Base de dados : MEDLINE
Pesquisa : D12.776.543.512 [Categoria DeCS]
Referências encontradas : 99 [refinar]
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[PMID]:29351320
[Au] Autor:Kumar P; van Son M; Zheng T; Valdink D; Raap J; Kros A; Huber M
[Ad] Endereço:Department of Physics, Huygens-Kamerlingh Onnes Laboratory, Leiden University, Leiden, The Netherlands.
[Ti] Título:Coiled-coil formation of the membrane-fusion K/E peptides viewed by electron paramagnetic resonance.
[So] Source:PLoS One;13(1):e0191197, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The interaction of the complementary K (Ac-(KIAALKE)3-GW-NH2) and E (Ac-(EIAALEK)3-GY-NH2) peptides, components of the zipper of an artificial membrane fusion system (Robson Marsden H. et al. Angew Chemie Int Ed. 2009) is investigated by electron paramagnetic resonance (EPR). By frozen solution continuous-wave EPR and double electron-electron resonance (DEER), the distance between spin labels attached to the K- and to the E-peptide is measured. Three constructs of spin-labelled K- and E-peptides are used in five combinations for low temperature investigations. The K/E heterodimers are found to be parallel, in agreement with previous studies. Also, K homodimers in parallel orientation were observed, a finding that was not reported before. Comparison to room-temperature, solution EPR shows that the latter method is less specific to detect this peptide-peptide interaction. Combining frozen solution cw-EPR for short distances (1.8 nm to 2.0 nm) and DEER for longer distances thus proves versatile to detect the zipper interaction in membrane fusion. As the methodology can be applied to membrane samples, the approach presented suggests itself for in-situ studies of the complete membrane fusion process, opening up new avenues for the study of membrane fusion.
[Mh] Termos MeSH primário: Proteínas de Fusão de Membrana/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Simulação por Computador
Espectroscopia de Ressonância de Spin Eletrônica
Fusão de Membrana/fisiologia
Proteínas de Fusão de Membrana/fisiologia
Modelos Moleculares
Oligopeptídeos/química
Domínios e Motivos de Interação entre Proteínas
Estrutura Quaternária de Proteína
Estrutura Secundária de Proteína
Marcadores de Spin
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Oligopeptides); 0 (Spin Labels)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180120
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191197


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[PMID]:28917834
[Au] Autor:Xu Y; Jo I; Wang L; Chen J; Fan S; Dong Y; Quan C; Ha NC
[Ad] Endereço:Department of Bioengineering, College of Life Science, Dalian Minzu University, Dalian 116600, Liaoning, China; Key Laboratory of Biotechnology and Bioresources Utilization (Dalian Minzu University), Ministry of Education, China. Electronic address: yongbinxu@dlnu.edu.cn.
[Ti] Título:Hexameric assembly of membrane fusion protein YknX of the sporulation delaying efflux pump from Bacillus amyloliquefaciens.
[So] Source:Biochem Biophys Res Commun;493(1):152-157, 2017 Nov 04.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Membrane fusion proteins (MFPs) play an essential role in the action of the drug efflux pumps and protein secretion systems in bacteria. The sporulation delaying protein (SDP) efflux pump YknWXYZ has been identified in diverse Bacillus species. The MFP YknX requires the ATP-binding cassette (ABC) transporter YknYZ and the Yip1 family protein YknW to form a functional complex. To date, the crystal structure, molecular function and mechanism of action of YknX remain unknown. In this study, to characterize the structural and biochemical roles of YknX in the functional assembly of YknWXYZ from B. amyloliquefaciens, we successfully obtained crystals of the YknX protein that diffracted X-rays to a resolution of 4.4 Å. We calculated an experimentally phased map using single-wavelength anomalous diffraction (SAD), revealing that YknX forms a hexameric assembly similar to that of MacA from Gram-negative bacteria. The hexameric assembly of YknX exhibited a funnel-like structure with a central channel and a conical mouth. Functional studies in vitro suggest that YknX can bind directly to peptidoglycan. Our study provides an improved understanding of the assembly of the YknWXYZ efflux pump and the role of YknX in the complex.
