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Pesquisa : A11.284.430.214.190.875.190.880.180 [Categoria DeCS]
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[PMID]:28119103
[Au] Autor:Csongradi C; du Plessis J; Aucamp ME; Gerber M
[Ad] Endereço:Centre of Excellence for Pharmaceutical Sciences (Pharmacen), North-West University, Private Bag X6001, Potchefstroom 2520, South Africa.
[Ti] Título:Topical delivery of roxithromycin solid-state forms entrapped in vesicles.
[So] Source:Eur J Pharm Biopharm;114:96-107, 2017 May.
[Is] ISSN:1873-3441
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Recently, considerable interest developed in using newer/improved antibiotics for the treatment of Acne vulgaris. During this study, different roxithromycin solid-state forms (i.e. crystalline and amorphous) were encapsulated into vesicle systems (niosomes, proniosomes, ufosomes and pro-ufosomes) for dermis targeted delivery. Characterization of the vesicles was done with transmission electron microscopy, light microscopy, droplet size, droplet size distribution, pH, zeta-potential and entrapment efficiency percentage. Finally, comparative release and topical diffusion studies were performed, to evaluate if targeted topical delivery was obtained and if the roxithromycin solid-state amorphous forms resulted in improved topical delivery. Vesicle systems containing different roxithromycin (2%) solid-state forms were successfully prepared and characterized. The vesicles showed optimal properties for topical delivery. All carrier systems had topical delivery to the epidermis-dermis, whilst no roxithromycin was found in the receptor compartment or stratum corneum-epidermis. The niosomes were the leading formulation and the two amorphous forms had better topical delivery than the crystalline form. Successful targeted delivery of roxithromycin was obtained in the dermis, where the activity against Propionibacterium acnes is needed. The amorphous forms seemed to have held their solid-state form during formulation and in the vesicles, showing improved topical delivery in comparison to the crystalline form.
[Mh] Termos MeSH primário: Antibacterianos/administração & dosagem
Roxitromicina/administração & dosagem
[Mh] Termos MeSH secundário: Administração Tópica
Vesículas Revestidas
Cristalização
Difusão
Portadores de Fármacos
Composição de Medicamentos
Sistemas de Liberação de Medicamentos
Seres Humanos
Técnicas In Vitro
Lipossomos
Testes de Sensibilidade Microbiana
Tamanho da Partícula
Propionibacterium acnes/efeitos dos fármacos
Pele/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Drug Carriers); 0 (Liposomes); 21KOF230FA (Roxithromycin)
[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:170126
[St] Status:MEDLINE


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[PMID]:27262127
[Au] Autor:Robinson DG; Neuhaus JM
[Ad] Endereço:Centre for Organismal Studies (COS), University of Heidelberg, Germany david.robinson@urz.uni-heidelberg.de.
[Ti] Título:Receptor-mediated sorting of soluble vacuolar proteins: myths, facts, and a new model.
[So] Source:J Exp Bot;67(15):4435-49, 2016 Aug.
[Is] ISSN:1460-2431
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To prevent their being released to the cell exterior, acid hydrolases are recognized by receptors at some point in the secretory pathway and diverted towards the lytic compartment of the cell (lysosome or vacuole). In animal cells, the receptor is called the mannosyl 6-phosphate receptor (MPR) and it binds hydrolase ligands in the trans-Golgi network (TGN). These ligands are then sequestered into clathrin-coated vesicles (CCVs) because of motifs in the cytosolic tail of the MPR which interact first with monomeric adaptors (Golgi-localized, Gamma-ear-containing, ARF-binding proteins, GGAs) and then with tetrameric (adaptin) adaptor complexes. The CCVs then fuse with an early endosome, whose more acidic lumen causes the ligands to dissociate. The MPRs are then recycled back to the TGN via retromer-coated carriers. Plants have vacuolar sorting receptors (VSRs) which were originally identified in CCVs isolated from pea (Pisum sativum L.) cotyledons. It was therefore assumed that VSRs would have an analogous function in plants to MPRs in animals. Although this dogma has enjoyed wide support over the last 20 years there are many inconsistencies. Recently, results have been published which are quite contrary to it. It now emerges that VSRs and their ligands can interact very early in the secretory pathway, and dissociate in the TGN, which, in contrast to its mammalian counterpart, has a pH of 5.5. Multivesicular endosomes in plants lack proton pump complexes and consequently have an almost neutral internal pH, which discounts them as organelles of pH-dependent receptor-ligand dissociation. These data force a critical re-evaluation of the role of CCVs at the TGN, especially considering that vacuolar cargo ligands have never been identified in them. We propose that one population of TGN-derived CCVs participate in retrograde transport of VSRs from the TGN. We also present a new model to explain how secretory and vacuolar cargo proteins are effectively separated after entering the late Golgi/TGN compartments.
