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  1 / 1989 MEDLINE  
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[PMID]:28784927
[Au] Autor:Bacconi M; Haag AF; Chiarot E; Donato P; Bagnoli F; Delany I; Bensi G
[Ad] Endereço:GSK Vaccines Srl, Siena, Italy.
[Ti] Título: Analysis of Staphylococcus aureus-Infected Mice Reveals Differential Temporal and Spatial Expression Patterns of .
[So] Source:Infect Immun;85(10), 2017 Oct.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:is an opportunistic human pathogen and a major cause of invasive infections such as bacteremia, endocarditis, pneumonia, and wound infections. FhuD2 is a staphylococcal lipoprotein involved in the uptake of iron-hydroxymate and is under the control of the iron uptake regulator Fur. This protein is part of an investigational multicomponent vaccine formulation that has shown protective efficacy in several murine models of infection. Even though expression has been shown to be upregulated in murine kidneys infected with , it is not known whether the bacterium undergoes increased iron deprivation during prolonged infection. Furthermore, different infection niches might provide different environments and levels of iron availability, resulting in different expression patterns among organs of the same host. To address these questions, we characterized the expression of the gene and confirmed Fur-dependent regulation of its expression. We further investigated its expression in mice infected with a bioluminescent reporter strain of expressing the luciferase operon under the control of the promoter. The emission of bioluminescence in different organs was followed over a 7-day time course, and quantitative real-time PCR analysis of the RNA transcribed from the endogenous gene was performed. Using this approach, we were able to show that expression was induced during infection in all organs analyzed and that differences in expression were observed at different time points and in different infected organs. Our data suggest that undergoes increased iron deprivation during the progression of infection in diverse host organs and accordingly induces dedicated iron acquisition mechanisms. Since FhuD2 plays a central role in providing the pathogen with the required iron, further knowledge of the patterns of expression during infection will be instrumental in better defining the role of this antigen in pathogenesis and as a vaccine antigen.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Regulação Bacteriana da Expressão Gênica
Ferro/metabolismo
Receptores de Lipoproteínas/genética
Infecções Estafilocócicas/microbiologia
Staphylococcus aureus/genética
[Mh] Termos MeSH secundário: Animais
Antígenos de Bactérias/genética
Proteínas de Bactérias/metabolismo
Microscopia Intravital
Luciferases/genética
Medições Luminescentes
Camundongos
Óperon
Reação em Cadeia da Polimerase em Tempo Real
Receptores de Lipoproteínas/metabolismo
Staphylococcus aureus/metabolismo
Staphylococcus aureus/patogenicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Receptors, Lipoprotein); E1UOL152H7 (Iron); EC 1.13.12.- (Luciferases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170809
[St] Status:MEDLINE


  2 / 1989 MEDLINE  
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[PMID]:28767685
[Au] Autor:Takano K; Kakuki T; Kaneko Y; Kohno T; Kikuchi S; Himi T; Kojima T
[Ad] Endereço:Department of Otolaryngology, Sapporo Medical University School of Medicine, Sapporo, Japan.
[Ti] Título:Histone deacetylase inhibition prevents cell death induced by loss of tricellular tight junction proteins in temperature-sensitive mouse cochlear cells.
[So] Source:PLoS One;12(8):e0182291, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tricellular tight junctions (tTJs) are specialized structures that occur where the corners of three cells meet to seal adjacent intercellular space. The molecular components of tTJs include tricellulin (TRIC) and lipolysis-stimulated lipoprotein receptor (LSR) which recruits TRIC, are required for normal hearing. Although loss of TRIC causes hearing loss with degeneration of cochlear cells, the detailed mechanisms remains unclear. In the present study, by using temperature-sensitive mouse cochlear cells, US/VOT-E36 cell line, we investigated the changes of TRIC and LSR during cochlear cell differentiation and the effects of histone deacetylase (HDAC) inhibitors against cell degeneration induced by loss of TRIC and LSR. During cell differentiation induced by the temperature change, expression of TRIC and LSR were clearly induced. Treatment with metformin enhanced expression TRIC and LSR via AMPK during cell differentiation. Loss of TRIC and LSR by the siRNAs induced cell death in differentiated cells. Treatment with HDAC inhibitors trichostatin A and HDAC6 inhibitor prevented the cell death induced by loss of TRIC and LSR. Collectively, these findings suggest that both tTJ proteins TRIC and LSR have crucial roles for the differentiated cochlear cell survival, and that HDAC inhibitors may be potential therapeutic agents to prevent hearing loss.
