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Pesquisa : A11.284.420 [Categoria DeCS]
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[PMID]:28467905
[Au] Autor:Ramdzan YM; Trubetskov MM; Ormsby AR; Newcombe EA; Sui X; Tobin MJ; Bongiovanni MN; Gras SL; Dewson G; Miller JML; Finkbeiner S; Moily NS; Niclis J; Parish CL; Purcell AW; Baker MJ; Wilce JA; Waris S; Stojanovski D; Böcking T; Ang CS; Ascher DB; Reid GE; Hatters DM
[Ad] Endereço:Department of Biochemistry and Molecular Biology and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, VIC 3010, Australia.
[Ti] Título:Huntingtin Inclusions Trigger Cellular Quiescence, Deactivate Apoptosis, and Lead to Delayed Necrosis.
[So] Source:Cell Rep;19(5):919-927, 2017 May 02.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Competing models exist in the literature for the relationship between mutant Huntingtin exon 1 (Httex1) inclusion formation and toxicity. In one, inclusions are adaptive by sequestering the proteotoxicity of soluble Httex1. In the other, inclusions compromise cellular activity as a result of proteome co-aggregation. Using a biosensor of Httex1 conformation in mammalian cell models, we discovered a mechanism that reconciles these competing models. Newly formed inclusions were composed of disordered Httex1 and ribonucleoproteins. As inclusions matured, Httex1 reconfigured into amyloid, and other glutamine-rich and prion domain-containing proteins were recruited. Soluble Httex1 caused a hyperpolarized mitochondrial membrane potential, increased reactive oxygen species, and promoted apoptosis. Inclusion formation triggered a collapsed mitochondrial potential, cellular quiescence, and deactivated apoptosis. We propose a revised model where sequestration of soluble Httex1 inclusions can remove the trigger for apoptosis but also co-aggregate other proteins, which curtails cellular metabolism and leads to a slow death by necrosis.
[Mh] Termos MeSH primário: Amiloide/metabolismo
Apoptose
Proteína Huntingtina/genética
[Mh] Termos MeSH secundário: Éxons
Células HEK293
Células HeLa
Seres Humanos
Proteína Huntingtina/metabolismo
Corpos de Inclusão/metabolismo
Potencial da Membrana Mitocondrial
Mutação
Espécies Reativas de Oxigênio/metabolismo
Ribonucleoproteínas/genética
Ribonucleoproteínas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid); 0 (HTT protein, human); 0 (Huntingtin Protein); 0 (Reactive Oxygen Species); 0 (Ribonucleoproteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180213
[Lr] Data última revisão:
180213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  2 / 12513 MEDLINE  
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[PMID]:28743267
[Au] Autor:Valdez-Cruz NA; Reynoso-Cereceda GI; Pérez-Rodriguez S; Restrepo-Pineda S; González-Santana J; Olvera A; Zavala G; Alagón A; Trujillo-Roldán MA
[Ad] Endereço:Programa de Investigación de Producción de Biomoléculas, Unidad de Bioprocesos, Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, AP. 70228, CP 04510, Mexico City, Mexico. adrivaldez1@gmail.com.
[Ti] Título:Production of a recombinant phospholipase A2 in Escherichia coli using resonant acoustic mixing that improves oxygen transfer in shake flasks.
[So] Source:Microb Cell Fact;16(1):129, 2017 Jul 25.
