlipidemics in irradiated rats.
[So] Source:Future Med Chem;9(13):1483-1493, 2017 Sep.
[Is] ISSN:1756-8927
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:AIM: Thymoquinone (TQ), has been reported to possess strong antihyperlipidemic properties. However, a variety of serious side effects has been reported for TQ. The present study aimed to evaluate the potential antihyperlipidemic activity of newly synthesized TQ analogs. METHODS & RESULTS: first, novel TQ derivatives were studied against radiation-induced dyslipidemia in male rats. Second, the most promising sulfur derivatives (4-7), were further tested to elucidate their possible mechanism(s) of actions. Results showed that they possess Hydroxymethyl Glutaryl-Co A reductase inhibitory activity, as well as stimulatory effects on the activities of each of plasma Lecithin-Cholesterol Acyltransferase and lipoprotein lipase enzymes. CONCLUSION: TQ derivatives (4-7), could be considered as promising agents in pathologies implicating impaired lipid metabolism, preclinical evaluation is warranted. [Formula: see text].
[Mh] Termos MeSH primário: Benzoquinonas/química
Hidroximetilglutaril-CoA Redutases/metabolismo
Hipolipemiantes/síntese química
[Mh] Termos MeSH secundário: Animais
Benzoquinonas/metabolismo
Benzoquinonas/uso terapêutico
Dislipidemias/tratamento farmacológico
Dislipidemias/etiologia
Dislipidemias/veterinária
Raios gama
Hidroximetilglutaril-CoA Redutases/sangue
Hidroximetilglutaril-CoA Redutases/química
Hipolipemiantes/farmacologia
Hipolipemiantes/uso terapêutico
Metabolismo dos Lipídeos/efeitos dos fármacos
Lipídeos/sangue
Lipase Lipoproteica/antagonistas & inibidores
Lipase Lipoproteica/metabolismo
Fígado/efeitos dos fármacos
Fígado/enzimologia
Fígado/efeitos da radiação
Masculino
Fosfatidilcolina-Esterol O-Aciltransferase/antagonistas & inibidores
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
Ratos
Ratos Wistar
Irradiação Corporal Total/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzoquinones); 0 (Hypolipidemic Agents); 0 (Lipids); 490-91-5 (thymoquinone); EC 1.1.1.- (Hydroxymethylglutaryl CoA Reductases); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.4155/fmc-2017-0054


  4 / 1990 MEDLINE  
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[PMID]:28664912
[Au] Autor:Russell MR; Graham C; D'Amato A; Gentry-Maharaj A; Ryan A; Kalsi JK; Ainley C; Whetton AD; Menon U; Jacobs I; Graham RLJ
[Ad] Endereço:Stoller Biomarker Discovery Centre and Pathology Node, Division of Molecular and Clinical Cancer Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Oxford Road Manchester, Manchester, UK.
[Ti] Título:A combined biomarker panel shows improved sensitivity for the early detection of ovarian cancer allowing the identification of the most aggressive type II tumours.
