Base de dados : MEDLINE
Pesquisa : G04.417 [Categoria DeCS]
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  1 / 25151 MEDLINE  
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[PMID]:29200852
[Au] Autor:Hu Y; Ke L; Chen H; Zhuo M; Yang X; Zhao D; Zeng S; Xiao X
[Ad] Endereço:Department of Pharmaceutics, School of Pharmaceutical Science, South-Central University for Nationalities.
[Ti] Título:Natural material-decorated mesoporous silica nanoparticle container for multifunctional membrane-controlled targeted drug delivery.
[So] Source:Int J Nanomedicine;12:8411-8426, 2017.
[Is] ISSN:1178-2013
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:To avoid the side effects caused by nonspecific targeting, premature release, weak selectivity, and poor therapeutic efficacy of current nanoparticle-based systems used for drug delivery, we fabricated natural material-decorated nanoparticles as a multifunctional, membrane-controlled targeted drug delivery system. The nanocomposite material coated with a membrane was biocompatible and integrated both specific tumor targeting and responsiveness to stimulation, which improved transmission efficacy and controlled drug release. Mesoporous silica nanoparticles (MSNs), which are known for their biocompatibility and high drug-loading capacity, were selected as a model drug container and carrier. The membrane was established by the polyelectrolyte composite method from chitosan (CS) which was sensitive to the acidic tumor microenvironment, folic acid-modified CS which recognizes the folate receptor expressed on the tumor cell surface, and a CD receptor-targeted polysaccharide hyaluronic acid. We characterized the structure of the nanocomposite as well as the drug release behavior under the control of the pH-sensitive membrane switch and evaluated the antitumor efficacy of the system in vitro. Our results provide a basis for the design and fabrication of novel membrane-controlled nanoparticles with improved tumor-targeting therapy.
[Mh] Termos MeSH primário: Materiais Biocompatíveis/química
Sistemas de Liberação de Medicamentos
Membranas Artificiais
Nanopartículas/química
Dióxido de Silício/química
[Mh] Termos MeSH secundário: Morte Celular
Quitosana/química
Liberação Controlada de Fármacos
Endocitose
Ácido Fólico/química
Células Hep G2
Seres Humanos
Nanopartículas/ultraestrutura
Tamanho da Partícula
Porosidade
Espectroscopia de Infravermelho com Transformada de Fourier
Eletricidade Estática
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biocompatible Materials); 0 (Membranes, Artificial); 7631-86-9 (Silicon Dioxide); 9012-76-4 (Chitosan); 935E97BOY8 (Folic Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.2147/IJN.S148438


  2 / 25151 MEDLINE  
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[PMID]:29362354
[Au] Autor:Garcia-Alai MM; Heidemann J; Skruzny M; Gieras A; Mertens HDT; Svergun DI; Kaksonen M; Uetrecht C; Meijers R
[Ad] Endereço:European Molecular Biology Laboratory (EMBL), Hamburg Outstation, Notkestrasse 85, 22607, Hamburg, Germany.
[Ti] Título:Epsin and Sla2 form assemblies through phospholipid interfaces.