[Is] ISSN:1475-2859
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Shake flasks are widely used during the development of bioprocesses for recombinant proteins. Cultures of recombinant Escherichia coli with orbital mixing (OM) have an oxygen limitation negatively affecting biomass growth and recombinant-protein production. With the aim to improve mixing and aeration in shake flask cultures, we analyzed cultures subjected to OM and the novel resonant acoustic mixing (RAM) by applying acoustic energy to E. coli BL21-Gold (DE3): a producer of recombinant phospholipase A2 (rPLA2) from Micrurus laticollaris snake venom. RESULTS: Comparing OM with RAM (200 rpm vs. 7.5g) at the same initial volumetric oxygen transfer coefficient (k a ≈ 80 h ) ~69% less biomass was obtained with OM compared with RAM. We analyzed two more conditions increasing agitation until maximal speed (12.5 and 20g), and ~1.6- and ~1.4-fold greater biomass was obtained as compared with cultures at 7.5g. Moreover, the specific growth rate was statistically similar in all cultures carried out in RAM, but ~1.5-fold higher than that in cultures carried out under OM. Almost half of the glucose was consumed in OM, whereas between 80 and 100% of the glucose was consumed in RAM cultures, doubling biomass per glucose yields. Differential organic acid production was observed, but acetate production was prevented at the maximal RAM (20g). The amount of rPLA2 in both, OM and RAM cultures, represented 38 ± 5% of the insoluble protein. A smaller proportion of α-helices and ß-sheet of purified inclusion bodies (IBs) were appreciated by ATR-FTIR from cultures carried out under OM, than those from RAM. At maximal agitation by RAM, internal E. coli localization patterns of protein aggregation changed, as well as, IBs proteolytic degradation, in conjunction with the formation of small external vesicles, although these changes did not significantly affect the cell survival response. CONCLUSIONS: In moderate-cell-density recombinant E. coli BL21-Gold (DE3) cultures, the agitation increases in RAM (up to the maximum) was not enough to avoid the classical oxygen limitation that happens in OM shake flasks. However, RAM presents a decrease of oxygen limitation, resulting in a favorable effect on biomass growth and volumetric rPLA2 production. While under OM a higher recombinant protein yield was obtained.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Oxigênio/metabolismo
Fosfolipases A2/metabolismo
[Mh] Termos MeSH secundário: Técnicas de Cultura Celular por Lotes
Escherichia coli/crescimento & desenvolvimento
Glucose/metabolismo
Corpos de Inclusão/genética
Corpos de Inclusão/metabolismo
Cinética
Microscopia Eletrônica de Transmissão
Fosfolipases A2/genética
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Recombinant Proteins); EC 3.1.1.4 (Phospholipases A2); IY9XDZ35W2 (Glucose); S88TT14065 (Oxygen)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1186/s12934-017-0746-1


  3 / 12513 MEDLINE  
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[PMID]:29186252
[Au] Autor:Antunes ACB; Véspoli ACG; Ferreira PS; Valente NYS
[Ad] Endereço:Department of Dermatology, Hospital das Clínicas, Faculdade de Medicina, Universidade de São Paulo (HC-FMUSP), São Paulo, SP, Brazil.
[Ti] Título:Pigmented Kamino bodies: a little-known histological finding. Prevalence in 19 cases of Reed nevus.
[So] Source:An Bras Dermatol;92(3):379-382, 2017 May-Jun.
[Is] ISSN:1806-4841
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:The present study aimed to determine the prevalence of Kamino bodies in Reed nevus, since most studies to date show conflicting data on this issue. This was a retrospective observational study, in which the histopathology of 19 Reed nevus lesions were reviewed. The slides were stained by hematoxylin and eosin and periodic acid-Schiff, with a special focus placed on the identification of Kamino bodies. Some clinical data were also collected. The median patient age was 12 years (range of 2 to 58). The women to men ratio was 5:4. Lesions were located on different parts of the body. Kamino bodies were found in eleven lesions (57.89%). five showed pigmented Kamino bodies (26.31%), four non-pigmented Kamino bodies (21,05%), and 2 (10.52%) had both. Kamino bodies, pigmented or not, are a common histological finding in Reed nevus and may well represent a good marker to differentiate these from malignant melanomas.
[Mh] Termos MeSH primário: Corpos de Inclusão/patologia
Nevo Pigmentado/patologia
Neoplasias Cutâneas/patologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Criança
Pré-Escolar
Feminino
Seres Humanos
Masculino
Meia-Idade
Prevalência
Estudos Retrospectivos
Coloração e Rotulagem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; OBSERVATIONAL STUDY
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180131
[Lr] Data última revisão:
180131
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE


  4 / 12513 MEDLINE  
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[PMID]:28465429
[Au] Autor:Wesolowski J; Weber MM; Nawrotek A; Dooley CA; Calderon M; St Croix CM; Hackstadt T; Cherfils J; Paumet F
[Ad] Endereço:Department of Microbiology and Immunology, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.