[So] Source:Br J Cancer;117(5):666-674, 2017 Aug 22.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: There is an urgent need for biomarkers for the early detection of ovarian cancer (OC). The purpose of this study was to assess whether changes in serum levels of lecithin-cholesterol acyltransferase (LCAT), sex hormone-binding globulin (SHBG), glucose-regulated protein, 78 kDa (GRP78), calprotectin and insulin-like growth factor-binding protein 2 (IGFBP2) are observed before clinical presentation and to assess the performance of these markers alone and in combination with CA125 for early detection. METHODS: This nested case-control study used samples from the United Kingdom Collaborative Trial of Ovarian Cancer Screening trial. The sample set consisted of 482 serum samples from 49 OC subjects and 31 controls, with serial samples spanning up to 7 years pre-diagnosis. The set was divided into the following: (I) a discovery set, which included all women with only two samples from each woman, the first at<14 months and the second at >32 months to diagnosis; and (ii) a corroboration set, which included all the serial samples from the same women spanning the 7-year period. Lecithin-cholesterol acyltransferase, SHBG, GRP78, calprotectin and IGFBP2 were measured using ELISA. The performance of the markers to detect cancers pre-diagnosis was assessed. RESULTS: A combined threshold model IGFBP2 >78.5 ng ml : LCAT <8.831 µg ml : CA125 >35 U ml outperformed CA125 alone for the earlier detection of OC. The threshold model was able to identify the most aggressive Type II cancers. In addition, it increased the lead time by 5-6 months and identified 26% of Type I subjects and 13% of Type II subjects that were not identified by CA125 alone. CONCLUSIONS: Combined biomarker panels (IGFBP2, LCAT and CA125) outperformed CA125 up to 3 years pre-diagnosis, identifying cancers missed by CA125, providing increased diagnostic lead times for Type I and Type II OC. The model identified more aggressive Type II cancers, with women crossing the threshold dying earlier, indicating that these markers can improve on the sensitivity of CA125 alone for the early detection of OC.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/sangue
Antígeno Ca-125/sangue
Detecção Precoce de Câncer/métodos
Proteína 2 de Ligação a Fator de Crescimento Semelhante à Insulina/sangue
Neoplasias Ovarianas/sangue
Neoplasias Ovarianas/diagnóstico
Fosfatidilcolina-Esterol O-Aciltransferase/sangue
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
Feminino
Proteínas de Choque Térmico/sangue
Seres Humanos
Complexo Antígeno L1 Leucocitário/sangue
Neoplasias Ovarianas/patologia
Globulina de Ligação a Hormônio Sexual/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CA-125 Antigen); 0 (Heat-Shock Proteins); 0 (Insulin-Like Growth Factor Binding Protein 2); 0 (Leukocyte L1 Antigen Complex); 0 (Sex Hormone-Binding Globulin); 0 (molecular chaperone GRP78); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.199


  5 / 1990 MEDLINE  
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[PMID]:28576974
[Au] Autor:Freeman LA; Demosky SJ; Konaklieva M; Kuskovsky R; Aponte A; Ossoli AF; Gordon SM; Koby RF; Manthei KA; Shen M; Vaisman BL; Shamburek RD; Jadhav A; Calabresi L; Gucek M; Tesmer JJG; Levine RL; Remaley AT
[Ad] Endereço:Lipid Metabolism Section, Cardiovascular and Pulmonary Branch (L.A.F., S.J.D., S.M.G., B.L.V., R.D.S., A.T.R.), Systems Biology Center (A.A., M.G.), and Laboratory of Biochemistry (R.L.L.), National Institutes of Health National Heart, Lung, and Blood Institute, Bethesda, Maryland; Department of Che
[Ti] Título:Lecithin:Cholesterol Acyltransferase Activation by Sulfhydryl-Reactive Small Molecules: Role of Cysteine-31.
[So] Source:J Pharmacol Exp Ther;362(2):306-318, 2017 Aug.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lecithin:cholesterol acyltransferase (LCAT) catalyzes plasma cholesteryl ester formation and is defective in familial lecithin:cholesterol acyltransferase deficiency (FLD), an autosomal recessive disorder characterized by low high-density lipoprotein, anemia, and renal disease. This study aimed to investigate the mechanism by which compound A [3-(5-(ethylthio)-1,3,4-thiadiazol-2-ylthio)pyrazine-2-carbonitrile], a small heterocyclic amine, activates LCAT. The effect of compound A on LCAT was tested in human plasma and with recombinant LCAT. Mass spectrometry and nuclear magnetic resonance were used to determine compound A adduct formation with LCAT. Molecular modeling was performed to gain insight into the effects of compound A on LCAT structure and activity. Compound A increased LCAT activity in a subset (three of nine) of LCAT mutations to levels comparable to FLD heterozygotes. The site-directed mutation LCAT-Cys31Gly prevented activation by compound A. Substitution of Cys31 with charged residues (Glu, Arg, and Lys) decreased LCAT activity, whereas bulky hydrophobic groups (Trp, Leu, Phe, and Met) increased activity up to 3-fold ( < 0.005). Mass spectrometry of a tryptic digestion of LCAT incubated with compound A revealed a +103.017 adduct on Cys31, consistent with the addition of a single hydrophobic cyanopyrazine ring. Molecular modeling identified potential interactions of compound A near Cys31 and structural changes correlating with enhanced activity. Functional groups important for LCAT activation by compound A were identified by testing compound A derivatives. Finally, sulfhydryl-reactive -lactams were developed as a new class of LCAT activators. In conclusion, compound A activates LCAT, including some FLD mutations, by forming a hydrophobic adduct with Cys31, thus providing a mechanistic rationale for the design of future LCAT activators.