[So] Source:Nat Commun;9(1):328, 2018 01 23.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In clathrin-mediated endocytosis, adapter proteins assemble together with clathrin through interactions with specific lipids on the plasma membrane. However, the precise mechanism of adapter protein assembly at the cell membrane is still unknown. Here, we show that the membrane-proximal domains ENTH of epsin and ANTH of Sla2 form complexes through phosphatidylinositol 4,5-bisphosphate (PIP2) lipid interfaces. Native mass spectrometry reveals how ENTH and ANTH domains form assemblies by sharing PIP2 molecules. Furthermore, crystal structures of epsin Ent2 ENTH domain from S. cerevisiae in complex with PIP2 and Sla2 ANTH domain from C. thermophilum illustrate how allosteric phospholipid binding occurs. A comparison with human ENTH and ANTH domains reveal only the human ENTH domain can form a stable hexameric core in presence of PIP2, which could explain functional differences between fungal and human epsins. We propose a general phospholipid-driven multifaceted assembly mechanism tolerating different adapter protein compositions to induce endocytosis.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Fúngicas/química
Fosfatidilinositol 4,5-Difosfato/química
Domínios Proteicos
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/genética
Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Sequência de Aminoácidos
Sítios de Ligação/genética
Membrana Celular/metabolismo
Chaetomium/genética
Chaetomium/metabolismo
Cristalografia por Raios X
Endocitose
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Seres Humanos
Modelos Moleculares
Fosfatidilinositol 4,5-Difosfato/metabolismo
Ligação Proteica
Multimerização Proteica
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Fungal Proteins); 0 (Phosphatidylinositol 4,5-Diphosphate); 0 (epsin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180125
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02443-x


  3 / 25151 MEDLINE  
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[PMID]:28460472
[Au] Autor:Å Urga S; Nanut MP; Kos J; Sabotic J
[Ad] Endereço:Department of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
[Ti] Título:Fungal lectin MpL enables entry of protein drugs into cancer cells and their subcellular targeting.
[So] Source:Oncotarget;8(16):26896-26910, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lectins have been recognized as promising carrier molecules for targeted drug delivery. They specifically bind carbohydrate moieties on cell membranes and trigger cell internalization. Fungal lectin MpL (Macrolepiota procera lectin) does not provoke cancer cell cytotoxicity but is able to bind aminopeptidase N (CD13) and integrin α3ß1, two glycoproteins that are overexpressed on the membrane of tumor cells. Upon binding, MpL is endocytosed in a clathrin-dependent manner and accumulates initially in the Golgi apparatus and, finally, in the lysosomes. For effective binding and internalization a functional binding site on the α-repeat is needed. To test the potential of MpL as a carrier for delivering protein drugs to cancer cells we constructed fusion proteins consisting of MpL and the cysteine peptidase inhibitors cystatin C and clitocypin. The fused proteins followed the same endocytic route as the unlinked MpL. Peptidase inhibitor-MpL fusions impaired both the intracellular degradation of extracellular matrix and the invasiveness of cancer cells. MpL is thus shown in vitro to be a lectin that can enable protein drugs to enter cancer cells, enhance their internalization and sort them to lysosomes and the Golgi apparatus.
[Mh] Termos MeSH primário: Portadores de Fármacos
Proteínas Fúngicas/metabolismo
Lectinas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Membrana Celular/metabolismo
Colágeno Tipo IV/metabolismo
Endocitose
Glicoproteínas/metabolismo
Seres Humanos
Espaço Intracelular/metabolismo
Ligação Proteica
Transporte Proteico
Proteólise
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type IV); 0 (Drug Carriers); 0 (Fungal Proteins); 0 (Glycoproteins); 0 (Lectins); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15849


  4 / 25151 MEDLINE  
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[PMID]:28455282
[Au] Autor:Sim X; Jarocha D; Hayes V; Hanby HA; Marks MS; Camire RM; French DL; Poncz M; Gadue P
[Ad] Endereço:Department of Cell and Molecular Biology, University of Pennsylvania School of Medicine, Philadelphia, PA.
[Ti] Título:Identifying and enriching platelet-producing human stem cell-derived megakaryocytes using factor V uptake.