[Mh] Termos MeSH primário: Bacillus amyloliquefaciens/química
Proteínas de Bactérias/química
Proteínas de Bactérias/ultraestrutura
Proteínas de Fusão de Membrana/química
Proteínas de Fusão de Membrana/ultraestrutura
Peptidoglicano/química
[Mh] Termos MeSH secundário: Sítios de Ligação
Dimerização
Proteínas de Membrana Transportadoras
Modelos Químicos
Modelos Moleculares
Ligação Proteica
Conformação Proteica
Esporos Bacterianos/química
Esporos Bacterianos/ultraestrutura
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Membrane Fusion Proteins); 0 (Membrane Transport Proteins); 0 (Peptidoglycan)
[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:170918
[St] Status:MEDLINE


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[PMID]:28356294
[Au] Autor:Aslamy A; Thurmond DC
[Ad] Endereço:Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, Indiana; and.
[Ti] Título:Exocytosis proteins as novel targets for diabetes prevention and/or remediation?
[So] Source:Am J Physiol Regul Integr Comp Physiol;312(5):R739-R752, 2017 May 01.
[Is] ISSN:1522-1490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Diabetes remains one of the leading causes of morbidity and mortality worldwide, affecting an estimated 422 million adults. In the US, it is predicted that one in every three children born as of 2000 will suffer from diabetes in their lifetime. Type 2 diabetes results from combinatorial defects in pancreatic ß-cell glucose-stimulated insulin secretion and in peripheral glucose uptake. Both processes, insulin secretion and glucose uptake, are mediated by exocytosis proteins, SNARE (soluble -ethylmaleimide-sensitive factor attachment protein receptor) complexes, Sec1/Munc18 (SM), and double C2-domain protein B (DOC2B). Increasing evidence links deficiencies in these exocytosis proteins to diabetes in rodents and humans. Given this, emerging studies aimed at restoring and/or enhancing cellular levels of certain exocytosis proteins point to promising outcomes in maintaining functional ß-cell mass and enhancing insulin sensitivity. In doing so, new evidence also shows that enhancing exocytosis protein levels may promote health span and longevity and may also harbor anti-cancer and anti-Alzheimer's disease capabilities. Herein, we present a comprehensive review of the described capabilities of certain exocytosis proteins and how these might be targeted for improving metabolic dysregulation.
[Mh] Termos MeSH primário: Diabetes Mellitus Tipo 2/tratamento farmacológico
Diabetes Mellitus Tipo 2/metabolismo
Exocitose/efeitos dos fármacos
Proteínas de Fusão de Membrana/metabolismo
Terapia de Alvo Molecular/métodos
Proteínas de Transporte Vesicular/metabolismo
[Mh] Termos MeSH secundário: Animais
Diabetes Mellitus Tipo 2/prevenção & controle
Sistemas de Liberação de Medicamentos/métodos
Medicina Baseada em Evidências
Seres Humanos
Proteínas de Fusão de Membrana/antagonistas & inibidores
Modelos Biológicos
Proteínas de Transporte Vesicular/antagonistas & inibidores
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Vesicular Transport Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170331
[St] Status:MEDLINE
[do] DOI:10.1152/ajpregu.00002.2017


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[PMID]:28235200
[Au] Autor:Fédry J; Liu Y; Péhau-Arnaudet G; Pei J; Li W; Tortorici MA; Traincard F; Meola A; Bricogne G; Grishin NV; Snell WJ; Rey FA; Krey T
[Ad] Endereço:Unité de Virologie Structurale, Institut Pasteur, 25-28 Rue du Docteur Roux, 75724 Paris, France; CNRS UMR 3569, 25-28 Rue du Docteur Roux, 75724 Paris, France; Université Paris Descartes Sorbonne Paris Cité, Institut Pasteur, Rue du Docteur Roux, 75015 Paris, France; Institute of Virology, Hannover
[Ti] Título:The Ancient Gamete Fusogen HAP2 Is a Eukaryotic Class II Fusion Protein.
[So] Source:Cell;168(5):904-915.e10, 2017 Feb 23.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sexual reproduction is almost universal in eukaryotic life and involves the fusion of male and female haploid gametes into a diploid cell. The sperm-restricted single-pass transmembrane protein HAP2-GCS1 has been postulated to function in membrane merger. Its presence in the major eukaryotic taxa-animals, plants, and protists (including important human pathogens like Plasmodium)-suggests that many eukaryotic organisms share a common gamete fusion mechanism. Here, we report combined bioinformatic, biochemical, mutational, and X-ray crystallographic studies on the unicellular alga Chlamydomonas reinhardtii HAP2 that reveal homology to class II viral membrane fusion proteins. We further show that targeting the segment corresponding to the fusion loop by mutagenesis or by antibodies blocks gamete fusion. These results demonstrate that HAP2 is the gamete fusogen and suggest a mechanism of action akin to viral fusion, indicating a way to block Plasmodium transmission and highlighting the impact of virus-cell genetic exchanges on the evolution of eukaryotic life.