[Ti] Título: Hijacks ARF GTPases To Coordinate Microtubule Posttranslational Modifications and Golgi Complex Positioning.
[So] Source:MBio;8(3), 2017 May 02.
[Is] ISSN:2150-7511
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The intracellular bacterium develops in a parasitic compartment called the inclusion. Posttranslationally modified microtubules encase the inclusion, controlling the positioning of Golgi complex fragments around the inclusion. The molecular mechanisms by which coopts the host cytoskeleton and the Golgi complex to sustain its infectious compartment are unknown. Here, using a genetically modified strain, we discovered that both posttranslationally modified microtubules and Golgi complex positioning around the inclusion are controlled by the chlamydial inclusion protein CT813/CTL0184/InaC and host ARF GTPases. CT813 recruits ARF1 and ARF4 to the inclusion membrane, where they induce posttranslationally modified microtubules. Similarly, both ARF isoforms are required for the repositioning of Golgi complex fragments around the inclusion. We demonstrate that CT813 directly recruits ARF GTPases on the inclusion membrane and plays a pivotal role in their activation. Together, these results reveal that uses CT813 to hijack ARF GTPases to couple posttranslationally modified microtubules and Golgi complex repositioning at the inclusion. is an important cause of morbidity and a significant economic burden in the world. However, how develops its intracellular compartment, the so-called inclusion, is poorly understood. Using genetically engineered mutants, we discovered that the effector protein CT813 recruits and activates host ADP-ribosylation factor 1 (ARF1) and ARF4 to regulate microtubules. In this context, CT813 acts as a molecular platform that induces the posttranslational modification of microtubules around the inclusion. These cages are then used to reposition the Golgi complex during infection and promote the development of the inclusion. This study provides the first evidence that ARF1 and ARF4 play critical roles in controlling posttranslationally modified microtubules around the inclusion and that hijacks this novel function of ARF to reposition the Golgi complex.
[Mh] Termos MeSH primário: Proteínas de Bactérias/metabolismo
Chlamydia trachomatis/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Complexo de Golgi/metabolismo
Microtúbulos/metabolismo
[Mh] Termos MeSH secundário: Fator 1 de Ribosilação do ADP/metabolismo
Fatores de Ribosilação do ADP/metabolismo
Actinas
Proteínas de Bactérias/genética
Chlamydia trachomatis/genética
Complexo de Golgi/ultraestrutura
Células HeLa
Interações Hospedeiro-Patógeno
Seres Humanos
Corpos de Inclusão/microbiologia
Microtúbulos/genética
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Bacterial Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.2 (ADP-Ribosylation Factor 1); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ARF4 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180126
[Lr] Data última revisão:
180126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE


  5 / 12513 MEDLINE  
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[PMID]:29200148
[Au] Autor:Aoki T; Kunishima S; Yamashita Y; Minamitani K; Ota S
[Ad] Endereço:Department of Pediatrics, Teikyo University Chiba Medical Center, Chiba.
[Ti] Título:Macrothrombocytopenia With Congenital Bilateral Cataracts: A Phenotype of MYH9 Disorder With Exon 24 Indel Mutations.
[So] Source:J Pediatr Hematol Oncol;40(1):76-78, 2018 Jan.
[Is] ISSN:1536-3678
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:MYH9 disorder is characterized by large platelets and granulocyte inclusion bodies, and can be complicated with young-adult onsets of nephropathy, sensorineural hearing loss, and cataracts. Congenital cataracts in patients with MYH9 disorder is rare, and their etiology has not been elucidated. We report a 3-year-old patient with MYH9 disorder who had a p.E1066_A1072del mutation and developed cataracts congenitally. A review of the literature reveals that patients with an MYH9 exon 24 indel mutation, including p.E1066_A1072del, are susceptible to developing congenital cataracts and should be followed closely for other nonhematological complications.