[So] Source:Blood;130(2):192-204, 2017 07 13.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stem cell-derived platelets have the potential to replace donor platelets for transfusion. Defining the platelet-producing megakaryocytes (MKs) within the heterogeneous MK culture may help to optimize the in vitro generation of platelets. Using 2 human stem cell models of megakaryopoiesis, we identified novel MK populations corresponding to distinct maturation stages. An immature, low granular (LG) MK pool (defined by side scatter on flow cytometry) gives rise to a mature high granular (HG) pool, which then becomes damaged by apoptosis and glycoprotein Ib α chain (CD42b) shedding. We define an undamaged HG/CD42b MK subpopulation, which endocytoses fluorescently labeled coagulation factor V (FV) from the media into α-granules and releases functional FV CD42b human platelet-like particles in vitro and when infused into immunodeficient mice. Importantly, these FV particles have the same size distribution as infused human donor platelets and are preferentially incorporated into clots after laser injury. Using drugs to protect HG MKs from apoptosis and CD42b shedding, we also demonstrate that apoptosis precedes CD42b shedding and that apoptosis inhibition enriches the FV HG/CD42b MKs, leading to increased platelet yield in vivo, but not in vitro. These studies identify a transition between distinct MK populations in vitro, including one that is primed for platelet release. Technologies to optimize and select these platelet-ready MKs may be important to efficiently generate functional platelets from in vitro-grown MKs.
[Mh] Termos MeSH primário: Plaquetas/citologia
Células da Medula Óssea/imunologia
Fator V/genética
Células Progenitoras de Megacariócitos/citologia
Megacariócitos/citologia
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Arteríolas/efeitos dos fármacos
Arteríolas/imunologia
Arteríolas/lesões
Biomarcadores/sangue
Plaquetas/imunologia
Células da Medula Óssea/citologia
Células da Medula Óssea/efeitos dos fármacos
Diferenciação Celular
Linhagem da Célula/imunologia
Endocitose
Fator V/imunologia
Fator V/farmacologia
Citometria de Fluxo
Expressão Gênica
Seres Humanos
Imunofenotipagem
Lasers
Células Progenitoras de Megacariócitos/imunologia
Megacariócitos/imunologia
Camundongos
Camundongos SCID
Complexo Glicoproteico GPIb-IX de Plaquetas/genética
Complexo Glicoproteico GPIb-IX de Plaquetas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Biomarkers); 0 (Platelet Glycoprotein GPIb-IX Complex); 9001-24-5 (Factor V)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180228
[Lr] Data última revisão:
180228
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-01-761049


  5 / 25151 MEDLINE  
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[PMID]:29317633
[Au] Autor:Guo P; Liu D; Subramanyam K; Wang B; Yang J; Huang J; Auguste DT; Moses MA
[Ad] Endereço:Vascular Biology Program, Boston Children's Hospital, 300 Longwood Avenue, Boston, MA, 02115, USA.
[Ti] Título:Nanoparticle elasticity directs tumor uptake.
[So] Source:Nat Commun;9(1):130, 2018 01 09.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:To date, the role of elasticity in drug delivery remains elusive due to the inability to measure microscale mechanics and alter rheology without affecting chemistry. Herein, we describe the in vitro cellular uptake and in vivo tumor uptake of nanolipogels (NLGs). NLGs are composed of identical lipid bilayers encapsulating an alginate core, with tunable elasticity. The elasticity of NLGs was evaluated by atomic force microscopy, which demonstrated that they exhibit Young's moduli ranging from 45 ± 9 to 19,000 ± 5 kPa. Neoplastic and non-neoplastic cells exhibited significantly greater uptake of soft NLGs (Young's modulus <1.6 MPa) relative to their elastic counterparts (Young's modulus >13.8 MPa). In an orthotopic breast tumor model, soft NLGs accumulated significantly more in tumors, whereas elastic NLGs preferentially accumulated in the liver. Our findings demonstrate that particle elasticity directs tumor accumulation, suggesting that it may be a design parameter to enhance tumor delivery efficiency.