[Mh] Termos MeSH primário: Proteínas de Transporte/metabolismo
Receptores de Superfície Celular/metabolismo
Vacúolos/metabolismo
[Mh] Termos MeSH secundário: Animais
Vesículas Revestidas por Clatrina/metabolismo
Vesículas Revestidas/metabolismo
Complexo de Golgi/metabolismo
Modelos Biológicos
Plantas/metabolismo
Rede trans-Golgi/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160605
[St] Status:MEDLINE
[do] DOI:10.1093/jxb/erw222


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[PMID]:26941330
[Au] Autor:Parmar HB; Duncan R
[Ad] Endereço:Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H 4R2, Canada.
[Ti] Título:A novel tribasic Golgi export signal directs cargo protein interaction with activated Rab11 and AP-1-dependent Golgi-plasma membrane trafficking.
[So] Source:Mol Biol Cell;27(8):1320-31, 2016 Apr 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The reovirus fusion-associated small transmembrane (FAST) proteins comprise a unique family of viral membrane fusion proteins dedicated to inducing cell-cell fusion. We recently reported that a polybasic motif (PBM) in the cytosolic tail of reptilian reovirus p14 FAST protein functions as a novel tribasic Golgi export signal. Using coimmunoprecipitation and fluorescence resonance energy transfer (FRET) assays, we now show the PBM directs interaction of p14 with GTP-Rab11. Overexpression of dominant-negative Rab11 and RNA interference knockdown of endogenous Rab11 inhibited p14 plasma membrane trafficking and resulted in p14 accumulation in the Golgi complex. This is the first example of Golgi export to the plasma membrane that is dependent on the interaction of membrane protein cargo with activated Rab11. RNA interference and immunofluorescence microscopy further revealed that p14 Golgi export is dependent on AP-1 (but not AP-3 or AP-4) and that Rab11 and AP-1 both colocalize with p14 at the TGN. Together these results imply the PBM mediates interactions of p14 with activated Rab11 at the TGN, resulting in p14 sorting into AP1-coated vesicles for anterograde TGN-plasma membrane transport.
[Mh] Termos MeSH primário: Complexo de Golgi/metabolismo
Sinais Direcionadores de Proteínas
Fator de Transcrição AP-1/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Membrana Celular/metabolismo
Vesículas Revestidas/metabolismo
Guanosina Trifosfato/metabolismo
Células HeLa
Seres Humanos
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Fator de Transcrição AP-1/genética
Proteínas Virais/genética
Proteínas Virais/metabolismo
Proteínas rab de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Protein Sorting Signals); 0 (Transcription Factor AP-1); 0 (Viral Proteins); 86-01-1 (Guanosine Triphosphate); EC 3.6.1.- (rab11 protein); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160305
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-12-0845


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[PMID]:26269206
[Au] Autor:Poznik M; Maitra U; König B
[Ad] Endereço:Faculty of Chemistry and Pharmacy, University of Regensburg, 93040 Regensburg, Germany. burkhard.koenig@ur.de.
[Ti] Título:The interface makes a difference: lanthanide ion coated vesicles hydrolyze phosphodiesters.
[So] Source:Org Biomol Chem;13(38):9789-92, 2015 Oct 14.
[Is] ISSN:1477-0539
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Lanthanide ions are strong Lewis acids. Their complexation to a variety of ligands can further enhance their Lewis acidity allowing the hydrolysis of phosphoesters and even DNA. We show that the interaction of lanthanide ions with vesicles from zwitterionic phosphatidylcholine lipids gives supramolecular structures in which the metal ion is loosely coordinated to the surface. This assembly provides a high density of Lewis-acidic metal centres, which hydrolyze phosphodiesters with enhanced rates.
