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Pesquisa : D12.776.157.530.100.228.250 [Categoria DeCS]
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[PMID]:28982861
[Au] Autor:Bobin-Dubigeon C; Chauvin A; Brillaud-Meflah V; Boiffard F; Joalland MP; Bard JM
[Ad] Endereço:Department of Biopathology, Institute of Cancer and Oncology, Saint-Herblain, France.
[Ti] Título:Liver X Receptor (LXR)-regulated Genes of Cholesterol Trafficking and Breast Cancer Severity.
[So] Source:Anticancer Res;37(10):5495-5498, 2017 10.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Liver X receptor [LXR; nuclear receptor subfamily 1, group H, member 2 (NR1H2, alias LXRB)] can inhibit proliferation and induce apoptosis of cancer cells. Its relationship with disease severity is not known. MATERIALS AND METHODS: Expression of LXRB, ATP binding cassette subfamily A member 1 (ABCA1), ATP binding cassette subfamily G member 1 (ABCG1), apolipoprotein E (APOE) and paraoxonase 2 (PON2) were determined in 69 breast tumors and were related to clinical stages of the disease and tumor characteristics, as well as time to recurrence. RESULTS: ABCG1 expression differed with the tumor Scarff Bloom and Richardson (SBR) status (p=0.02), with a lower expression in SBRIII than in SBRII and SBRI. ABCG1 expression was significantly higher in estrogen receptor-positive tumors (N=63) (p=0.02). APOE expression was significantly lower in progesterone receptor-positive tumors (N=55) (p=0.03). No relationship with time to recurrence was observed. CONCLUSION: Expression of some LXR-dependent genes is related to breast tumor characteristics, but not time to recurrence. This may be due to a lack of study power or too short a follow-up time.
[Mh] Termos MeSH primário: Neoplasias da Mama/genética
Colesterol/metabolismo
Receptores X do Fígado/genética
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/genética
Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Adulto
Idoso
Idoso de 80 Anos ou mais
Apolipoproteínas E/genética
Apolipoproteínas E/metabolismo
Arildialquilfosfatase/genética
Arildialquilfosfatase/metabolismo
Neoplasias da Mama/metabolismo
Neoplasias da Mama/patologia
Neoplasias da Mama/terapia
Intervalo Livre de Doença
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Estimativa de Kaplan-Meier
Receptores X do Fígado/metabolismo
Meia-Idade
Recidiva Local de Neoplasia
Estadiamento de Neoplasias
Estudos Retrospectivos
Fatores de Tempo
Resultado do Tratamento
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, human); 0 (ABCG1 protein, human); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (ApoE protein, human); 0 (Apolipoproteins E); 0 (Liver X Receptors); 0 (NR1H2 protein, human); 97C5T2UQ7J (Cholesterol); EC 3.1.8.1 (Aryldialkylphosphatase); EC 3.1.8.1 (PON2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE


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[PMID]:28807695
[Au] Autor:Monzel JV; Budde T; Meyer Zu Schwabedissen HE; Schwebe M; Bien-Möller S; Lütjohann D; Kroemer HK; Jedlitschky G; Grube M
[Ad] Endereço:Dept. of Pharmacology at the Center of Drug Absorption and Transport (C_DAT), University Medicine, Greifswald, Germany.
[Ti] Título:Doxorubicin enhances oxysterol levels resulting in a LXR-mediated upregulation of cardiac cholesterol transporters.