[Mh] Termos MeSH primário: Células Ciliadas Auditivas/citologia
Inibidores de Histona Desacetilases/farmacologia
Proteína 2 com Domínio MARVEL/metabolismo
Metformina/farmacologia
Receptores de Lipoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Morte Celular/efeitos dos fármacos
Diferenciação Celular/efeitos dos fármacos
Linhagem Celular
Regulação da Expressão Gênica/efeitos dos fármacos
Células Ciliadas Auditivas/efeitos dos fármacos
Camundongos
Temperatura Ambiente
Proteínas de Junções Íntimas/metabolismo
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Histone Deacetylase Inhibitors); 0 (MARVEL Domain Containing 2 Protein); 0 (Marveld2 protein, mouse); 0 (Receptors, Lipoprotein); 0 (Tight Junction Proteins); 0 (angulin-1 protein, mouse); 9100L32L2N (Metformin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182291


  3 / 1989 MEDLINE  
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[PMID]:28402248
[Au] Autor:Beigneux AP; Miyashita K; Ploug M; Blom DJ; Ai M; Linton MF; Khovidhunkit W; Dufour R; Garg A; McMahon MA; Pullinger CR; Sandoval NP; Hu X; Allan CM; Larsson M; Machida T; Murakami M; Reue K; Tontonoz P; Goldberg IJ; Moulin P; Charrière S; Fong LG; Nakajima K; Young SG
[Ad] Endereço:From the Departments of Medicine (A.P.B., M.A.M., N.P.S., X.H., C.M.A., M.L., L.G.F., S.G.Y.), Rheumatology (M.A.M.), Human Genetics (K.R., S.G.Y.), and Pathology and Laboratory Medicine (P.T.), David Geffen School of Medicine, University of California, Los Angeles, Los Angeles, and the Cardiovascul
[Ti] Título:Autoantibodies against GPIHBP1 as a Cause of Hypertriglyceridemia.
[So] Source:N Engl J Med;376(17):1647-1658, 2017 04 27.
[Is] ISSN:1533-4406
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: A protein that is expressed on capillary endothelial cells, called GPIHBP1 (glycosylphosphatidylinositol-anchored high-density lipoprotein binding protein 1), binds lipoprotein lipase and shuttles it to its site of action in the capillary lumen. A deficiency in GPIHBP1 prevents lipoprotein lipase from reaching the capillary lumen. Patients with GPIHBP1 deficiency have low plasma levels of lipoprotein lipase, impaired intravascular hydrolysis of triglycerides, and severe hypertriglyceridemia (chylomicronemia). During the characterization of a monoclonal antibody-based immunoassay for GPIHBP1, we encountered two plasma samples (both from patients with chylomicronemia) that contained an interfering substance that made it impossible to measure GPIHBP1. That finding raised the possibility that those samples might contain GPIHBP1 autoantibodies. METHODS: Using a combination of immunoassays, Western blot analyses, and immunocytochemical studies, we tested the two plasma samples (as well as samples from other patients with chylomicronemia) for the presence of GPIHBP1 autoantibodies. We also tested the ability of GPIHBP1 autoantibodies to block the binding of lipoprotein lipase to GPIHBP1. RESULTS: We identified GPIHBP1 autoantibodies in six patients with chylomicronemia and found that these autoantibodies blocked the binding of lipoprotein lipase to GPIHBP1. As in patients with GPIHBP1 deficiency, those with GPIHBP1 autoantibodies had low plasma levels of lipoprotein lipase. Three of the six patients had systemic lupus erythematosus. One of these patients who had GPIHBP1 autoantibodies delivered a baby with plasma containing maternal GPIHBP1 autoantibodies; the infant had severe but transient chylomicronemia. Two of the patients with chylomicronemia and GPIHBP1 autoantibodies had a response to treatment with immunosuppressive agents. CONCLUSIONS: In six patients with chylomicronemia, GPIHBP1 autoantibodies blocked the ability of GPIHBP1 to bind and transport lipoprotein lipase, thereby interfering with lipoprotein lipase-mediated processing of triglyceride-rich lipoproteins and causing severe hypertriglyceridemia. (Funded by the National Heart, Lung, and Blood Institute and the Leducq Foundation.).