[Mh] Termos MeSH primário: Cisteína/fisiologia
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
Compostos de Sulfidrila/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Ativação Enzimática/efeitos dos fármacos
Ativação Enzimática/fisiologia
Ativadores de Enzimas/química
Ativadores de Enzimas/metabolismo
Ativadores de Enzimas/farmacologia
Células HEK293
Seres Humanos
Deficiência da Lecitina Colesterol Aciltransferase/metabolismo
Modelos Moleculares
Fosfatidilcolina-Esterol O-Aciltransferase/química
Compostos de Sulfidrila/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Activators); 0 (Sulfhydryl Compounds); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170604
[St] Status:MEDLINE
[do] DOI:10.1124/jpet.117.240457


  6 / 1990 MEDLINE  
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[PMID]:28442378
[Au] Autor:Mani V; Arivalagan S; Islam Siddique A; Namasivayam N
[Ad] Endereço:Department of Biochemistry and Biotechnology, Faculty of Science, Annamalai University, Annamalainagar 608 002, Tamilnadu, India.
[Ti] Título:Antihyperlipidemic and antiapoptotic potential of zingerone on alcohol induced hepatotoxicity in experimental rats.
[So] Source:Chem Biol Interact;272:197-206, 2017 Jun 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The ultimate aim of this present study was to investigate the antihyperlipidemic and antiapoptotic potential of zingerone (ZO) on alcohol induced hepatotoxicity in experimental rats. Male albino wistar rats were divided in four groups. Groups 1 and 2 rats received isocaloric glucose and dimethyl sulphoxide (2% DMSO), liver toxicity was induced in groups 3 and 4 by supplementing 30% ethanol post orally for 60 days. In addition to, groups 2 and 4 received zingerone (20 mg/kg body weight in 2% DMSO) daily during the final 30 days of the experimental period. Ethanol alone administered rats showed increased levels/activities of plasma total cholesterol (TC), triglycerides (TG), free fatty acids (FFA), phospholipids (PL), low density lipoproteins (LDL), very low density lipoproteins (VLDL), tissue TC, TG, FFA, PL, HMG-CoA reductase, phase I xenobiotic enzymes, collagen and fat accumulation, DNA damage and increased Bax, caspase-3 and caspase-9 expressions and decrease in the levels/activities of plasma high density lipoproteins (HDL), lipoprotein lipase (LPL), lecithin cholesterol acyl transferase (LCAT), phase II xenobiotic enzymes and a decreased Bcl-2 expression. Zingerone supplementation was able to counter and reverse the ethanol induced changes in all the above parameters in experimental rats. Together results portray zingerone exhibits antihyperlipidemic and antiapoptotic potential on alcohol induced hepatotoxicity.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Etanol/toxicidade
Guaiacol/análogos & derivados
Fígado/efeitos dos fármacos
[Mh] Termos MeSH secundário: Acil Coenzima A/metabolismo
Animais
Caspase 3/metabolismo
Caspase 9/metabolismo
Dano ao DNA/efeitos dos fármacos
Modelos Animais de Doenças
Regulação para Baixo/efeitos dos fármacos
Ácidos Graxos não Esterificados/metabolismo
Guaiacol/farmacologia
Lipoproteínas HDL/sangue
Lipoproteínas LDL/sangue
Fígado/metabolismo
Fígado/patologia
Hepatopatias Alcoólicas/etiologia
Hepatopatias Alcoólicas/metabolismo
Masculino
Fosfatidilcolina-Esterol O-Aciltransferase/sangue
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Ratos
Ratos Wistar
Proteína X Associada a bcl-2/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Fatty Acids, Nonesterified); 0 (Lipoproteins, HDL); 0 (Lipoproteins, LDL); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (bcl-2-Associated X Protein); 1553-55-5 (3-hydroxy-3-methylglutaryl-coenzyme A); 3K9958V90M (Ethanol); 4MMW850892 (zingerone); 6JKA7MAH9C (Guaiacol); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 9)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE


  7 / 1990 MEDLINE  
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[PMID]:28391892
[Au] Autor:Nagao Y; Hirayama S; Kon M; Sasamoto K; Sugihara M; Hirayama A; Isshiki M; Seino U; Miyazaki O; Miida T
[Ad] Endereço:Department of Clinical Laboratory Medicine, Graduate School of Medicine, Juntendo University, Bunkyo-ku, Tokyo, Japan.