[So] Source:Biochem Pharmacol;144:108-119, 2017 Nov 15.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The anthracycline-mediated cardiotoxicity is still not completely understood. To examine the impact of cholesterol metabolism and transport in this context, cholesterol and oxysterol levels as well as the expression of the cholesterol transporters ABCA1 and ABCG1 were analyzed in doxorubicin-treated HL-1 murine cardiomyocytes as well as in mouse model for acute doxorubicin-induced cardiotoxicity. Doxorubicin-treated HL-1 cells exhibited enhanced cholesterol (153±20% of control), oxysterol (24S-hydroxycholesterol: 206±29% of control) and cholesterol precursor levels (lathosterol: 122±12% of control; desmosterol: 188±10% of control) indicating enhanced cholesterol synthesis. Moreover, abca1 and abcg1 were upregulated on mRNA, protein and functional level caused by a doxorubicin-mediated activation of the nuclear receptor LXR. In addition, the oxysterols not only induced the abca1 and abcg1 in HL-1 cells but also enhanced the expression of endothelin-1 and transforming growth factor-ß, which have already been identified as important factors in doxorubicin-induced cardiotoxicity. These in vitro findings were verified in a murine model for acute doxorubicin-induced cardiotoxicity, demonstrating elevated cardiac (2.1±0.2vs. 3.6±1.0ng/mg) and systemic cholesterol levels (105.0±8.4vs. 130.0±4.3mg/dl), respectively, as well as enhanced oxysterol levels such as cardiac 24S-hydroxycholesterol (2.1±0.2vs. 3.6±1.0ng/mg). In line with these findings cardiac mRNA expression of abca1 (303% of control) and abcg1 (161% of control) was induced. Taken together, our data demonstrate enhanced cholesterol and oxysterol levels by doxorubicin, resulting in a LXR-dependent upregulation of abca1 and abcg1. In this context, the cytotoxic effects of oxysterols and their impact on cardiac gene expression should be considered as an important factor in doxorubicin-induced cardiotoxicity.
[Mh] Termos MeSH primário: Transportador 1 de Cassete de Ligação de ATP/biossíntese
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/biossíntese
Doxorrubicina/farmacologia
Receptores X do Fígado/fisiologia
Miócitos Cardíacos/metabolismo
Oxisteróis/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Colesterol/metabolismo
Relação Dose-Resposta a Droga
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Miócitos Cardíacos/efeitos dos fármacos
Regulação para Cima/efeitos dos fármacos
Regulação para Cima/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ABCG1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Liver X Receptors); 0 (Oxysterols); 80168379AG (Doxorubicin); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170816
[St] Status:MEDLINE


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[PMID]:28587984
[Au] Autor:Li J; Yue M; Zhou D; Wang M; Zhang H
[Ad] Endereço:College of Pharmaceutical Sciences, Soochow University, Suzhou, China.
[Ti] Título:Abcb1a but not Abcg2 played a predominant role in limiting the brain distribution of Huperzine A in mice.
[So] Source:Food Chem Toxicol;107(Pt A):68-73, 2017 Sep.
[Is] ISSN:1873-6351
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Huperzine A has been used for improving symptoms of Alzheimer's disease. Its cholinergic side effect is thought to be an exaggerated pharmacological outcome linked to its high brain or CNS concentrations. Although Huperzine A is brain penetrable, its interaction with efflux transporters (ABCB1 and ABCG2) has not been fully investigated. The aim of the present study was to characterize roles of ABCB1 and ABCG2 in the transmembrane transport of Huperzine A and identify a rate limiting step in its brain distribution. Data obtained from stably transfected MDCK II cells showed that Huperzine A is a substrate of ABCB1 but not ABCG2. ABCB1 inhibitors significantly inhibited ABCB1 mediated efflux of Huperzine A. In Abcb1a mice, the brain to plasma concentration ratio of Huperzine A was significantly increased as compared to the wild type mice, while there were no obvious differences between the wild type and Abcg2 mice. Taken together, the present study demonstrated that ABCB1 but not ABCG2 played a predominant role in the efflux of Huperzine A across BBB. The current finding is clinically relevant as changes in ABCB1 activity in the presence of ABCB1 inhibitors or genetic polymorphism may affect efficacy and safety of Huperzine A.
[Mh] Termos MeSH primário: Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Membro 2 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Alcaloides/farmacocinética
Encéfalo/metabolismo
Sesquiterpenos/farmacocinética
[Mh] Termos MeSH secundário: Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 2 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Animais
Transporte Biológico
Encéfalo/efeitos dos fármacos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCG1 protein, mouse); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 2); 0 (Abcg2 protein, mouse); 0 (Alkaloids); 0 (Sesquiterpenes); 0111871I23 (huperzine A)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170608
[St] Status:MEDLINE


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[PMID]:28549616
[Au] Autor:Zhu RG; Sun YD; Hou YT; Fan JG; Chen G; Li TP
[Ad] Endereço:Department of Food Science, College of Light Industry, Liaoning University, Liaoning Engineering Research Center for Food Bioprocessing, Shenyang Key Laboratory of Food Bioprocessing and Quality Control, Shenyang 110036, China. Electronic address: zhurugang@lnu.edu.cn.