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Hiperlipoproteinemia Tipo I/imunologia
Lipase Lipoproteica/metabolismo
Receptores de Lipoproteínas/imunologia
[Mh] Termos MeSH secundário: Adulto
Autoanticorpos/fisiologia
Feminino
Seres Humanos
Hiperlipoproteinemia Tipo I/sangue
Imunoensaio
Lipólise
Lipase Lipoproteica/sangue
Masculino
Meia-Idade
Ligação Proteica
Transporte Proteico
Receptores de Lipoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (GPIHBP1 protein, human); 0 (Receptors, Lipoprotein); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170413
[St] Status:MEDLINE
[do] DOI:10.1056/NEJMoa1611930


  4 / 1989 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


  5 / 1989 MEDLINE  
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[PMID]:28115844
[Au] Autor:Rui M; Qu Y; Gao T; Ge Y; Feng C; Xu X
[Ad] Endereço:Department of Pharmaceutics, School of Pharmacy, Jiangsu University, Zhenjiang, People's Republic of China.
[Ti] Título:Simultaneous delivery of anti-miR21 with doxorubicin prodrug by mimetic lipoprotein nanoparticles for synergistic effect against drug resistance in cancer cells.
[So] Source:Int J Nanomedicine;12:217-237, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:The development of drug resistance in cancer cells is one of the major obstacles to achieving effective chemotherapy. We hypothesized that the combination of a doxorubicin (Dox) prodrug and microRNA (miR)21 inhibitor might show synergistic antitumor effects on drug-resistant breast cancer cells. In this study, we aimed to develop new high-density lipoprotein-mimicking nanoparticles (HMNs) for coencapsulation and codelivery of this potential combination. Dox was coupled with a nuclear localization signal (NLS) peptide to construct a prodrug (NLS-Dox), thereby electrostatically condensing miR21 inhibitor (anti-miR21) to form cationic complexes. The HMNs were formulated by shielding these complexes with anionic lipids and Apo AI proteins. We have characterized that the coloaded HMNs had uniformly dispersed distribution, favorable negatively charged surface, and high coencapsulation efficiency. The HMN formulation effectively codelivered NLS-Dox and anti-miR21 into Dox-resistant breast cancer MCF7/ADR cells and wild-type MCF7 cells via a high-density-lipoprotein receptor-mediated pathway, which facilitated the escape of Pgp drug efflux. The coloaded HMNs consisting of NLS-Dox/anti-miR21 demonstrated greater cytotoxicity with enhanced intracellular accumulation in resistant MCF7/ADR cells compared with free Dox solution. The reversal of drug resistance by coloaded HMNs might be attributed to the suppression of miR21 expression and the related antiapoptosis network. Furthermore, the codelivery of anti-miR21 and NLS-Dox by HMNs showed synergistic antiproliferative effects in MCF7/ADR-bearing nude mice, and was more effective in tumor inhibition than other drug formulations. These data suggested that codelivery of anti-miR21 and chemotherapeutic agents by HMNs might be a promising strategy for antitumor therapy, and could restore the drug sensitivity of cancer cells, alter intracellular drug distribution, and ultimately enhance chemotherapeutic effects.