[Mh] Termos MeSH primário: Vesículas Revestidas/química
Elementos da Série dos Lantanídeos/química
Lipídeos de Membrana/química
Fosfatidilcolinas/química
[Mh] Termos MeSH secundário: Hidrólise
Espectroscopia de Ressonância Magnética
Modelos Moleculares
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lanthanoid Series Elements); 0 (Membrane Lipids); 0 (Phosphatidylcholines); EDS2L3ODLV (1,2-oleoylphosphatidylcholine)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150814
[St] Status:MEDLINE
[do] DOI:10.1039/c5ob01265a


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[PMID]:25840125
[Au] Autor:Naderkhani E; Vasskog T; Flaten GE
[Ad] Endereço:Drug Transport and Delivery Research Group, Department of Pharmacy, University of Tromsø, The Arctic University of Norway, Universitetsveien 57, NO-9037 Tromsø, Norway.
[Ti] Título:Biomimetic PVPA in vitro model for estimation of the intestinal drug permeability using fasted and fed state simulated intestinal fluids.
[So] Source:Eur J Pharm Sci;73:64-71, 2015 Jun 20.
[Is] ISSN:1879-0720
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A prerequisite for successful oral drug therapy is the drug's ability to cross the gastrointestinal barrier. Considering the increasing number of new chemical entities in modern drug discovery, reliable and fast in vitro models are required for early and efficient prediction of intestinal permeability. To mimic the intestinal environment, use of biorelevant media may provide valuable information on in vivo drug permeation. The present study aims at improving the novel biomimetic phospholipid vesicle-based permeation assay's (PVPAbiomimetic) biorelevance by investigating the applicability of the biorelevant media; fasted state simulated intestinal fluid (FaSSIF) and fed state simulated intestinal fluid (FeSSIF). The FaSSIF and FeSSIF's influence on the permeability of the model drugs acyclovir, indomethacin, griseofulvin and nadolol was then assessed. The barriers' robustness in terms of storage stability was also evaluated. The barriers were found to maintain their integrity in presence of FaSSIF and FeSSIF. The model drugs showed changes in permeability in presence of the different simulated intestinal fluids that were in agreement with previous reports. Moreover, the barrier showed improved storage stability by maintaining its integrity for 6months. Altogether, this study moves the PVPAbiomimetic an important step towards a better in vitro permeability model for use in drug development.
[Mh] Termos MeSH primário: Biomimética
Vesículas Revestidas/química
Fosfolipídeos/química
[Mh] Termos MeSH secundário: Líquidos Corporais/química
Líquidos Corporais/metabolismo
Estabilidade de Medicamentos
Jejum/metabolismo
Fluoresceínas/metabolismo
Seres Humanos
Absorção Intestinal
Intestinos/metabolismo
Cinética
Lipossomos
Membranas Artificiais
Fósforo/metabolismo
Ácido Taurocólico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fluoresceins); 0 (Liposomes); 0 (Membranes, Artificial); 0 (Phospholipids); 27YLU75U4W (Phosphorus); 5E090O0G3Z (Taurocholic Acid); V0YM2B16TS (fluorexon)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:150429
[Lr] Data última revisão:
150429
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150404
[St] Status:MEDLINE


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[PMID]:25774831
[Au] Autor:Almonacid M; Ahmed WW; Bussonnier M; Mailly P; Betz T; Voituriez R; Gov NS; Verlhac MH
[Ad] Endereço:CIRB, Collège de France, and CNRS-UMR7241 and INSERM-U1050, Equipe Labellisée Ligue Contre le Cancer, Paris F-75005, France.
[Ti] Título:Active diffusion positions the nucleus in mouse oocytes.
[So] Source:Nat Cell Biol;17(4):470-9, 2015 Apr.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In somatic cells, the position of the cell centroid is dictated by the centrosome. The centrosome is instrumental in nucleus positioning, the two structures being physically connected. Mouse oocytes have no centrosomes, yet harbour centrally located nuclei. We demonstrate how oocytes define their geometric centre in the absence of centrosomes. Using live imaging of oocytes, knockout for the formin 2 actin nucleator, with off-centred nuclei, together with optical trapping and modelling, we discover an unprecedented mode of nucleus positioning. We document how active diffusion of actin-coated vesicles, driven by myosin Vb, generates a pressure gradient and a propulsion force sufficient to move the oocyte nucleus. It promotes fluidization of the cytoplasm, contributing to nucleus directional movement towards the centre. Our results highlight the potential of active diffusion, a prominent source of intracellular transport, able to move large organelles such as nuclei, providing in vivo evidence of its biological function.