[Ti] Título:Pectin penta-oligogalacturonide reduces cholesterol accumulation by promoting bile acid biosynthesis and excretion in high-cholesterol-fed mice.
[So] Source:Chem Biol Interact;272:153-159, 2017 Jun 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Haw pectin penta-oligogalacturonide (HPPS) has important role in improving cholesterol metabolism and promoting the conversion of cholesterol to bile acids (BA) in mice fed high-cholesterol diet (HCD). However, the mechanism is not clear. This study aims to investigate the effects of HPPS on cholesterol accumulation and the regulation of hepatic BA synthesis and transport in HCD-fed mice. Results showed that HPPS significantly decreased plasma and hepatic TC levels but increased plasma high-density lipoprotein cholesterol (HDL-C) and apolipoprotein A-I (apoA-I) levels, compared to HCD. BA analysis showed that HPPS markedly decreased hepatic and small intestine BA levels but increased the gallbladder BA levels, and finally decreased the total BA pool size, compared to HCD. Studies of molecular mechanism revealed that HPPS promoted hepatic ATP-binding cassette transporter A1 (ABCA1), ATP-binding cassette transporter G1 (ABCG1), and scavenger receptor BI (SR-BI) expression but did not affect ATB binding cassette transporter G5/G8 (ABCG5/8) expression. HPPS inactivated hepatic farnesoid X receptor (FXR) and target genes expression, which resulted in significant increase of cholesterol 7α-hydroxylase 1 (CYP7A1) and sterol 12α-hydroxylase (CYP8B1) expression, with up-regulations of 204.2% and 33.5% for mRNA levels, respectively, compared with HCD. In addition, HPPS markedly enhanced bile salt export pump (BSEP) expression but didn't affect the sodium/taurocholate co-transporting polypeptide (NTCP) expression. In conclusion, the study revealed that HPPS reduced cholesterol accumulation by promoting BA synthesis in the liver and excretion in the feces, and might promote macrophage-to-liver reverse cholesterol transport (RCT) but did not liver-to-fecal RCT.
[Mh] Termos MeSH primário: Ácidos e Sais Biliares/metabolismo
Colesterol/sangue
Expressão Gênica/efeitos dos fármacos
Oligossacarídeos/farmacologia
Pectinas/farmacologia
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/genética
Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Animais
Apolipoproteína A-I/sangue
Colesterol 7-alfa-Hidroxilase/genética
Colesterol 7-alfa-Hidroxilase/metabolismo
HDL-Colesterol/sangue
Dieta Hiperlipídica
Intestino Delgado/efeitos dos fármacos
Intestino Delgado/metabolismo
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Camundongos
Pectinas/química
Receptores Depuradores Classe B/genética
Receptores Depuradores Classe B/metabolismo
Esteroide 12-alfa-Hidroxilase/genética
Esteroide 12-alfa-Hidroxilase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ABCG1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Apolipoprotein A-I); 0 (Bile Acids and Salts); 0 (Cholesterol, HDL); 0 (Oligosaccharides); 0 (Pectins); 0 (Scarb1 protein, mouse); 0 (Scavenger Receptors, Class B); 97C5T2UQ7J (Cholesterol); EC 1.14.14.23 (Cholesterol 7-alpha-Hydroxylase); EC 1.14.14.23 (Cyp7a1 protein, mouse); EC 1.14.18.8 (Steroid 12-alpha-Hydroxylase)
[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:170528
[St] Status:MEDLINE


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[PMID]:28315462
[Au] Autor:Kober AC; Manavalan APC; Tam-Amersdorfer C; Holmér A; Saeed A; Fanaee-Danesh E; Zandl M; Albrecher NM; Björkhem I; Kostner GM; Dahlbäck B; Panzenboeck U
[Ad] Endereço:Institute of Pathophysiology and Immunology, Medical University of Graz, Graz, Austria.
[Ti] Título:Implications of cerebrovascular ATP-binding cassette transporter G1 (ABCG1) and apolipoprotein M in cholesterol transport at the blood-brain barrier.