[Ti] Título:Current smokers with hyperlipidemia lack elevated preß1-high-density lipoprotein concentrations.
[So] Source:J Clin Lipidol;11(1):242-249, 2017 Jan - Feb.
[Is] ISSN:1933-2874
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Preß1-high-density lipoprotein (HDL) is an efficient acceptor of cell-derived free cholesterol, which is converted into lipid-rich HDL by lecithin-cholesterol acyltransferase. Previous studies have shown that preß1-HDL is significantly higher in individuals with hyperlipidemia. Preß1-HDL concentrations may be altered in smokers, who are at high risk for atherosclerosis. OBJECTIVE: The aim of the present study was to investigate the effect of smoking on preß1-HDL concentrations. METHODS: We measured the preß1-HDL concentration and lecithin-cholesterol acyltransferase-dependent conversion rate (CHT ) in 74 men (39 nonsmokers and 35 smokers) using an immunoassay. RESULTS: The smoker and nonsmoker groups were further divided into normolipidemic and hyperlipidemic subjects. Among nonsmokers, the mean preß1-HDL concentration was 27% higher in hyperlipidemics than in normolipidemics (25.5 ± 6.7 vs 20.3 ± 4.6 mg/L apoAI, P < .01). In contrast, mean preß1-HDL concentrations did not differ between hyperlipidemic and normolipidemic smokers (19.9 ± 3.1 vs 22.4 ± 6.9 mg/L apoAI). We found a positive correlation between preß1-HDL concentration and CHT in nonsmokers, but not in smokers. Smoking a single cigarette did not change preß1-HDL concentrations or CHT . Compared with nonsmokers, preß1-HDL concentrations were relatively low in hyperlipidemic smokers but not in normolipidemic smokers, and CHT was not a significant determinant of preß1-HDL concentrations in smokers. CONCLUSION: Our findings suggest that smoking may be disadvantageous to individuals with hyperlipidemia because preß1-HDL metabolism is altered.
[Mh] Termos MeSH primário: Hiperlipidemias/sangue
Lipoproteínas HDL/sangue
Fumar/efeitos adversos
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Hiperlipidemias/enzimologia
Hiperlipidemias/etiologia
Lipoproteínas HDL/química
Masculino
Meia-Idade
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
Risco
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipoproteins, HDL); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171023
[Lr] Data última revisão:
171023
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  8 / 1990 MEDLINE  
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[PMID]:27581838
[Au] Autor:Dullaart RP; Garcia E; Jeyarajah E; Gruppen EG; Connelly MA
[Ad] Endereço:Department of Endocrinology, University Medical Center Groningen, University of Groningen, P.O. Box 30.001, Groningen, 9700 RB, The Netherlands. r.p.f.dullaart@umcg.nl.
[Ti] Título:Plasma phospholipid transfer protein activity is inversely associated with betaine in diabetic and non-diabetic subjects.
[So] Source:Lipids Health Dis;15(1):143, 2016 Aug 31.