[Mh] Termos MeSH primário: Neoplasias da Mama/metabolismo
Módulo de Elasticidade
Nanopartículas/química
Nanopartículas/metabolismo
[Mh] Termos MeSH secundário: Animais
Neoplasias da Mama/patologia
Linhagem Celular
Linhagem Celular Tumoral
Clorpromazina/farmacologia
Endocitose/efeitos dos fármacos
Filipina/farmacologia
Seres Humanos
Hidrazonas/farmacologia
Fígado/metabolismo
Células MCF-7
Neoplasias Mamárias Experimentais/metabolismo
Camundongos Endogâmicos BALB C
Microscopia de Força Atômica
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Hydrazones); 0 (N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide); 87Z59R7D14 (Filipin); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02588-9


  6 / 25151 MEDLINE  
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[PMID]:28467637
[Au] Autor:Li X; Zhou M; Huang W; Yang H
[Ad] Endereço:Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.
[Ti] Título:N-glycosylation of the ß adrenergic receptor regulates receptor function by modulating dimerization.
[So] Source:FEBS J;284(13):2004-2018, 2017 07.
[Is] ISSN:1742-4658
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:N-glycosylation is a common post-translational modification of G-protein-coupled receptors (GPCRs). However, it remains unknown how N-glycosylation affects GPCR signaling. ß adrenergic receptor (ß AR) has three N-glycosylation sites: Asn6, Asn15 at the N-terminus, and Asn187 at the second extracellular loop (ECL2). Here, we show that deletion of the N-glycan did not affect receptor expression and ligand binding. Deletion of the N-glycan at the N-terminus rather than Asn187 showed decreased effects on isoproterenol-promoted G-protein-dependent signaling, ß-arrestin2 recruitment, and receptor internalization. Both N6Q and N15Q showed decreased receptor dimerization, while N187Q did not influence receptor dimerization. As decreased ß AR homodimer accompanied with reduced efficiency for receptor function, we proposed that the N-glycosylation of ß AR regulated receptor function by influencing receptor dimerization. To verify this hypothesis, we further paid attention to the residues at the dimerization interface. Studies of Lys60 and Glu338, two residues at the receptor dimerization interface, exhibited that the K60A/E338A showed decreased ß AR dimerization and its effects on receptor signaling were similar to N6Q and N15Q, which further supported the importance of receptor dimerization for receptor function. This work provides new insights into the relationship among glycosylation, dimerization, and function of GPCRs. ENZYMES: Peptide-N-glycosidase F (PNGase F, EC 3.2.2.11); endo-ß-N-acetylglucosaminidase A (Endo-A, EC 3.2.1.96).
[Mh] Termos MeSH primário: Multimerização Proteica
Receptores Adrenérgicos beta 2/química
Receptores Adrenérgicos beta 2/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Agonistas Adrenérgicos beta/farmacologia
Sítios de Ligação/genética
Western Blotting
Endocitose/efeitos dos fármacos
Glicosilação
Células HEK293
Seres Humanos
Isoproterenol/farmacologia
Microscopia Confocal
Mutação
Polissacarídeos/metabolismo
Processamento de Proteína Pós-Traducional
Receptores Adrenérgicos beta 2/genética
beta-Arrestinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adrenergic beta-Agonists); 0 (Polysaccharides); 0 (Receptors, Adrenergic, beta-2); 0 (beta-Arrestins); L628TT009W (Isoproterenol)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/febs.14098


  7 / 25151 MEDLINE  
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[PMID]:28460240
[Au] Autor:Lo Presti L; Kahmann R
[Ad] Endereço:Max Planck Institute for Terrestrial Microbiology, Dept. Organismic Interactions, Karl-von-Frisch-Strasse 10, 35043 Marburg, Germany.
[Ti] Título:How filamentous plant pathogen effectors are translocated to host cells.
[So] Source:Curr Opin Plant Biol;38:19-24, 2017 08.
[Is] ISSN:1879-0356
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The interaction of microbes with "signature" plants is largely governed by secreted effector proteins, which serve to dampen plant defense responses and modulate host cell processes. Secreted effectors can function either in the apoplast or within plant cell compartments. How oomycetes and fungi translocate their effectors to plant cells is still poorly understood and controversial. While most oomycete effectors share a common 'signature' that was proposed to mediate their uptake via endocytosis, fungal effectors display no conserved motifs at the primary amino acid sequence level. Here we summarize current knowledge in the field of oomycete and fungal effector uptake and highlight emerging themes that may unite rather than set apart these unrelated filamentous pathogens.