[So] Source:Biochim Biophys Acta;1862(6):573-588, 2017 06.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Impaired cholesterol/lipoprotein metabolism is linked to neurodegenerative diseases such as Alzheimer's disease (AD). Cerebral cholesterol homeostasis is maintained by the highly efficient blood-brain barrier (BBB) and flux of the oxysterols 24(S)-hydroxycholesterol and 27-hydroxycholesterol, potent liver-X-receptor (LXR) activators. HDL and their apolipoproteins are crucial for cerebral lipid transfer, and loss of ATP binding cassette transporters (ABC)G1 and G4 results in toxic accumulation of oxysterols in the brain. The HDL-associated apolipoprotein (apo)M is positively correlated with pre-ß HDL formation in plasma; its presence and function in the brain was thus far unknown. Using an in vitro model of the BBB, we examined expression, regulation, and functions of ABCG1, ABCG4, and apoM in primary porcine brain capillary endothelial cells (pBCEC). RT Q-PCR analyses and immunoblotting revealed that in addition to ABCA1 and scavenger receptor, class B, type I (SR-BI), pBCEC express high levels of ABCG1, which was up-regulated by LXR activation. Immunofluorescent staining, site-specific biotinylation and immunoprecipitation revealed that ABCG1 is localized both to early and late endosomes and on apical and basolateral plasma membranes. Using siRNA interference to silence ABCG1 (by 50%) reduced HDL-mediated [ H]-cholesterol efflux (by 50%) but did not reduce [ H]-24(S)-hydroxycholesterol efflux. In addition to apoA-I, pBCEC express and secrete apoM mainly to the basolateral (brain) compartment. HDL enhanced expression and secretion of apoM by pBCEC, apoM-enriched HDL promoted cellular cholesterol efflux more efficiently than apoM-free HDL, while apoM-silencing diminished cellular cholesterol release. We suggest that ABCG1 and apoM are centrally involved in regulation of cholesterol metabolism/turnover at the BBB.
[Mh] Termos MeSH primário: Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Apolipoproteínas/metabolismo
Barreira Hematoencefálica/metabolismo
Membrana Celular/metabolismo
Colesterol/metabolismo
Modelos Biológicos
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Animais
Apolipoproteínas/genética
Transporte Biológico Ativo/fisiologia
Membrana Celular/genética
Colesterol/genética
Receptores X do Fígado/genética
Receptores X do Fígado/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Apolipoproteins); 0 (Liver X Receptors); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE


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[PMID]:28315324
[Au] Autor:Li Y; Jiang B; Liang P; Tong Z; Liu M; Lv Q; Liu Y; Liu X; Tang Y; Xiao X
[Ad] Endereço:Department of Pathophysiology, Xiangya School of Medicine, Central South University, Changsha, Hunan 410008, PR China.
[Ti] Título:Nucleolin protects macrophages from oxLDL-induced foam cell formation through up-regulating ABCA1 expression.
[So] Source:Biochem Biophys Res Commun;486(2):364-371, 2017 Apr 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Our recent studies have indicated that nucleolin, as a multifunctional RNA-binding protein, exerts protective effects in the myocardial cells and endothelial cells under the condition of oxidative stress. However, the function of nucleolin and its potential mechanism in macrophage-derived foam cell formation remain largely unexplored. ApoE-/- mice were fed with a high-fat diet (HFD) for 10-24 weeks. Protein expression was measured by western blotting or immunofluorescence, and gene expression at the mRNA level was detected by qRT-PCR. The level of lipid in macrophages was examined by Oil Red O staining, high-performance liquid chromatography (HPLC) and NBD-cholesterol. Actinomycin D (Act D) was used to determine the stability of ABCA1 mRNA in macrophages. The interaction of nucleolin with ABCA1 mRNA was assessed using co-immunoprecipitation (co-IP). The aortas advanced plaques demonstrated significantly lower levels of nucleolin protein compared with early plaques in ApoE-/- mice, in which the macrophage foam cells occupied main body. Nucleolin expression at the mRNA and protein levels in RAW264.7 macrophages was significantly reduced by oxidized low-density lipoprotein (oxLDL) in a dose- and time-dependent manner. Furthermore, nucleolin overexpression markedly attenuated lipid accumulation in oxLDL-challenged macrophages through increasing cholesterol efflux. In addition, nucleolin overexpression significantly increased the expression of ATP-binding cassette transporter A1 (ABCA1) at the mRNA and protein levels without affecting expressions of scavenger receptors (SR)-A, SR-B1, CD36 and ATP-binding cassette transporter G1 (ABCG1) at the mRNA level. Moreover, nucleolin overexpression increased the stability of ABCA1 mRNA in macrophages, whereas nucleolin ablation abrogated the oxLDL-induced up-regulation of ABCA1. The up-regulation of ABCA1 by nucleolin resulted from its protein-RNA interaction. Our data suggested that nucleolin inhibited foam cell formation through enhancing stability of ABCA1 mRNA and subsequently increasing cholesterol efflux.