[Mh] Termos MeSH primário: Catarata/congênito
Granulócitos/ultraestrutura
Mutação INDEL
Proteínas Motores Moleculares/genética
Cadeias Pesadas de Miosina/genética
Trombocitopenia/complicações
[Mh] Termos MeSH secundário: Plaquetas/patologia
Catarata/genética
Pré-Escolar
Éxons
Granulócitos/patologia
Perda Auditiva Neurossensorial
Seres Humanos
Corpos de Inclusão/patologia
Fenótipo
Trombocitopenia/congênito
Trombocitopenia/etiologia
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYH9 protein, human); 0 (Molecular Motor Proteins); EC 3.6.4.1 (Myosin Heavy Chains)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180112
[Lr] Data última revisão:
180112
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE
[do] DOI:10.1097/MPH.0000000000000998


  6 / 12513 MEDLINE  
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[PMID]:29186589
[Au] Autor:Gal J; Chen J; Katsumata Y; Fardo DW; Wang WX; Artiushin S; Price D; Anderson S; Patel E; Zhu H; Nelson PT
[Ad] Endereço:Department of Molecular and Cellular Biochemistry; Department of Biostatistics; Sanders-Brown Center on Aging; Department of Pathology, University of Kentucky, Lexington, Kentucky; and Research and Development, Lexington VA Medical Center, Lexington, Kentucky.
[Ti] Título:Detergent Insoluble Proteins and Inclusion Body-Like Structures Immunoreactive for PRKDC/DNA-PK/DNA-PKcs, FTL, NNT, and AIFM1 in the Amygdala of Cognitively Impaired Elderly Persons.
[So] Source:J Neuropathol Exp Neurol;77(1):21-39, 2018 Jan 01.
[Is] ISSN:1554-6578
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Misfolded protein in the amygdala is a neuropathologic feature of Alzheimer disease and many other neurodegenerative disorders. We examined extracts from human amygdala (snap-frozen at autopsy) to investigate whether novel and as yet uncharacterized misfolded proteins would be detectable. Polypeptides from the detergent-insoluble, urea-soluble protein fractions of amygdala were interrogated using liquid chromatography-electrospray ionization-tandem mass spectrometry. Among the detergent-insoluble proteins identified in amygdala of demented subjects but not controls were Tau, TDP-43, Aß, α-synuclein, and ApoE. Additional detergent-insoluble proteins from demented subjects in the high-molecular weight portion of SDS gels included NNT, TNIK, PRKDC (DNA-PK, or DNA-PKcs), ferritin light chain (FTL), AIFM1, SYT11, STX1B, EAA1, COL25A1, M4K4, CLH1, SQSTM, SYNJ1, C3, and C4. In follow-up immunohistochemical experiments, NNT, TNIK, PRKDC, AIFM1, and FTL were observed in inclusion body-like structures in cognitively impaired subjects' amygdalae. Double-label immunofluorescence revealed that FTL and phospho-PRKDC immunoreactivity colocalized partially with TDP-43 and/or Tau inclusion bodies. Western blots showed high-molecular weight "smears", particularly for NNT and PRKDC. A preliminary genetic association study indicated that rare NNT, TNIK, and PRKDC gene variants had nominally significant association with Alzheimer-type dementia risk. In summary, novel detergent-insoluble proteins, with evidence of proteinaceous deposits, were found in amygdalae of elderly, cognitively impaired subjects.
[Mh] Termos MeSH primário: Doença de Alzheimer/metabolismo
Tonsila do Cerebelo/metabolismo
Disfunção Cognitiva/metabolismo
Corpos de Inclusão/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Doença de Alzheimer/patologia
Tonsila do Cerebelo/patologia
Apoferritinas/metabolismo
Fator de Indução de Apoptose/metabolismo
Cromatografia Líquida
Disfunção Cognitiva/patologia
Proteína Quinase Ativada por DNA/metabolismo
Proteínas de Ligação a DNA/metabolismo
Seres Humanos
Corpos de Inclusão/patologia
Proteínas Mitocondriais/metabolismo
NADP Trans-Hidrogenase Específica para A ou B/metabolismo
Proteínas Nucleares/metabolismo
Proteômica
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (AIFM1 protein, human); 0 (Apoptosis Inducing Factor); 0 (DNA-Binding Proteins); 0 (FTL protein, human); 0 (Mitochondrial Proteins); 0 (Nuclear Proteins); 9013-31-4 (Apoferritins); EC 1.6.1.2 (NADP Transhydrogenase, AB-Specific); EC 1.6.1.2 (NNT protein, human); EC 2.7.11.1 (DNA-Activated Protein Kinase); EC 2.7.11.1 (PRKDC protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180109
[Lr] Data última revisão:
180109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE
[do] DOI:10.1093/jnen/nlx097


  7 / 12513 MEDLINE  
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[PMID]:29223157
[Au] Autor:Sidorin EV; Khomenko VA; Kim NY; Dmitrenok PS; Stenkova AM; Novikova OD; Solov'eva TF
[Ad] Endereço:Elyakov Pacific Institute of Bioorganic Chemistry, Far-Eastern Branch of the Russian Academy of Sciences, Vladivostok, 690022, Russia. sev1972@mail.ru.