[Mh] Termos MeSH primário: Chlamydomonas/metabolismo
Proteínas de Fusão de Membrana/química
Proteínas de Plantas/química
Plasmodium/metabolismo
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Evolução Biológica
Chlamydomonas/citologia
Cristalografia por Raios X
Células Germinativas/química
Células Germinativas/metabolismo
Proteínas de Fusão de Membrana/genética
Proteínas de Fusão de Membrana/metabolismo
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Plasmodium/citologia
Domínios Proteicos
Proteínas de Protozoários/genética
Proteínas de Protozoários/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Plant Proteins); 0 (Protozoan Proteins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170225
[St] Status:MEDLINE


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[PMID]:27986571
[Au] Autor:Molino D; Zemirli N; Codogno P; Morel E
[Ad] Endereço:Cell Biology Department of Institut Necker-Enfants Malades (INEM), INSERM U1151-CNRS UMR 8253, Paris, France; Université Paris Descartes-Sorbonne Paris Cité, F-75993 Paris, France.
[Ti] Título:The Journey of the Autophagosome through Mammalian Cell Organelles and Membranes.
[So] Source:J Mol Biol;429(4):497-514, 2017 Feb 17.
[Is] ISSN:1089-8638
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Autophagy is an intracellular degradation process carried out by a double-membrane organelle, termed the autophagosome, which sequesters cytoplasmic material destined for lysosomal degradation and recycling. Autophagy and autophagosome biogenesis are highly conserved processes in eukaryotes and are essential for cell survival, stress responses, and homeostasis. Autophagosomes are dynamic and complex organelles that can originate from several different membrane compartments. Autophagosomes traffic through the cell to fuse with lysosomes or other compartments. Despite identification of key proteins necessary for autophagosome assembly and transport, such as those encoded by the autophagy-related genes, the relationship and interdependence of the autophagosome with other intracellular endo-membranes, including those of organelles involved in exocytosis and endocytic trafficking pathways, are still poorly understood. Here we discuss formation of autophagosomes, the journey of these organelles through the cell, and their close interplay with other mammalian organelles from points of view of signalization platforms and membrane dynamics.
[Mh] Termos MeSH primário: Autofagossomos/fisiologia
Autofagia
[Mh] Termos MeSH secundário: Animais
Retículo Endoplasmático/metabolismo
Seres Humanos
Membranas Intracelulares/metabolismo
Lisossomos/fisiologia
Mamíferos/metabolismo
Proteínas de Fusão de Membrana/metabolismo
Mitocôndrias/fisiologia
Transporte Proteico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Membrane Fusion Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE


  6 / 99 MEDLINE  
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[PMID]:27836986
[Au] Autor:Carnemolla R; Villa CH; Greineder CF; Zaitsev S; Patel KR; Kowalska MA; Atochin DN; Cines DB; Siegel DL; Esmon CT; Muzykantov VR
[Ad] Endereço:Department of Pharmacology, The Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania; USA.
[Ti] Título:Targeting thrombomodulin to circulating red blood cells augments its protective effects in models of endotoxemia and ischemia-reperfusion injury.