[Mh] Termos MeSH primário: Transportador 1 de Cassete de Ligação de ATP/genética
Aterosclerose/genética
Hiperlipidemias/genética
Lipoproteínas LDL/farmacologia
Fosfoproteínas/genética
RNA Mensageiro/genética
Proteínas de Ligação a RNA/genética
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Animais
Apolipoproteínas E/deficiência
Apolipoproteínas E/genética
Aterosclerose/etiologia
Aterosclerose/metabolismo
Aterosclerose/patologia
Transporte Biológico/efeitos dos fármacos
Antígenos CD36/genética
Antígenos CD36/metabolismo
Diferenciação Celular
Linhagem Celular
Colesterol/metabolismo
Dieta Hiperlipídica
Relação Dose-Resposta a Droga
Células Espumosas/efeitos dos fármacos
Células Espumosas/metabolismo
Células Espumosas/patologia
Regulação da Expressão Gênica
Hiperlipidemias/etiologia
Hiperlipidemias/metabolismo
Hiperlipidemias/patologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Macrófagos/patologia
Masculino
Camundongos
Camundongos Knockout
Fosfoproteínas/metabolismo
Estabilidade de RNA
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/metabolismo
Receptores Depuradores Classe A/genética
Receptores Depuradores Classe A/metabolismo
Receptores Depuradores Classe B/genética
Receptores Depuradores Classe B/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ABCG1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Apolipoproteins E); 0 (CD36 Antigens); 0 (Lipoproteins, LDL); 0 (Phosphoproteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 0 (Scarb1 protein, mouse); 0 (Scavenger Receptors, Class A); 0 (Scavenger Receptors, Class B); 0 (nucleolin); 0 (oxidized low density lipoprotein); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170319
[St] Status:MEDLINE


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[PMID]:28296196
[Au] Autor:He J; Zhang G; Pang Q; Yu C; Xiong J; Zhu J; Chen F
[Ad] Endereço:Department of Endocrinology, Shanghai Ninth People's Hospital, Shanghai Jiao Tong University School of Medicine, China.
[Ti] Título:SIRT6 reduces macrophage foam cell formation by inducing autophagy and cholesterol efflux under ox-LDL condition.
[So] Source:FEBS J;284(9):1324-1337, 2017 May.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SIRT6 is a pivotal regulator of lipid metabolism. It is also closely connected to cardiovascular diseases, which are the main cause of death in diabetic patients. We observed a decrease in the expression of SIRT6 and key autophagy effectors (ATG5, LC3B, and LAMP1) in ox-LDL-induced foam cells, a special form of lipid-laden macrophages. In these cells, SIRT6 WT but not SIRT6 H133Y overexpression markedly reduced foam cell formation, as shown by Oil Red O staining, while inducing autophagy flux, as determined by both mRFP-GFP-LC3 labeling and transmission electron microscopy. Silencing the key autophagy initiation gene ATG5, reversed the autophagy-promoting effect of SIRT6 in ox-LDL-treated THP1 cells, as evidenced by an increase in foam cells. Cholesterol efflux assays indicated that SIRT6 overexpression in foam cells promoted cholesterol efflux, increased the levels of ABCA1 and ABCG1, and reduced miR-33 levels. By transfecting miR-33 into cells overexpressing SIRT6, we observed that reduced foam cell formation and autophagy flux induction were largely reversed. These data imply that SIRT6 plays an essential role in protecting against atherosclerosis by reducing foam cell formation through an autophagy-dependent pathway.