[Mh] Termos MeSH primário: Doxorrubicina/administração & dosagem
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
MicroRNAs/antagonistas & inibidores
Nanopartículas/administração & dosagem
Pró-Fármacos/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/administração & dosagem
Antineoplásicos/química
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Doxorrubicina/farmacologia
Resistência a Medicamentos Antineoplásicos/genética
Feminino
Seres Humanos
Lipídeos/química
Lipoproteínas HDL/química
Lipoproteínas HDL/metabolismo
Células MCF-7/efeitos dos fármacos
Camundongos Nus
MicroRNAs/genética
Nanopartículas/química
Sinais de Localização Nuclear/química
Pró-Fármacos/farmacologia
Receptores de Lipoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Lipids); 0 (Lipoproteins, HDL); 0 (MIRN21 microRNA, human); 0 (MicroRNAs); 0 (Nuclear Localization Signals); 0 (Prodrugs); 0 (Receptors, Lipoprotein); 0 (high density lipoprotein receptors); 80168379AG (Doxorubicin)
[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:170125
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S122171


  6 / 1989 MEDLINE  
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[PMID]:27984852
[Au] Autor:Hayne CK; Lafferty MJ; Eglinger BJ; Kane JP; Neher SB
[Ad] Endereço:Department Biochemistry and Biophysics, University of North Carolina at Chapel Hill , 120 Mason Farm Road, CB7260, Chapel Hill, North Carolina 27599, United States.
[Ti] Título:Biochemical Analysis of the Lipoprotein Lipase Truncation Variant, LPL , Reveals Increased Lipoprotein Uptake.
[So] Source:Biochemistry;56(3):525-533, 2017 Jan 24.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lipoprotein lipase (LPL) is responsible for the hydrolysis of triglycerides from circulating lipoproteins. Whereas most identified mutations in the LPL gene are deleterious, one mutation, LPL , causes a gain of function. This mutation truncates two amino acids from LPL's C-terminus. Carriers of LPL have decreased VLDL levels and increased HDL levels, a cardioprotective phenotype. LPL is used in Alipogene tiparvovec, the gene therapy product for individuals with familial LPL deficiency. It is unclear why LPL results in a serum lipid profile more favorable than that of LPL. In vitro reports vary as to whether LPL is more active than LPL. We report a comprehensive, biochemical comparison of purified LPL and LPL dimers. We found no difference in specific activity on synthetic and natural substrates. We also did not observe a difference in the K for ANGPTL4 inhibition of LPL relative to that of LPL. Finally, we analyzed LPL-mediated uptake of fluorescently labeled lipoprotein particles and found that LPL enhanced lipoprotein uptake to a greater degree than LPL did. An LPL structural model suggests that the LPL truncation exposes residues implicated in LPL binding to uptake receptors.
[Mh] Termos MeSH primário: HDL-Colesterol/química
LDL-Colesterol/química
Lipase Lipoproteica/química
Mutação
Receptores de Lipoproteínas/química
Triglicerídeos/química
[Mh] Termos MeSH secundário: Proteína 4 Semelhante a Angiopoietina
Angiopoietinas/química
Angiopoietinas/genética
Angiopoietinas/metabolismo
Animais
Transporte Biológico
HDL-Colesterol/metabolismo
LDL-Colesterol/metabolismo
VLDL-Colesterol/química
VLDL-Colesterol/metabolismo
Expressão Gênica
Seres Humanos
Hiperlipidemias/sangue
Hiperlipidemias/genética
Hiperlipidemias/patologia
Lipase Lipoproteica/genética
Lipase Lipoproteica/metabolismo
Camundongos
Modelos Moleculares
Ligação Proteica
Domínios Proteicos
Multimerização Proteica
Estrutura Secundária de Proteína
Receptores de Lipoproteínas/genética
Receptores de Lipoproteínas/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Serina/química
Serina/metabolismo
Especificidade por Substrato
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ANGPTL4 protein, human); 0 (Angiopoietin-like 4 Protein); 0 (Angiopoietins); 0 (Cholesterol, HDL); 0 (Cholesterol, LDL); 0 (Cholesterol, VLDL); 0 (GPI-HBP1 protein, mouse); 0 (GPIHBP1 protein, human); 0 (Receptors, Lipoprotein); 0 (Recombinant Proteins); 0 (Triglycerides); 452VLY9402 (Serine); EC 3.1.1.34 (LPL protein, human); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.6b00945


  7 / 1989 MEDLINE  
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[PMID]:27875259
[Au] Autor:Hu X; Sleeman MW; Miyashita K; Linton MF; Allan CM; He C; Larsson M; Tu Y; Sandoval NP; Jung RS; Mapar A; Machida T; Murakami M; Nakajima K; Ploug M; Fong LG; Young SG; Beigneux AP
[Ad] Endereço:Departments of Medicine University of California Los Angeles, Los Angeles, CA.