[Is] ISSN:1476-511X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The choline metabolite, betaine, plays a role in lipid metabolism, and may predict the development of cardiovascular disease and type 2 diabetes mellitus (T2DM). Phospholipid transfer protein (PLTP) and lecithin:cholesterol acyltransferase (LCAT) require phosphatidylcholine as substrate, raising the possibility that there is an intricate relationship of these protein factors with choline metabolism. Here we determined the relationships of PLTP and LCAT activity with betaine in subjects with and without T2DM. METHODS: Plasma betaine (nuclear magnetic resonance spectroscopy), PLTP activity (liposome-vesicle HDL system), LCAT activity (exogenous substrate assay) and (apo)lipoproteins were measured in 65 type 2 diabetic (T2DM) and in 55 non-diabetic subjects. RESULTS: PLTP and LCAT activity were elevated in T2DM (p < 0.05), whereas the difference in betaine was not significant. In age-, sex- and diabetes status-controlled correlation analysis, betaine was inversely correlated with triglycerides and positively with HDL cholesterol (p < 0.05 to 0.01). PLTP and LCAT activity were positively correlated with triglycerides and inversely with HDL cholesterol (p < 0.05 to 0.001). PLTP (r = -0.245, p = 0.006) and LCAT activity (r = -0.195, p = 0.035) were correlated inversely with betaine. The inverse association of PLTP activity with betaine remained significant after additional adjustment for body mass index and lipoprotein variables (ß = -0.179, p = 0.034), whereas its association with LCAT activity lost significance (ß = -0.056, p = 0.44). CONCLUSIONS: Betaine may influence lipoprotein metabolism via an effect on PLTP activity.
[Mh] Termos MeSH primário: Betaína/sangue
Diabetes Mellitus Tipo 2/sangue
Proteínas de Transferência de Fosfolipídeos/sangue
[Mh] Termos MeSH secundário: Fatores Etários
Idoso
Glicemia/análise
HDL-Colesterol/sangue
Feminino
Seres Humanos
Masculino
Meia-Idade
Fosfatidilcolina-Esterol O-Aciltransferase/sangue
Triglicerídeos/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Cholesterol, HDL); 0 (Phospholipid Transfer Proteins); 0 (Triglycerides); 3SCV180C9W (Betaine); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170327
[Lr] Data última revisão:
170327
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160902
[St] Status:MEDLINE
[do] DOI:10.1186/s12944-016-0313-5


  9 / 1990 MEDLINE  
              first record previous record next record last record
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[PMID]:27379467
[Au] Autor:Bekhet OH; Zeljkovic A; Vekic J; Paripovic D; Janac J; Joksic J; Gojkovic T; Spasojevic-Kalimanovska V; Peco-Antic A; Milosevski-Lomic G; Jelic-Ivanovic Z
[Ad] Endereço:a Department of Medical Biochemistry, Faculty of Pharmacy , University of Belgrade , Belgrade , Serbia ;
[Ti] Título:Hypertension, lipoprotein subclasses and lipid transfer proteins in obese children and adolescents.
[So] Source:Scand J Clin Lab Invest;76(6):472-8, 2016 Oct.
[Is] ISSN:1502-7686
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Obesity-related childhood hypertension is associated with disturbances of serum lipids, but less is known about distribution of lipoprotein subclasses and activities of proteins involved in reverse cholesterol transport in hypertensive obese children. Our objective was to determine low-density lipoprotein (LDL) and high-density lipoprotein (HDL) subclasses distribution and activities of lecithin:cholesterol acyltransferase (LCAT) and cholesteryl ester transfer protein (CETP) in hypertensive and non-hypertensive obese children. METHODS: A total of 40 hypertensive and 25 non-hypertensive obese children were enrolled. Lipoprotein subclasses were assessed by polyacrylamide gradient gel electrophoresis. LCAT and CETP activities were determined as a rate of formation and a rate of transfer of cholesteryl esters. RESULTS: Despite of comparable values of serum lipid parameters, a shift toward smaller LDL and HDL subclasses was observed in hypertensive compared to normotensive obese children. Activities of LCAT were similar, but proatherogenic CETP activities were significantly higher in the hypertensive group (p = 0.036). LCAT/net CETP ratio inversely correlated with relative proportion of small, dense LDL particles (ρ = -0.423; p = 0.025) in the group with hypertension. CONCLUSIONS: The results of our study demonstrated a tendency toward altered distribution of lipoprotein subclasses in favor of more proatherogenic particles in childhood hypertension. Also, hypertensive obese children had increased proatherogenic CETP activity.