[Mh] Termos MeSH primário: Núcleo Celular/fisiologia
Citoplasma/fisiologia
Corrente Citoplasmática/fisiologia
Proteínas dos Microfilamentos/genética
Proteínas Nucleares/genética
Oócitos/citologia
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Vesículas Revestidas/fisiologia
Corrente Citoplasmática/efeitos dos fármacos
Feminino
Espaço Intracelular/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Proteínas dos Microfilamentos/farmacologia
Microtúbulos/fisiologia
Miosina Tipo II/metabolismo
Miosina Tipo V/metabolismo
Nocodazol/farmacologia
Proteínas Nucleares/farmacologia
Moduladores de Tubulina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Microfilament Proteins); 0 (Nuclear Proteins); 0 (Tubulin Modulators); 0 (formin 2, mouse); EC 3.6.1.- (Myosin Type II); EC 3.6.1.- (Myosin Type V); SH1WY3R615 (Nocodazole)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150317
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3131


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[PMID]:25637016
[Au] Autor:Arvidsson I; Ståhl AL; Hedström MM; Kristoffersson AC; Rylander C; Westman JS; Storry JR; Olsson ML; Karpman D
[Ad] Endereço:Department of Pediatrics, Clinical Sciences Lund, Lund University, 22184 Lund, Sweden;
[Ti] Título:Shiga toxin-induced complement-mediated hemolysis and release of complement-coated red blood cell-derived microvesicles in hemolytic uremic syndrome.
[So] Source:J Immunol;194(5):2309-18, 2015 Mar 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Shiga toxin (Stx)-producing Escherichia coli (STEC) cause hemolytic uremic syndrome (HUS). This study investigated whether Stx2 induces hemolysis and whether complement is involved in the hemolytic process. RBCs and/or RBC-derived microvesicles from patients with STEC-HUS (n = 25) were investigated for the presence of C3 and C9 by flow cytometry. Patients exhibited increased C3 deposition on RBCs compared with controls (p < 0.001), as well as high levels of C3- and C9-bearing RBC-derived microvesicles during the acute phase, which decreased after recovery. Stx2 bound to P1 (k) and P2 (k) phenotype RBCs, expressing high levels of the P(k) Ag (globotriaosylceramide), the known Stx receptor. Stx2 induced the release of hemoglobin and lactate dehydrogenase in whole blood, indicating hemolysis. Stx2-induced hemolysis was not demonstrated in the absence of plasma and was inhibited by heat inactivation, as well as by the terminal complement pathway Ab eculizumab, the purinergic P2 receptor antagonist suramin, and EDTA. In the presence of whole blood or plasma/serum, Stx2 induced the release of RBC-derived microvesicles coated with C5b-9, a process that was inhibited by EDTA, in the absence of factor B, and by purinergic P2 receptor antagonists. Thus, complement-coated RBC-derived microvesicles are elevated in HUS patients and induced in vitro by incubation of RBCs with Stx2, which also induced hemolysis. The role of complement in Stx2-mediated hemolysis was demonstrated by its occurrence only in the presence of plasma and its abrogation by heat inactivation, EDTA, and eculizumab. Complement activation on RBCs could play a role in the hemolytic process occurring during STEC-HUS.