[Ti] Título:Monoclonal antibodies that bind to the Ly6 domain of GPIHBP1 abolish the binding of LPL.
[So] Source:J Lipid Res;58(1):208-215, 2017 Jan.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:GPIHBP1, an endothelial cell protein, binds LPL in the interstitial spaces and shuttles it to its site of action inside blood vessels. For years, studies of human GPIHBP1 have been hampered by an absence of useful antibodies. We reasoned that monoclonal antibodies (mAbs) against human GPIHBP1 would be useful for 1) defining the functional relevance of GPIHBP1's Ly6 and acidic domains to the binding of LPL; 2) ascertaining whether human GPIHBP1 is expressed exclusively in capillary endothelial cells; and 3) testing whether GPIHBP1 is detectable in human plasma. Here, we report the development of a panel of human GPIHBP1-specific mAbs. Two mAbs against GPIHBP1's Ly6 domain, RE3 and RG3, abolished LPL binding, whereas an antibody against the acidic domain, RF4, did not. Also, mAbs RE3 and RG3 bound with reduced affinity to a mutant GPIHBP1 containing an Ly6 domain mutation (W109S) that abolishes LPL binding. Immunohistochemistry studies with the GPIHBP1 mAbs revealed that human GPIHBP1 is expressed only in capillary endothelial cells. Finally, we created an ELISA that detects GPIHBP1 in human plasma. That ELISA should make it possible for clinical lipidologists to determine whether plasma GPIHBP1 levels are a useful biomarker of metabolic or vascular disease.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Lipase Lipoproteica/imunologia
Receptores de Lipoproteínas/imunologia
Triglicerídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação/imunologia
Linhagem Celular
Drosophila
Células Endoteliais/enzimologia
Células Endoteliais/imunologia
Seres Humanos
Lipase Lipoproteica/antagonistas & inibidores
Lipase Lipoproteica/isolamento & purificação
Camundongos
Receptores de Lipoproteínas/genética
Triglicerídeos/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (GPIHBP1 protein, human); 0 (Receptors, Lipoprotein); 0 (Triglycerides); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M072462


  8 / 1989 MEDLINE  
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[PMID]:27811232
[Au] Autor:Allan CM; Larsson M; Jung RS; Ploug M; Bensadoun A; Beigneux AP; Fong LG; Young SG
[Ad] Endereço:Departments of Medicine University of California Los Angeles, Los Angeles, CA 90095.
[Ti] Título:Mobility of "HSPG-bound" LPL explains how LPL is able to reach GPIHBP1 on capillaries.