[So] Source:FASEB J;31(2):761-770, 2017 Feb.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Endothelial thrombomodulin (TM) regulates coagulation and inflammation via several mechanisms, including production of activated protein C (APC). Recombinant APC and soluble fragments of TM (sTM) have been tested in settings associated with insufficiency of the endogenous TM/APC pathway, such as sepsis. We previously designed a fusion protein of TM [single-chain variable fragment antibody (scFv)/TM] targeted to red blood cells (RBCs) to improve pharmacokinetics and antithrombotic effects without increasing bleeding. Here, scFv/TM was studied in mouse models of systemic inflammation and ischemia-reperfusion injury. Injected concomitantly with or before endotoxin, scFv/TM provided more potent protection against liver injury and release of pathological mediators than sTM, showing similar efficacy at up to 50-fold lower doses. scFv/TM provided protection when injected after endotoxin, whereas sTM did not, and augmented APC production by thrombin ∼50-fold more than sTM. However, scFv/TM injected after endotoxin did not reduce thrombin/antithrombin complexes; nor did antibodies that block APC anticoagulant activity suppress the prophylactic anti-inflammatory effect of scFv/TM. Therefore, similar to endogenous TM, RBC-anchored scFv/TM activates several protective pathways. Finally, scFv/TM was more effective at reducing cerebral infarct volume and alleviated neurological deficits than sTM after cerebral ischemia/reperfusion injury. These results indicate that RBC-targeted scFv/TM exerts multifaceted cytoprotective effects and may find utility in systemic and focal inflammatory and ischemic disorders.-Carnemolla, R., Villa, C. H., Greineder, C. F., Zaitseva, S., Patel, K. R., Kowalska, M. A., Atochin, D. N., Cines, D. B., Siegel, D. L., Esmon, C. T., Muzykantov, V. R. Targeting thrombomodulin to circulating red blood cells augments its protective effects in models of endotoxemia and ischemia-reperfusion injury.
[Mh] Termos MeSH primário: Endotoxemia/prevenção & controle
Eritrócitos/metabolismo
Traumatismo por Reperfusão/prevenção & controle
Trombomodulina/administração & dosagem
Trombomodulina/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Inflamação/tratamento farmacológico
Masculino
Proteínas de Fusão de Membrana
Camundongos
Camundongos Endogâmicos C57BL
Trombomodulina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Thrombomodulin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201600912R


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[PMID]:26879310
[Au] Autor:Yan S; Zhang H; Guo X; Wang J; Dai J
[Ad] Endereço:Key Laboratory of Animal Ecology and Conservation Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing, 100101, People's Republic of China.
[Ti] Título:High perfluorooctanoic acid exposure induces autophagy blockage and disturbs intracellular vesicle fusion in the liver.
[So] Source:Arch Toxicol;91(1):247-258, 2017 Jan.
[Is] ISSN:1432-0738
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Perfluorooctanoic acid (PFOA) has been shown to cause hepatotoxicity and other toxicological effects. Though PPARα activation by PFOA in the liver has been well accepted as an important mechanism of PFOA-induced hepatotoxicity, several pieces of evidence have shown that the hepatotoxic effects of PFOA may not be fully explained by PPARα activation. In this study, we observed autophagosome accumulation in mouse livers as well as HepG2 cells after PFOA exposure. Further in vitro study revealed that the accumulation of autophagosomes was not caused by autophagic flux stimulation. In addition, we observed that PFOA exposure affected the proteolytic activity of HepG2 cells while significant dysfunction of lysosomes was not detected. Quantitative proteomic analysis of crude lysosomal fractions from HepG2 cells treated with PFOA revealed that 54 differentially expressed proteins were related to autophagy or vesicular trafficking and fusion. The proteomic results were further validated in the cells in vitro and livers in vivo after PFOA exposure, which implied potential dysfunction at the late stage of autophagy. However, in HepG2 cells, it seemed that further inhibition of autophagy did not significantly alter the effects of PFOA on cell viability. Although these findings demonstrate that PFOA blocked autophagy and disturbed intracellular vesicle fusion in the liver, the changes in autophagy were observed only at high cytotoxic concentrations of PFOA, suggesting that autophagy may not be a primary target or mode of toxicity. Furthermore, since altered liver autophagy was not observed at concentrations of PFOA associated with human exposures, the relevance of these findings must be questioned.