[Ti] Título:Self-Organization of Recombinant Membrane Porin OmpF from Yersinia pseudotuberculosis in Aqueous Environments.
[So] Source:Biochemistry (Mosc);82(11):1304-1313, 2017 Nov.
[Is] ISSN:1608-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Recombinant porin OmpF (an integral protein of bacterial outer membrane) from Yersinia pseudotuberculosis was synthesized in Escherichia coli cells as inclusion bodies. By combining the methods of anion-exchange and gel filtration chromatographies, recombinant OmpF (rOmpF) was isolated as an individual protein in its denatured state, and its characteristic properties (molecular mass, N-terminal amino acid sequence, and hydrodynamic radius of the protein in 8 M urea solution) were determined. According to the data of gel filtration, dynamic light scattering, optical spectroscopy, and binding of the hydrophobic fluorescent probe 8-anilino-1-naphthalenesulfonic acid, the rOmpF is fully unfolded in 8 M urea and exists in random coil conformation. In aqueous solutions, rOmpF undergoes conformational changes, reversible self-association, and aggregation. When transferred from 8 M urea into water, PBS (containing 0.15 M NaCl, pH 7.4), or buffer containing 0.8 M urea (pH 8.0), fully unfolded rOmpF forms relatively compact monomeric intermediates prone to self-association with formation of multimers. The oligomeric intermediates have high content of native protein-like secondary structure and pronounced tertiary structure. In acidic media (pH 5.0, close to the protein isoelectric point), rOmpF undergoes rapid irreversible aggregation. Therefore, we found that medium composition significantly affects both porin folding and processes of its self-association and aggregation.
[Mh] Termos MeSH primário: Porinas/química
Yersinia pseudotuberculosis/química
[Mh] Termos MeSH secundário: Proteínas da Membrana Bacteriana Externa
Proteínas de Bactérias
Escherichia coli/genética
Escherichia coli/metabolismo
Corpos de Inclusão
Porinas/biossíntese
Porinas/isolamento & purificação
Conformação Proteica
Desnaturação Proteica/efeitos dos fármacos
Dobramento de Proteína/efeitos dos fármacos
Multimerização Proteica/efeitos dos fármacos
Renaturação Proteica/efeitos dos fármacos
Proteínas Recombinantes
Soluções/química
Soluções/farmacologia
Água
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Outer Membrane Proteins); 0 (Bacterial Proteins); 0 (OmpF protein); 0 (Porins); 0 (Recombinant Proteins); 0 (Solutions); 059QF0KO0R (Water)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171211
[St] Status:MEDLINE
[do] DOI:10.1134/S0006297917110086


  8 / 12513 MEDLINE  
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[PMID]:27776208
[Au] Autor:Song X; Wen Y; Zhu JL; Zhao F; Zhang ZX; Li J
[Ad] Endereço:Department of Biomedical Engineering, Faculty of Engineering, Faculty of Engineering, National University of Singapore , 7 Engineering Drive 1, Singapore 117574, Singapore.
[Ti] Título:Thermoresponsive Delivery of Paclitaxel by ß-Cyclodextrin-Based Poly(N-isopropylacrylamide) Star Polymer via Inclusion Complexation.
[So] Source:Biomacromolecules;17(12):3957-3963, 2016 12 12.