[Mh] Termos MeSH primário: Autofagia
Colesterol/metabolismo
Células Espumosas/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Lipoproteínas LDL/antagonistas & inibidores
Macrófagos/metabolismo
Sirtuínas/metabolismo
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/genética
Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Substituição de Aminoácidos
Proteína 5 Relacionada à Autofagia/antagonistas & inibidores
Proteína 5 Relacionada à Autofagia/genética
Proteína 5 Relacionada à Autofagia/metabolismo
Linhagem Celular Tumoral
Células Espumosas/citologia
Células Espumosas/imunologia
Células Espumosas/ultraestrutura
Seres Humanos
Lipoproteínas LDL/efeitos adversos
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Glicoproteínas de Membrana Associadas ao Lisossomo/genética
Glicoproteínas de Membrana Associadas ao Lisossomo/metabolismo
Macrófagos/citologia
Macrófagos/imunologia
Macrófagos/ultraestrutura
MicroRNAs/metabolismo
Microscopia Eletrônica de Transmissão
Proteínas Associadas aos Microtúbulos/genética
Proteínas Associadas aos Microtúbulos/metabolismo
Mutação
Interferência de RNA
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Sirtuínas/antagonistas & inibidores
Sirtuínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, human); 0 (ABCG1 protein, human); 0 (ATG5 protein, human); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Autophagy-Related Protein 5); 0 (LAMP1 protein, human); 0 (Lipoproteins, LDL); 0 (Luminescent Proteins); 0 (Lysosome-Associated Membrane Glycoproteins); 0 (MAP1LC3B protein, human); 0 (MIRN33 microRNA, human); 0 (MicroRNAs); 0 (Microtubule-Associated Proteins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (oxidized low density lipoprotein); 97C5T2UQ7J (Cholesterol); EC 3.5.1.- (SIRT6 protein, human); EC 3.5.1.- (Sirtuins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170316
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14055


  8 / 532 MEDLINE  
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[PMID]:28253220
[Au] Autor:Mo C; Yang M; Han X; Li J; Gao G; Tai H; Huang N; Xiao H
[Ad] Endereço:aLab for Aging Research, The Center of Gerontology and Geriatrics, State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan UniversitybDepartment of Immunology, School of Basic Medical Sciences, Chengdu Medical College, Chengdu, ChinacDepartment of Molecular Genetics and Microbiology, Gene Therapy Center, University of Massachusetts School of Medicine, Worcester, Massachusetts, USA.
[Ti] Título:Fat mass and obesity-associated protein attenuates lipid accumulation in macrophage foam cells and alleviates atherosclerosis in apolipoprotein E-deficient mice.
[So] Source:J Hypertens;35(4):810-821, 2017 Apr.
[Is] ISSN:1473-5598
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Genome-wide association studies have linked variants of fat mass and obesity-associated protein (FTO) to obesity. However, the molecular function of FTO remains unclear. In this study, we sought to investigate the potential effects of FTO in modulating cholesterol deposition in macrophage foam cells, as well as whether FTO exerts antiatherosclerotic properties in apolipoprotein E-deficient mice. METHOD AND RESULTS: We transfected RAW264.7 cells with plasmids encoding a wild-type or mutant FTO gene (I367F). The upregulation of FTO markedly attenuated cholesterol ester accumulation in macrophages loaded with oxidized LDL, whereas the downregulation of FTO reversed this effect. Moreover, FTO attenuated the mRNA and protein expression of a scavenger receptor, CD36, which was accompanied by the decline of peroxisome proliferator-activated receptor γ protein. In addition, FTO enhanced the phosphorylation of AMP-activated protein kinase (AMPK)α and acetyl-CoA carboxylase, which was effectively suppressed by FTO small interfering RNA. Pretreatment with compound C or transfection with a dominant-negative AMPKα blocked the FTO-mediated upregulation of ATP-binding cassette transporter A1 and ATP-binding cassette transporter G1. Furthermore, FTO suppressed IL-1ß secretion independent of the activation of the nucleotide-binding oligomerization domain-like receptor family pyrin domain containing 3 inflammasome. In-vivo experiments were performed using apolipoprotein E-deficient mice that were infected with adeno-associated virus serotype 9-derived vectors encoding a wild-type or mutant FTO gene. FTO overexpression prevented the formation of atherosclerotic plaques and markedly reduced the content of plasma total cholesterol and LDL cholesterol. Notably, the antiatherosclerotic properties of FTO were observed only in male mice. CONCLUSION: We propose that the FTO-dependent control of cholesterol deposition may provide avenues for the treatment of atherosclerosis.