[Mh] Termos MeSH primário: Autofagossomos/efeitos dos fármacos
Autofagia/efeitos dos fármacos
Caprilatos/toxicidade
Doença Hepática Induzida por Substâncias e Drogas/patologia
Poluentes Ambientais/toxicidade
Fluorcarbonetos/toxicidade
Fígado/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Autofagossomos/metabolismo
Autofagossomos/patologia
Proteínas Relacionadas à Autofagia/antagonistas & inibidores
Proteínas Relacionadas à Autofagia/genética
Proteínas Relacionadas à Autofagia/metabolismo
Caprilatos/administração & dosagem
Sobrevivência Celular/efeitos dos fármacos
Doença Hepática Induzida por Substâncias e Drogas/metabolismo
Proteínas do Citoesqueleto/antagonistas & inibidores
Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/metabolismo
Relação Dose-Resposta a Droga
Poluentes Ambientais/administração & dosagem
Fluorcarbonetos/administração & dosagem
Perfilação da Expressão Gênica
Regulação da Expressão Gênica/efeitos dos fármacos
Células Hep G2
Seres Humanos
Fígado/metabolismo
Fígado/patologia
Lisossomos/efeitos dos fármacos
Lisossomos/metabolismo
Lisossomos/patologia
Masculino
Proteínas de Fusão de Membrana/antagonistas & inibidores
Proteínas de Fusão de Membrana/genética
Proteínas de Fusão de Membrana/metabolismo
Camundongos Endogâmicos BALB C
Proteólise/efeitos dos fármacos
Interferência de RNA
Distribuição Aleatória
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autophagy-Related Proteins); 0 (Caprylates); 0 (Cytoskeletal Proteins); 0 (Environmental Pollutants); 0 (Fluorocarbons); 0 (Membrane Fusion Proteins); 947VD76D3L (perfluorooctanoic acid)
[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:160217
[St] Status:MEDLINE
[do] DOI:10.1007/s00204-016-1675-1


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[PMID]:27307091
[Au] Autor:Ho R; Stroupe C
[Ad] Endereço:Department of Molecular Physiology and Biological Physics and Center for Membrane Biology, University of Virginia School of Medicine, Charlottesville, VA, USA.
[Ti] Título:The HOPS/Class C Vps Complex Tethers High-Curvature Membranes via a Direct Protein-Membrane Interaction.
[So] Source:Traffic;17(10):1078-90, 2016 Oct.
[Is] ISSN:1600-0854
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Membrane tethering is a physical association of two membranes before their fusion. Many membrane tethering factors have been identified, but the interactions that mediate inter-membrane associations remain largely a matter of conjecture. Previously, we reported that the homotypic fusion and protein sorting/Class C vacuolar protein sorting (HOPS/Class C Vps) complex, which has two binding sites for the yeast vacuolar Rab GTPase Ypt7p, can tether two low-curvature liposomes when both membranes bear Ypt7p. Here, we show that HOPS tethers highly curved liposomes to Ypt7p-bearing low-curvature liposomes even when the high-curvature liposomes are protein-free. Phosphorylation of the curvature-sensing amphipathic lipid-packing sensor (ALPS) motif from the Vps41p HOPS subunit abrogates tethering of high-curvature liposomes. A HOPS complex without its Vps39p subunit, which contains one of the Ypt7p binding sites in HOPS, lacks tethering activity, though it binds high-curvature liposomes and Ypt7p-bearing low-curvature liposomes. Thus, HOPS tethers highly curved membranes via a direct protein-membrane interaction. Such high-curvature membranes are found at the sites of vacuole tethering and fusion. There, vacuole membranes bend sharply, generating large areas of vacuole-vacuole contact. We propose that HOPS localizes via the Vps41p ALPS motif to these high-curvature regions. There, HOPS binds via Vps39p to Ypt7p in an apposed vacuole membrane.
[Mh] Termos MeSH primário: Membranas Intracelulares/metabolismo
Fusão de Membrana/fisiologia
Complexos Multiproteicos/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Vacúolos/metabolismo
Proteínas de Transporte Vesicular/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Proteínas de Fluorescência Verde/genética
Lipossomos/química
Lipossomos/metabolismo
Proteínas Luminescentes/genética
Proteínas de Fusão de Membrana/química
Proteínas de Fusão de Membrana/genética
Proteínas de Fusão de Membrana/metabolismo
Microscopia Confocal
Microscopia de Fluorescência
Complexos Multiproteicos/química
Corpos Multivesiculares/metabolismo
Fosforilação
Ligação Proteica
Transporte Proteico
Proteínas de Transporte Vesicular/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Luminescent Proteins); 0 (Membrane Fusion Proteins); 0 (Multiprotein Complexes); 0 (Saccharomyces cerevisiae Proteins); 0 (Vesicular Transport Proteins); 0 (red fluorescent protein); 147336-22-9 (Green Fluorescent Proteins); EC 3.6.1.- (YPT7 protein, S cerevisiae); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160617
[St] Status:MEDLINE
[do] DOI:10.1111/tra.12421


  9 / 99 MEDLINE  
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[PMID]:27095536
[Au] Autor:Gillespie JW; Wei L; Petrenko VA
[Ti] Título:Selection of Lung Cancer-Specific Landscape Phage for Targeted Drug Delivery.