[Mh] Termos MeSH primário: Hipertensão/sangue
Obesidade Pediátrica/sangue
[Mh] Termos MeSH secundário: Adolescente
Biomarcadores/sangue
Criança
Proteínas de Transferência de Ésteres de Colesterol/sangue
Feminino
Seres Humanos
Hipertensão/diagnóstico
Lipoproteínas HDL/sangue
Lipoproteínas LDL/sangue
Masculino
Obesidade Pediátrica/diagnóstico
Fosfatidilcolina-Esterol O-Aciltransferase/sangue
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (CETP protein, human); 0 (Cholesterol Ester Transfer Proteins); 0 (Lipoproteins, HDL); 0 (Lipoproteins, LDL); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160706
[St] Status:MEDLINE
[do] DOI:10.1080/00365513.2016.1201849


  10 / 1990 MEDLINE  
              first record previous record
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Fotocópia
[PMID]:27354333
[Au] Autor:Soupene E; Borja MS; Borda M; Larkin SK; Kuypers FA
[Ad] Endereço:Children's Hospital Oakland Research Institute, Oakland, California 94609, USA esoupene@chori.org.
[Ti] Título:Featured Article: Alterations of lecithin cholesterol acyltransferase activity and apolipoprotein A-I functionality in human sickle blood.
[So] Source:Exp Biol Med (Maywood);241(17):1933-1942, 2016 Nov.
[Is] ISSN:1535-3699
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In sickle cell disease (SCD) cholesterol metabolism appears dysfunctional as evidenced by abnormal plasma cholesterol content in a subpopulation of SCD patients. Specific activity of the high density lipoprotein (HDL)-bound lecithin cholesterol acyltransferase (LCAT) enzyme, which catalyzes esterification of cholesterol, and generates lysoPC (LPC) was significantly lower in sickle plasma compared to normal. Inhibitory amounts of LPC were present in sickle plasma, and the red blood cell (RBC) lysophosphatidylcholine acyltransferase (LPCAT), essential for the removal of LPC, displayed a broad range of activity. The functionality of sickle HDL appeared to be altered as evidenced by a decreased HDL-Apolipoprotein A-I exchange in sickle plasma as compared to control. Increased levels of oxidized proteins including ApoA-I were detected in sickle plasma. In vitro incubation of sickle plasma with washed erythrocytes affected the ApoA-I-exchange supporting the view that the RBC blood compartment can affect cholesterol metabolism in plasma. HDL functionality appeared to decrease during acute vaso-occlusive episodes in sickle patients and was associated with an increase of secretory PLA , a marker for increased inflammation. Simvastatin treatment to improve the anti-inflammatory function of HDL did not ameliorate HDL-ApoA-I exchange in sickle patients. Thus, the cumulative effect of an inflammatory and highly oxidative environment in sickle blood contributes to a decrease in cholesterol esterification and HDL function, related to hypocholesterolemia in SCD.
[Mh] Termos MeSH primário: Anemia Falciforme/sangue
Anemia Falciforme/enzimologia
Apolipoproteína A-I/fisiologia
Fosfatidilcolina-Esterol O-Aciltransferase/metabolismo
[Mh] Termos MeSH secundário: Adulto
Anemia Falciforme/metabolismo
Anemia Falciforme/fisiopatologia
Biomarcadores/sangue
Estudos de Casos e Controles
Eritrócitos/química
Hemoglobina Fetal/análise
Seres Humanos
Fosfatidilcolina-Esterol O-Aciltransferase/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoprotein A-I); 0 (Biomarkers); 9034-63-3 (Fetal Hemoglobin); EC 2.3.1.43 (Phosphatidylcholine-Sterol O-Acyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170608
[Lr] Data última revisão:
170608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160630
[St] Status:MEDLINE



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