[Mh] Termos MeSH primário: Fungos/patogenicidade
Oomicetos/patogenicidade
Plantas/metabolismo
Plantas/microbiologia
[Mh] Termos MeSH secundário: Endocitose/genética
Endocitose/fisiologia
Interações Hospedeiro-Patógeno
Doenças das Plantas/genética
Doenças das Plantas/microbiologia
Plantas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE


  8 / 25151 MEDLINE  
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[PMID]:29233871
[Au] Autor:Fraser J; Cabodevilla AG; Simpson J; Gammoh N
[Ad] Endereço:Cancer Research UK Edinburgh Centre, Institute of Genetics and Molecular Medicine, University of Edinburgh, Crewe Road South, Edinburgh EH4 2XR, U.K.
[Ti] Título:Interplay of autophagy, receptor tyrosine kinase signalling and endocytic trafficking.
[So] Source:Essays Biochem;61(6):597-607, 2017 12 12.
[Is] ISSN:1744-1358
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Vesicular trafficking events play key roles in the compartmentalization and proper sorting of cellular components. These events have crucial roles in sensing external signals, regulating protein activities and stimulating cell growth or death decisions. Although mutations in vesicle trafficking players are not direct drivers of cellular transformation, their activities are important in facilitating oncogenic pathways. One such pathway is the sensing of external stimuli and signalling through receptor tyrosine kinases (RTKs). The regulation of RTK activity by the endocytic pathway has been extensively studied. Compelling recent studies have begun to highlight the association between autophagy and RTK signalling. The influence of this interplay on cellular status and its relevance in disease settings will be discussed here.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Endocitose/fisiologia
Receptores Proteína Tirosina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia/genética
Endocitose/genética
Seres Humanos
Neoplasias/genética
Neoplasias/metabolismo
Receptores Proteína Tirosina Quinases/genética
Transdução de Sinais/genética
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.1042/EBC20170091


  9 / 25151 MEDLINE  
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[PMID]:28449430
[Au] Autor:Li S; Xiong Y; Zhang X
[Ad] Endereço:Department of Bone and Soft Tissue Tumor Surgery, Cancer Hospital of China Medical University, Liaoning Cancer Hospital & Institute, Shenyang, Liaoning Province 110042, China.
[Ti] Título:Poloxamer surface modified trimethyl chitosan nanoparticles for the effective delivery of methotrexate in osteosarcoma.
[So] Source:Biomed Pharmacother;90:872-879, 2017 Jun.
[Is] ISSN:1950-6007
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The present work is an effort to explore the poloxamer-modified trimethyl chitosan (TMC) encapsulated MTX for osteosarcoma treatment in order to improve the therapeutic efficacy and minimize severe toxicity associated with the clinical usage of MTX. The methotrexate-loaded pluronic-chitosan nanoparticles (MTCN) was nanosized and exhibited a controlled release of drug from the carrier system. The MTCN showed higher accumulation in cell cytoplasm region evident by the high red fluorescence indicating its uptake through energy-dependent endocytosis process. MTCN exhibited the increased cytotoxicity in MG63 cells compared free MTX due to its enhanced cellular uptake. Especially, MTCN exhibited a superior apoptosis effect with bright chromatin condensation and nuclear fragmentation was observed and showed remarkably higher apoptosis (∼48%) compared to that of free drug. The results of this investigation clearly demonstrate that the poloxamer-modified trimethyl chitosan (TMC) seems to have a great potential as a drug carrier in cancer chemotherapy. The present research work offers immense scope for further exploitation of poloxamer-modified trimethyl chitosan (TMC) in future for the development of nanoparticulate drug delivery system for cancer chemotherapy.