[So] Source:Comb Chem High Throughput Screen;19(5):412-22, 2016.
[Is] ISSN:1875-5402
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Cancer cell-specific diagnostic or therapeutic tools are commonly believed to significantly increase the success rate of cancer diagnosis and targeted therapies. To extend the repertoire of available cancer cell-specific phage fusion proteins and study their efficacy as navigating moieties, we used two landscape phage display libraries f8/8 and f8/9 displaying an 8- or 9-mer random peptide fusion to identify a panel of novel peptide families that are specific to Calu-3 cells. Using a phage capture assay, we showed that two of the selected phage clones, ANGRPSMT and VNGRAEAP (phage and their recombinant proteins are named by the sequence of the fusion peptide), are selective for the Calu-3 cell line in comparison to phenotypically normal lung epithelial cells and distribute into unique subcellular fractions.
[Mh] Termos MeSH primário: Neoplasias Pulmonares/tratamento farmacológico
Terapia de Alvo Molecular/métodos
Biblioteca de Peptídeos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Linhagem Celular Tumoral
Sistemas de Liberação de Medicamentos
Seres Humanos
Neoplasias Pulmonares/patologia
Proteínas de Fusão de Membrana/metabolismo
Peptídeos
Frações Subcelulares/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Fusion Proteins); 0 (Peptide Library); 0 (Peptides)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160421
[St] Status:MEDLINE


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[PMID]:26725667
[Au] Autor:Takahashi Y; Nishikawa M; Takakura Y
[Ad] Endereço:Graduate School of Pharmaceutical Sciences, Kyoto University.
[Ti] Título:[Analysis and Control of in Vivo Kinetics of Exosomes for the Development of Exosome-based DDS].
[So] Source:Yakugaku Zasshi;136(1):49-53, 2016.
[Is] ISSN:1347-5231
[Cp] País de publicação:Japan
[La] Idioma:jpn
[Ab] Resumo:  Exosomes are secretory membrane vesicles containing lipids, proteins, and nucleic acids. They act as intercellular transporters by delivering their components to exosome recipient cells. Based on their endogenous delivery system properties, exosomes are expected to become drug delivery systems (DDS) for various molecules such as nucleic acid-based drugs. Important factors such as drug loading to exosomes, production, and pharmacokinetics of exosomes need to be considered for the development of exosome-based DDS. Of these, the pharmacokinetics of exosomes have rarely been studied, probably because of the lack of quantitative evaluation methods of in vivo exosomal pharmacokinetics. We selected lactadherin as an exosome tropic protein and developed it as a fusion protein with Gaussia luciferase to label exosomes for in vivo imaging. In addition, a fusion protein of lactadherin and streptavidin was developed, and the tissue distribution of exosomes was quantitatively evaluated by radiolabeling the exosomes using (125)I-labeled biotin. Using labeled exosomes, we found that intravenously injected exosomes were rapidly cleared from the systemic circulation by macrophages. In addition, the exosomes were mainly distributed to the liver, lung, and spleen. We also examined the effect of exosome isolation methods on their physicochemical and pharmacokinetic properties. We found that exosomes collected by the ultracentrifugation-based density-gradient method were more dispersed than exosomes collected by other methods, including the ultracentrifugation-based pelleting method. The gradient method is more time-consuming than others; therefore the development of a more efficient method for exosome isolation will advance the development of exosome-based DDS.
[Mh] Termos MeSH primário: Sistemas de Liberação de Medicamentos
Exossomos/metabolismo
Farmacocinética
[Mh] Termos MeSH secundário: Antígenos de Superfície
Centrifugação com Gradiente de Concentração
Seres Humanos
Injeções Intravenosas
Macrófagos/metabolismo
Proteínas de Fusão de Membrana
Proteínas do Leite
Estreptavidina
Distribuição Tecidual
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, Surface); 0 (MFGE8 protein, human); 0 (Membrane Fusion Proteins); 0 (Milk Proteins); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160105
[St] Status:MEDLINE
[do] DOI:10.1248/yakushi.15-00227-2



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