[Mh] Termos MeSH primário: Vesículas Revestidas/efeitos dos fármacos
Eritrócitos/efeitos dos fármacos
Infecções por Escherichia coli/sangue
Escherichia coli O157/patogenicidade
Síndrome Hemolítico-Urêmica/sangue
Toxina Shiga/toxicidade
[Mh] Termos MeSH secundário: Adulto
Idoso
Anticorpos Monoclonais Humanizados/farmacologia
Criança
Pré-Escolar
Vesículas Revestidas/química
Vesículas Revestidas/imunologia
Ativação do Complemento/efeitos dos fármacos
Complemento C3/química
Complemento C9/química
Complexo de Ataque à Membrana do Sistema Complemento/química
Ácido Edético/farmacologia
Eritrócitos/química
Eritrócitos/imunologia
Eritrócitos/patologia
Infecções por Escherichia coli/imunologia
Infecções por Escherichia coli/microbiologia
Infecções por Escherichia coli/patologia
Escherichia coli O157/imunologia
Escherichia coli O157/metabolismo
Feminino
Expressão Gênica
Hemólise/efeitos dos fármacos
Síndrome Hemolítico-Urêmica/imunologia
Síndrome Hemolítico-Urêmica/microbiologia
Síndrome Hemolítico-Urêmica/patologia
Seres Humanos
Lactente
L-Lactato Desidrogenase/secreção
Masculino
Meia-Idade
Antagonistas do Receptor Purinérgico P2/farmacologia
Receptores Purinérgicos P2/genética
Receptores Purinérgicos P2/imunologia
Toxina Shiga/química
Toxina Shiga/imunologia
Suramina/farmacologia
Triexosilceramidas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal, Humanized); 0 (Complement C3); 0 (Complement C9); 0 (Complement Membrane Attack Complex); 0 (Purinergic P2 Receptor Antagonists); 0 (Receptors, Purinergic P2); 0 (Trihexosylceramides); 6032D45BEM (Suramin); 71965-57-6 (globotriaosylceramide); 75757-64-1 (Shiga Toxin); 9G34HU7RV0 (Edetic Acid); A3ULP0F556 (eculizumab); EC 1.1.1.27 (L-Lactate Dehydrogenase)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:150225
[Lr] Data última revisão:
150225
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:150201
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1402470


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[PMID]:25004848
[Au] Autor:Shami G; Cheng D; Henriquez J; Braet F
[Ad] Endereço:School of Medical Sciences (Discipline of Anatomy and Histology) - The Bosch Institute, The University of Sydney, NSW 2006, Australia. Electronic address: gerryshami@gmail.com.
[Ti] Título:Assessment of different fixation protocols on the presence of membrane-bound vesicles in Caco-2 cells: a multidimensional view by means of correlative light and 3-D transmission electron microscopy.
[So] Source:Micron;67:20-29, 2014 Dec.
[Is] ISSN:1878-4291
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Herein, we present a comparative analysis of a variety of chemical and physical fixation protocols for the specific visualisation of the membrane-bound vesicles (MBVs) in the Caco-2 colorectal cancer (CRC) cell line. In so doing, we validated the applicability of specific specimen preparation protocols for the preservation and contrasting of membrane-associated vesicles. Next, by employing the best respective chemical (GOT) and physical (SHPF) fixation methods for the application of transmission electron tomography and modelling we were able to characterise MBVs in three-dimensions and at the nanometer scale. In the second part of this study, we employ a correlative light and electron microscopy (CLEM) approach in order to determine which vesicular compartments are implicated in the uptake of FITC-BSA as a model protein drug. In so doing, we provide a solid foundation for future studies investigating chemotherapeutic drug uptake, transport and fate in cancer cell lines.
[Mh] Termos MeSH primário: Células CACO-2/ultraestrutura
Vesículas Citoplasmáticas/ultraestrutura
Microscopia Eletrônica de Transmissão/métodos
Microscopia/métodos
Fixação de Tecidos/métodos
[Mh] Termos MeSH secundário: Albuminas/metabolismo
Albuminas/ultraestrutura
Clatrina/metabolismo
Clatrina/ultraestrutura
Vesículas Revestidas/ultraestrutura
Criopreservação/métodos
Fixadores
Glutaral
Seres Humanos
Imagem Tridimensional/métodos
Tetróxido de Ósmio
Taninos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Albumins); 0 (Clathrin); 0 (Fixatives); 0 (Tannins); P40W033BGM (Osmium Tetroxide); T3C89M417N (Glutaral)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140710
[St] Status:MEDLINE


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[PMID]:24844592
[Au] Autor:Paul P; Simm S; Mirus O; Scharf KD; Fragkostefanakis S; Schleiff E
[Ad] Endereço:Department of Biosciences Molecular Cell Biology of Plants.
[Ti] Título:The complexity of vesicle transport factors in plants examined by orthology search.