[Mh] Termos MeSH primário: Dioxigenase FTO Dependente de alfa-Cetoglutarato/metabolismo
Apolipoproteínas E/deficiência
Colesterol/metabolismo
Células Espumosas/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/genética
Proteínas Quinases Ativadas por AMP/metabolismo
Transportador 1 de Cassete de Ligação de ATP
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Transportadores de Cassetes de Ligação de ATP
Acetil-CoA Carboxilase/metabolismo
Dioxigenase FTO Dependente de alfa-Cetoglutarato/genética
Animais
Apolipoproteínas E/genética
Antígenos CD36/genética
Antígenos CD36/metabolismo
Colesterol/sangue
Inflamassomos/metabolismo
Interleucina-1beta/metabolismo
Lipoproteínas LDL/metabolismo
Masculino
Camundongos
Obesidade/metabolismo
PPAR gama
Fosforilação
Placa Aterosclerótica/prevenção & controle
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/metabolismo
Transfecção
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Apolipoproteins E); 0 (CD36 Antigens); 0 (Inflammasomes); 0 (Interleukin-1beta); 0 (Lipoproteins, LDL); 0 (PPAR gamma); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (oxidized low density lipoprotein); 97C5T2UQ7J (Cholesterol); EC 1.14.11.33 (Alpha-Ketoglutarate-Dependent Dioxygenase FTO); EC 2.7.11.31 (AMP-Activated Protein Kinases); EC 6.4.1.2 (Acetyl-CoA Carboxylase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE
[do] DOI:10.1097/HJH.0000000000001255


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[PMID]:28232480
[Au] Autor:Pulakazhi Venu VK; Adijiang A; Seibert T; Chen YX; Shi C; Batulan Z; O'Brien ER
[Ad] Endereço:Department of Cardiac Sciences, Libin Cardiovascular Institute of Alberta, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
[Ti] Título:Heat shock protein 27-derived atheroprotection involves reverse cholesterol transport that is dependent on GM-CSF to maintain ABCA1 and ABCG1 expression in ApoE mice.
[So] Source:FASEB J;31(6):2364-2379, 2017 Jun.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recently, we demonstrated that heat shock protein (HSP)-27 is protective against the development of experimental atherosclerosis, reducing plaque cholesterol content by more than 30%. Moreover, elevated HSP-27 levels are predictive of relative freedom from clinical cardiovascular events. HSP-27 signaling occurs the activation of NF-κB, which induces a marked up-regulation in expression of granulocyte-monocyte colony-stimulating factor (GM-CSF), a cytokine that is known to alter ABC transporters involved in reverse cholesterol transport (RCT). Therefore, we hypothesized that HSP-27-derived GM-CSF has a potent role in impeding plaque formation by promoting macrophage RCT and sought to better characterize this pathway. Treatment of THP-1 cells, RAW-Blue cells, and primary macrophages with recombinant HSP-27 resulted in NF-κB activation TLR-4 and was inhibited by various pharmacologic blockers of this pathway. Moreover, HSP-27-induced upregulation of GM-CSF expression was dependent on TLR-4 signaling. Recombinant (r)HSP-27 treatment of ApoE female (but not male) mice for 4 wk yielded reductions in plaque area and cholesterol clefts of 33 and 47%, respectively, with no effect on GM-CSF ApoE mice. With 12 wk of rHSP-27 treatment, both female and male mice showed reductions in plaque burden (55 and 42%, respectively) and a 60% reduction in necrotic core area but no treatment effect in GM-CSF ApoE mice. functional studies revealed that HSP-27 enhanced the expression of ABCA1 and ABCG1, as well as facilitated cholesterol efflux by ∼10%. These novel findings establish a paradigm for HSP-27-mediated RCT and set the stage for the development of HSP-27 atheroprotective therapeutics.-Pulakazhi Venu, V. K., Adijiang, A., Seibert, T., Chen, Y.-X., Shi, C., Batulan, Z., O'Brien, E. R. Heat shock protein 27-derived atheroprotection involves reverse cholesterol transport that is dependent on GM-CSF to maintain ABCA1 and ABCG1 expression in ApoE mice.