[Is] ISSN:1526-4602
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Paclitaxel (PTX), a hydrophobic anticancer drug, is facing several clinical limitations such as low bioavailability and drug resistance. To solve the problems, a well-defined ß-cyclodextrin-poly(N-isopropylacrylamide) star polymer was synthesized and used as a nanocarrier to improve the water solubility and aim to thermoresponsive delivery of PTX to cancer cells. The star polymer was able to form supramolecular self-assembled inclusion complex with PTX via host-guest interaction at room temperature, which is below the low critical solution temperature (LCST) of the star polymer, significantly improving the solubilization of PTX. At body temperature (above LCST), the phase transition of poly(N-isopropylacrylamide) segments induced the formation of nanoparticles, which greatly enhanced the cellular uptake of the polymer-drug complex, resulting in efficient thermoresponsive delivery of PTX. In particular, the polymer-drug complex exhibited better antitumor effects than the commercial formulation of PTX in overcoming the multi-drug resistance in AT3B-1 cells.
[Mh] Termos MeSH primário: Acrilamidas/química
Sistemas de Liberação de Medicamentos
Nanopartículas/administração & dosagem
Paclitaxel/farmacologia
Polímeros/administração & dosagem
Neoplasias da Próstata/tratamento farmacológico
beta-Ciclodextrinas/química
[Mh] Termos MeSH secundário: Animais
Antineoplásicos Fitogênicos/administração & dosagem
Antineoplásicos Fitogênicos/farmacologia
Sobrevivência Celular/efeitos dos fármacos
Resistência a Múltiplos Medicamentos/efeitos dos fármacos
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Corpos de Inclusão
Masculino
Nanopartículas/química
Paclitaxel/administração & dosagem
Polímeros/química
Ratos
Temperatura Ambiente
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acrylamides); 0 (Antineoplastic Agents, Phytogenic); 0 (Polymers); 0 (beta-Cyclodextrins); B7GFF17L9U (N-isopropylacrylamide); P88XT4IS4D (Paclitaxel)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171213
[Lr] Data última revisão:
171213
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  9 / 12513 MEDLINE  
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[PMID]:28466142
[Au] Autor:Mackenzie IR; Neumann M
[Ad] Endereço:Department of Pathology, Vancouver General Hospital, University of British Columbia, 855 West 12th Avenue, Vancouver, BC, V5Z 1M9, Canada. ian.mackenzie@vch.ca.
[Ti] Título:Reappraisal of TDP-43 pathology in FTLD-U subtypes.
[So] Source:Acta Neuropathol;134(1):79-96, 2017 Jul.
[Is] ISSN:1432-0533
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Frontotemporal lobar degeneration with tau-negative, ubiquitin-immunoreactive (-ir) pathology (FTLD-U) is subclassified based on the type and cortical laminar distribution of neuronal inclusions. Following the discovery of the transactive response DNA-binding protein Mr 43 kD (TDP-43) as the ubiquitinated protein in most FTLD-U, the same pathological criteria have been used to classify FTLD cases based on TDP-43-ir changes. However, the fact that immunohistochemistry (IHC) for ubiquitin and TDP-43 each recognizes slightly different pathological changes in these cases means that the original FTLD-U subtype criteria may not be directly applicable for use with TDP-43 IHC. We formally re-evaluated the TDP-43-ir pathological features that characterize the different FTLD-U subtypes to see if the current classification could be refined. In our series of 78 cases, 81% were classified as one of the common FTLD-U subtypes (29% A, 35% B, 17% C). With TDP-43 IHC, each subtype demonstrated consistent intra-group pathological features and clear inter-group differences. The TDP-43-ir changes that characterized type A and C cases were similar to those seen with ubiquitin IHC; specifically, compact neuronal cytoplasmic inclusions (NCI), short thick dystrophic neurites (DN), and lentiform neuronal intranuclear inclusions concentrated in cortical layer II in type A cases, and a predominance of long thick DN in type C. However, type B cases showed significant differences with TDP-43 compared with ubiquitin IHC; with many diffuse granular NCI and wispy thread and dots-like profiles in all cortical layers. The remaining 15 cases (12 with C9orf72 mutations) showed changes that were consistent with combined type A and type B pathology. These findings suggest that the pathological criteria for subtyping FTLD cases based on TDP-43 IHC might benefit from some refinement that recognizes differences in the morphologies of NCI and neurites. Furthermore, there is a significant subset of cases (most with the C9orf72 mutation) with the pathological features of multiple FTLD-TDP subtypes for which appropriate classification is difficult.