[So] Source:PLoS One;9(5):e97745, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Vesicle transport is a central process to ensure protein and lipid distribution in eukaryotic cells. The current knowledge on the molecular components and mechanisms of this process is majorly based on studies in Saccharomyces cerevisiae and Arabidopsis thaliana, which revealed 240 different proteinaceous factors either experimentally proven or predicted to be involved in vesicle transport. In here, we performed an orthologue search using two different algorithms to identify the components of the secretory pathway in yeast and 14 plant genomes by using the 'core-set' of 240 factors as bait. We identified 4021 orthologues and (co-)orthologues in the discussed plant species accounting for components of COP-II, COP-I, Clathrin Coated Vesicles, Retromers and ESCRTs, Rab GTPases, Tethering factors and SNAREs. In plants, we observed a significantly higher number of (co-)orthologues than yeast, while only 8 tethering factors from yeast seem to be absent in the analyzed plant genomes. To link the identified (co-)orthologues to vesicle transport, the domain architecture of the proteins from yeast, genetic model plant A. thaliana and agriculturally relevant crop Solanum lycopersicum has been inspected. For the orthologous groups containing (co-)orthologues from yeast, A. thaliana and S. lycopersicum, we observed the same domain architecture for 79% (416/527) of the (co-)orthologues, which documents a very high conservation of this process. Further, publically available tissue-specific expression profiles for a subset of (co-)orthologues found in A. thaliana and S. lycopersicum suggest that some (co-)orthologues are involved in tissue-specific functions. Inspection of localization of the (co-)orthologues based on available proteome data or localization predictions lead to the assignment of plastid- as well as mitochondrial localized (co-)orthologues of vesicle transport factors and the relevance of this is discussed.
[Mh] Termos MeSH primário: Fenômenos Fisiológicos Vegetais
Vesículas Transportadoras/fisiologia
[Mh] Termos MeSH secundário: Transporte Biológico
Vesículas Revestidas/fisiologia
Biologia Computacional
Bases de Dados Factuais
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Proteínas SNARE/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Endosomal Sorting Complexes Required for Transport); 0 (SNARE Proteins); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140522
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0097745


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[PMID]:24641164
[Au] Autor:Lam AT; Li J; Chen AK; Reuveny S; Oh SK; Birch WR
[Ad] Endereço:1 Stem Cell Group, Bioprocessing Technology Institute , Agency for Science, Technology and Research (A*STAR), Singapore , Singapore.
[Ti] Título:Cationic surface charge combined with either vitronectin or laminin dictates the evolution of human embryonic stem cells/microcarrier aggregates and cell growth in agitated cultures.
[So] Source:Stem Cells Dev;23(14):1688-703, 2014 Jul 15.
[Is] ISSN:1557-8534
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The expansion of human pluripotent stem cells (hPSC) for biomedical applications generally compels a defined, reliable, and scalable platform. Bioreactors offer a three-dimensional culture environment that relies on the implementation of microcarriers (MC), as supports for cell anchorage and their subsequent growth. Polystyrene microspheres/MC coated with adhesion-promoting extracellular matrix (ECM) protein, vitronectin (VN), or laminin (LN) have been shown to support hPSC expansion in a static environment. However, they are insufficient to promote human embryonic stem cells (hESC) seeding and their expansion in an agitated environment. The present study describes an innovative technology, consisting of a cationic charge that underlies the ECM coatings. By combining poly-L-lysine (PLL) with a coating of ECM protein, cell attachment efficiency and cell spreading are improved, thus enabling seeding under agitation in a serum-free medium. This coating combination also critically enables the subsequent formation and evolution of hPSC/MC aggregates, which ensure cell viability and generate high yields. Aggregate dimensions of at least 300 µm during early cell growth give rise to ≈15-fold expansion at 7 days' culture. Increasing aggregate numbers at a quasi-constant size of ≈300 µm indicates hESC growth within a self-regulating microenvironment. PLL+LN enables cell seeding and aggregate evolution under constant agitation, whereas PLL+VN requires an intermediate 2-day static pause to attain comparable aggregate sizes and correspondingly high expansion yields. The cells' highly reproducible bioresponse to these defined and characterized MC surface properties is universal across multiple cell lines, thus confirming the robustness of this scalable expansion process in a defined environment.
[Mh] Termos MeSH primário: Técnicas de Cultura de Células
Células-Tronco Embrionárias/efeitos dos fármacos
Laminina/administração & dosagem
Células-Tronco Pluripotentes/efeitos dos fármacos
Vitronectina/administração & dosagem
[Mh] Termos MeSH secundário: Reatores Biológicos
Proliferação Celular/efeitos dos fármacos
Microambiente Celular/efeitos dos fármacos
Vesículas Revestidas/química
Meios de Cultura Livres de Soro
Células-Tronco Embrionárias/citologia
Matriz Extracelular/metabolismo
Seres Humanos
Laminina/química
Laminina/metabolismo
Lisina/química
Microesferas
Células-Tronco Pluripotentes/citologia
Vitronectina/química
Vitronectina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Culture Media, Serum-Free); 0 (Laminin); 0 (Vitronectin); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140320
[St] Status:MEDLINE
[do] DOI:10.1089/scd.2013.0645



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