[Mh] Termos MeSH primário: Transportador 1 de Cassete de Ligação de ATP/metabolismo
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Apolipoproteínas E/metabolismo
Aterosclerose/prevenção & controle
Colesterol/metabolismo
Proteínas de Choque Térmico HSP27/metabolismo
[Mh] Termos MeSH secundário: Transportador 1 de Cassete de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Animais
Apolipoproteínas E/genética
Linhagem Celular
Regulação da Expressão Gênica/fisiologia
Fator Estimulador de Colônias de Granulócitos e Macrófagos/genética
Fator Estimulador de Colônias de Granulócitos e Macrófagos/metabolismo
Proteínas de Choque Térmico HSP27/genética
Seres Humanos
Macrófagos
Camundongos
Camundongos Knockout
NF-kappa B/genética
NF-kappa B/metabolismo
Receptor 4 Toll-Like/genética
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ABCG1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Apolipoproteins E); 0 (HSP27 Heat-Shock Proteins); 0 (NF-kappa B); 0 (Toll-Like Receptor 4); 83869-56-1 (Granulocyte-Macrophage Colony-Stimulating Factor); 97C5T2UQ7J (Cholesterol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601188R


  10 / 532 MEDLINE  
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[PMID]:28199412
[Au] Autor:Zhang R; Dong S; Ma WW; Cai XP; Le ZY; Xiao R; Zhou Q; Yu HL
[Ad] Endereço:School of Public Health, Beijing Key Laboratory of Environmental Toxicology, Capital Medical University, Beijing, People's Republic of China.
[Ti] Título:Modulation of cholesterol transport by maternal hypercholesterolemia in human full-term placenta.
[So] Source:PLoS One;12(2):e0171934, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The significance of maternal cholesterol transporting to the fetus under normal as well as pathological circumstances is less understood. The objective of this study was to observe the effects of maternal hypercholesterolemia on placental cholesterol transportation. Human full-time placenta, maternal and venous cord blood were sampled at delivery from the pregnant women with serum total cholesterol (TC) concentrations at third trimester higher than 7.25 mM (n = 19) and the pregnant women with normal TC concentrations (n = 19). Serum lipids and expression of genes related to cholesterol transportation were measured by western blot or real-time PCR. The results indicated that serum TC, high density lipoprotein cholesterol (HDL-C), and low density lipoprotein cholesterol (LDL-C) levels were significantly increased, in pregnancies, but decreased in cord blood in hypercholesterolemic group compared to the matched control group. All the subjects were no-drinking, non-smoker, and gestational disease free. The mRNA expression of lipoprotein receptors, including LDLR and VLDLR were significantly increased, while the protein expression of PCSK9 was significantly increased in hypercholesterolemic placenta. In conclusion, maternal hypercholesterolemia might decrease the transportation of cholesterol from mother to fetus because of the high levels of PCSK9 protein expression.
[Mh] Termos MeSH primário: Colesterol/sangue
Hipercolesterolemia/patologia
Placenta/metabolismo
[Mh] Termos MeSH secundário: Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/genética
Membro 1 da Subfamília G de Transportadores de Cassetes de Ligação de ATP/metabolismo
Adulto
Estudos de Casos e Controles
HDL-Colesterol/sangue
LDL-Colesterol/sangue
Feminino
Sangue Fetal/metabolismo
Seres Humanos
Hipercolesterolemia/metabolismo
Receptores X do Fígado/genética
Receptores X do Fígado/metabolismo
Gravidez
Terceiro Trimestre da Gravidez
Pró-Proteína Convertase 9/metabolismo
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Receptores de Lipoproteínas/genética
Receptores de Lipoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCG1 protein, human); 0 (ATP Binding Cassette Transporter, Sub-Family G, Member 1); 0 (Cholesterol, HDL); 0 (Cholesterol, LDL); 0 (Liver X Receptors); 0 (RNA, Messenger); 0 (Receptors, Lipoprotein); 97C5T2UQ7J (Cholesterol); EC 3.4.21.- (PCSK9 protein, human); EC 3.4.21.- (Proprotein Convertase 9)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0171934



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