[Mh] Termos MeSH primário: Proteínas de Ligação a DNA/metabolismo
Demência Frontotemporal/classificação
Demência Frontotemporal/patologia
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Proteína C9orf72/genética
Córtex Cerebral/metabolismo
Córtex Cerebral/patologia
Feminino
Demência Frontotemporal/genética
Demência Frontotemporal/metabolismo
Seres Humanos
Imuno-Histoquímica
Corpos de Inclusão/metabolismo
Corpos de Inclusão/patologia
Masculino
Meia-Idade
Neurônios/metabolismo
Neurônios/patologia
Fosforilação
Ubiquitinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (C9orf72 Protein); 0 (C9orf72 protein, human); 0 (DNA-Binding Proteins); 0 (TDP-43 protein, human); 0 (Ubiquitins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171211
[Lr] Data última revisão:
171211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1007/s00401-017-1716-8


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[PMID]:28951248
[Au] Autor:Li R; Zhu LN; Ren LQ; Weng JY; Sun JS
[Ad] Endereço:Tianjin Key Laboratory of Animal and Plant Resistance, College of Life Science, Tianjin Normal University, Tianjin, People's Republic of China.
[Ti] Título:Molecular cloning and characterization of glycogen synthase in Eriocheir sinensis.
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;214:47-56, 2017 Dec.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycogen plays an important role in glucose and energy homeostasis at cellular and organismal levels. In glycogen synthesis, glycogen synthase (GS) is a rate-limiting enzyme catalysing the addition of α-1,4-linked glucose units from (UDP) -glucose to a nascent glycogen chain using glycogenin (GN) as a primer. While studies on mammalian liver GS (GYS2) are numerous, enzymes from crustaceans, which also use glycogen and glucose as their main energy source, have received less attention. In the present study, we amplified full-length GS cDNA from Eriocheir sinensis. Tissue expression profiling revealed the highest expression of GS in the hepatopancreas. During moulting, GS expression and activity declined, and glycogen levels in the hepatopancreas were reduced. Recombinant GS was expressed in Escherichia coli Rosetta (DE3), and induction at 37°C or 16°C yielded EsGS in insoluble inclusion bodies (EsGS-I) or in soluble form (EsGS-S), respectively. Enzyme activity was measured in a cell-free system containing glucose-6-phosphate (G6P), and both forms possessed glycosyltransferase activity, but refolded EsGS-I was more active. Enzyme activity of both GS and EsGS-I in the hepatopancreas was optimum at 25°C, which is coincident with the optimum growth temperature of Chinese mitten crab, and higher (37°C) or lower (16°C) temperatures resulted in lower enzyme activity. Taken together, the results suggest that GS may be important for maintaining normal physiological functions such as growth and reproduction.
[Mh] Termos MeSH primário: Proteínas de Artrópodes/genética
Braquiúros/enzimologia
Glicogênio Sintase/genética
Glicogênio/biossíntese
Hepatopâncreas/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas de Artrópodes/metabolismo
Sítios de Ligação
Braquiúros/genética
Braquiúros/crescimento & desenvolvimento
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glucose-6-Fosfato/metabolismo
Glucosiltransferases/metabolismo
Glicogênio Sintase/metabolismo
Glicoproteínas/metabolismo
Hepatopâncreas/crescimento & desenvolvimento
Corpos de Inclusão/química
Cinética
Muda/genética
Especificidade de Órgãos
Filogenia
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Glycoproteins); 0 (Recombinant Proteins); 0 (glycogenin); 56-73-5 (Glucose-6-Phosphate); 9005-79-2 (Glycogen); EC 2.4.1.- (Glucosyltransferases); EC 2.4.1.11 (Glycogen Synthase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170928
[St] Status:MEDLINE



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