[So] Source:J Lipid Res;58(1):216-225, 2017 Jan.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In mice lacking glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 (GPIHBP1), the LPL secreted by adipocytes and myocytes remains bound to heparan sulfate proteoglycans (HSPGs) on all cells within tissues. That observation raises a perplexing issue: Why isn't the freshly secreted LPL in wild-type mice captured by the same HSPGs, thereby preventing LPL from reaching GPIHBP1 on capillaries? We hypothesized that LPL-HSPG interactions are transient, allowing the LPL to detach and move to GPIHBP1 on capillaries. Indeed, we found that LPL detaches from HSPGs on cultured cells and moves to: 1) soluble GPIHBP1 in the cell culture medium; 2) GPIHBP1-coated agarose beads; and 3) nearby GPIHBP1-expressing cells. Movement of HSPG-bound LPL to GPIHBP1 did not occur when GPIHBP1 contained a Ly6 domain missense mutation (W109S), but was almost normal when GPIHBP1's acidic domain was mutated. To test the mobility of HSPG-bound LPL in vivo, we injected GPIHBP1-coated agarose beads into the brown adipose tissue of GPIHBP1-deficient mice. LPL moved quickly from HSPGs on adipocytes to GPIHBP1-coated beads, thereby depleting LPL stores on the surface of adipocytes. We conclude that HSPG-bound LPL in the interstitial spaces of tissues is mobile, allowing the LPL to move to GPIHBP1 on endothelial cells.
[Mh] Termos MeSH primário: Adipócitos/metabolismo
Proteoglicanas de Heparan Sulfato/metabolismo
Lipase Lipoproteica/genética
Receptores de Lipoproteínas/genética
[Mh] Termos MeSH secundário: Animais
Capilares/enzimologia
Capilares/metabolismo
Linhagem Celular
Quilomícrons/metabolismo
Meios de Cultura/química
Células Hep G2
Seres Humanos
Lipólise/genética
Lipase Lipoproteica/metabolismo
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chylomicrons); 0 (Culture Media); 0 (GPI-HBP1 protein, mouse); 0 (Heparan Sulfate Proteoglycans); 0 (Receptors, Lipoprotein); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M072520


  9 / 1989 MEDLINE  
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Fotocópia
[PMID]:27793914
[Au] Autor:Takano K; Kakuki T; Obata K; Nomura K; Miyata R; Kondo A; Kurose M; Kakiuchi A; Kaneko Y; Kohno T; Himi T; Kojima T
[Ad] Endereço:Department of Otolaryngology, Research Institute for Frontier Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan kent@sapmed.ac.jp.
[Ti] Título:The Behavior and Role of Lipolysis-stimulated Lipoprotein Receptor, a Component of Tricellular Tight Junctions, in Head and Neck Squamous Cell Carcinomas.
[So] Source:Anticancer Res;36(11):5895-5904, 2016 11.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Lipolysis-stimulated lipoprotein receptor (LSR) knockdown has also been reported to increase the motility and invasiveness of certain cancer cells. Here, we describe, for the first time, the behavior and role of LSR in head and neck squamous cell carcinoma (HNSCC) in vivo and in vitro. MATERIALS AND METHODS: Samples of HNSCC, normal palatine tonsils, the pharynx carcinoma cell line Detroit562 and primary cultured HNSCC were characterized by immunostaining, western blot, real-time polymerase chain reaction (PCR), Matrigel invasion and proliferation assays. RESULTS: Protein and mRNA of LSR were strongly expressed, as well as claudin-1 in HNSCC tissues than in normal tissues, especially in invasive tissues. Knock-down of LSR and claudin-1 (CLDN-1), but not tricellulin (TRIC) by siRNAs, markedly induced invasiveness of Detroit562 cells and primary cultured HNSCC. LSR inhibited the development and progression of HNSCC. CONCLUSION: LSR is a potential target for new forms of head and neck cancer therapy.