[Mh] Termos MeSH primário: Neoplasias Ósseas/tratamento farmacológico
Quitosana/análogos & derivados
Metotrexato/administração & dosagem
Metotrexato/química
Nanopartículas/química
Osteossarcoma/tratamento farmacológico
Poloxâmero/química
[Mh] Termos MeSH secundário: Antineoplásicos/administração & dosagem
Antineoplásicos/química
Linhagem Celular Tumoral
Quitosana/química
Portadores de Fármacos/química
Sistemas de Liberação de Medicamentos/métodos
Endocitose/efeitos dos fármacos
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Drug Carriers); 0 (pluronic-chitosan); 106392-12-5 (Poloxamer); 9012-76-4 (Chitosan); YL5FZ2Y5U1 (Methotrexate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  10 / 25151 MEDLINE  
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[PMID]:28451521
[Au] Autor:Stolle AS; Norkowski S; Körner B; Schmitz J; Lüken L; Frankenberg M; Rüter C; Schmidt MA
[Ad] Endereço:Institute of Infectiology, Center for Molecular Biology of Inflammation, University of MünsterMünster, Germany.
[Ti] Título:T3SS-Independent Uptake of the Short-Trip Toxin-Related Recombinant NleC Effector of Enteropathogenic Leads to NF-κB p65 Cleavage.
[So] Source:Front Cell Infect Microbiol;7:119, 2017.
[Is] ISSN:2235-2988
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Effector proteins secreted by the type 3 secretion system (T3SS) of pathogenic bacteria have been shown to precisely modulate important signaling cascades of the host for the benefit of the pathogens. Among others, the non-LEE encoded T3SS effector protein NleC of enteropathogenic (EPEC) is a Zn-dependent metalloprotease and suppresses innate immune responses by directly targeting the NF-κB signaling pathway. Many pathogenic bacteria release potent bacterial toxins of the A-B type, which-in contrast to the direct cytoplasmic injection of T3SS effector proteins-are released first into the environment. In this study, we found that NleC displays characteristics of bacterial A-B toxins, when applied to eukaryotic cells as a recombinant protein. Although lacking a B subunit, that typically mediates the uptake of toxins, recombinant NleC (rNleC) induces endocytosis via lipid rafts and follows the endosomal-lysosomal pathway. The conformation of rNleC is altered by low pH to facilitate its escape from acidified endosomes. This is reminiscent of the homologous A-B toxin AIP56 of the fish pathogen ( ). The recombinant protease NleC is functional inside eukaryotic cells and cleaves p65 of the NF-κB pathway. Here, we describe the endocytic uptake mechanism of rNleC, characterize its intracellular trafficking and demonstrate that its specific activity of cleaving p65 requires activation of host cells e.g., by IL1ß. Further, we propose an evolutionary link between some T3SS effector proteins and bacterial toxins from apparently unrelated bacteria. In summary, these properties might suggest rNleC as an interesting candidate for future applications as a potential therapeutic against immune disorders.
[Mh] Termos MeSH primário: Escherichia coli Enteropatogênica/genética
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/toxicidade
Proteínas Recombinantes
Fator de Transcrição RelA/metabolismo
Sistemas de Secreção Tipo III/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Toxinas Bacterianas/metabolismo
Endocitose/efeitos dos fármacos
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/metabolismo
Proteínas de Escherichia coli/fisiologia
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Concentração de Íons de Hidrogênio
Interleucina-1beta
Lisossomos/efeitos dos fármacos
NF-kappa B/metabolismo
Photobacterium/metabolismo
Domínios Proteicos
Estrutura Secundária de Proteína
Transporte Proteico
Alinhamento de Sequência
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Toxins); 0 (Escherichia coli Proteins); 0 (Interleukin-1beta); 0 (NF-kappa B); 0 (RELA protein, human); 0 (Recombinant Proteins); 0 (Transcription Factor RelA); 0 (Type III Secretion Systems); 0 (Z0986 protein, E coli)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.3389/fcimb.2017.00119



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