[Mh] Termos MeSH primário: Carcinoma de Células Escamosas/metabolismo
Neoplasias de Cabeça e Pescoço/metabolismo
Receptores de Lipoproteínas/fisiologia
Junções Íntimas/fisiologia
[Mh] Termos MeSH secundário: Carcinoma de Células Escamosas/patologia
Linhagem Celular Tumoral
Claudina-1/metabolismo
Neoplasias de Cabeça e Pescoço/patologia
Seres Humanos
Lipólise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Claudin-1); 0 (Receptors, Lipoprotein)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170131
[Lr] Data última revisão:
170131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161030
[St] Status:MEDLINE


  10 / 1989 MEDLINE  
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Texto completo
[PMID]:27694217
[Au] Autor:Pal R; Ke Q; Pihan GA; Yesilaltay A; Penman ML; Wang L; Chitraju C; Kang PM; Krieger M; Kocher O
[Ad] Endereço:Department of Pathology and Center for Vascular Biology Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts.
[Ti] Título:Carboxy-terminal deletion of the HDL receptor reduces receptor levels in liver and steroidogenic tissues, induces hypercholesterolemia, and causes fatal heart disease.
[So] Source:Am J Physiol Heart Circ Physiol;311(6):H1392-H1408, 2016 Dec 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The HDL receptor SR-BI mediates the transfer of cholesteryl esters from HDL to cells and controls HDL abundance and structure. Depending on the genetic background, loss of SR-BI causes hypercholesterolemia, anemia, reticulocytosis, splenomegaly, thrombocytopenia, female infertility, and fatal coronary heart disease (CHD). The carboxy terminus of SR-BI ( QEAKL ) must bind to the cytoplasmic adaptor PDZK1 for normal hepatic-but not steroidogenic cell-expression of SR-BI protein. To determine whether SR-BI's carboxy terminus is also required for normal protein levels in steroidogenic cells, we introduced into SR-BI's gene a Ala/STOP mutation that produces a truncated receptor (SR-BIΔCT). As expected, the dramatic reduction of hepatic receptor protein in SR-BIΔCT mice was similar to that in PDZK1 knockout (KO) mice. Unlike SR-BI KO females, SR-BIΔCT females were fertile. The severity of SR-BIΔCT mice's hypercholesterolemia was intermediate between those of SR-BI KO and PDZK1 KO mice. Substantially reduced levels of the receptor in adrenal cortical cells, ovarian cells, and testicular Leydig cells in SR-BIΔCT mice suggested that steroidogenic cells have an adaptor(s) functionally analogous to hepatic PDZK1. When SR-BIΔCT mice were crossed with apolipoprotein E KO mice (SR-BIΔCT/apoE KO), pathologies including hypercholesterolemia, macrocytic anemia, hepatic and splenic extramedullary hematopoiesis, massive splenomegaly, reticulocytosis, thrombocytopenia, and rapid-onset and fatal occlusive coronary arterial atherosclerosis and CHD (median age of death: 9 wk) were observed. These results provide new insights into the control of SR-BI in steroidogenic cells and establish SR-BIΔCT/apoE KO mice as a new animal model for the study of CHD.
[Mh] Termos MeSH primário: Córtex Suprarrenal/metabolismo
Hipercolesterolemia/genética
Células Intersticiais do Testículo/metabolismo
Fígado/metabolismo
Ovário/metabolismo
Receptores Depuradores Classe B/genética
[Mh] Termos MeSH secundário: Anemia Macrocítica/genética
Animais
Apolipoproteínas E/genética
Doença da Artéria Coronariana/genética
Doença da Artéria Coronariana/mortalidade
Doença das Coronárias/genética
Doença das Coronárias/mortalidade
Oclusão Coronária/genética
Oclusão Coronária/mortalidade
Feminino
Técnicas de Introdução de Genes
Hematopoese Extramedular/genética
Immunoblotting
Lipoproteínas HDL/genética
Masculino
Camundongos
Mutação
Reação em Cadeia da Polimerase
Receptores de Lipoproteínas/genética
Reticulocitose/genética
Esplenomegalia/genética
Trombocitopenia/genética
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Apolipoproteins E); 0 (Lipoproteins, HDL); 0 (Receptors, Lipoprotein); 0 (Scarb1 protein, mouse); 0 (Scavenger Receptors, Class B); 0 (high density lipoprotein receptors)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00463.2016



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