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Pesquisa : D04.345.566.735 [Categoria DeCS]
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[PMID]:28767681
[Au] Autor:Thongbai B; Miller SL; Stadler M; Wittstein K; Hyde KD; Lumyong S; Raspé O
[Ad] Endereço:Centre of Excellence in Fungal Research, and School of Science, Mae Fah Luang University, Chiang Rai, Thailand.
[Ti] Título:Study of three interesting Amanita species from Thailand: Morphology, multiple-gene phylogeny and toxin analysis.
[So] Source:PLoS One;12(8):e0182131, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amanita ballerina and A. brunneitoxicaria spp. nov. are introduced from Thailand. Amanita fuligineoides is also reported for the first time from Thailand, increasing the known distribution of this taxon. Together, those findings support our view that many taxa are yet to be discovered in the region. While both morphological characters and a multiple-gene phylogeny clearly place A. brunneitoxicaria and A. fuligineoides in sect. Phalloideae (Fr.) Quél., the placement of A. ballerina is problematic. On the one hand, the morphology of A. ballerina shows clear affinities with stirps Limbatula of sect. Lepidella. On the other hand, in a multiple-gene phylogeny including taxa of all sections in subg. Lepidella, A. ballerina and two other species, including A. zangii, form a well-supported clade sister to the Phalloideae sensu Bas 1969, which include the lethal "death caps" and "destroying angels". Together, the A. ballerina-A. zangii clade and the Phalloideae sensu Bas 1969 also form a well-supported clade. We therefore screened for two of the most notorious toxins by HPLC-MS analysis of methanolic extracts from the basidiomata. Interestingly, neither α-amanitin nor phalloidin was found in A. ballerina, whereas Amanita fuligineoides was confirmed to contain both α-amanitin and phalloidin, and A. brunneitoxicaria contained only α-amanitin. Together with unique morphological characteristics, the position in the phylogeny indicates that A. ballerina is either an important link in the evolution of the deadly Amanita sect. Phalloideae species, or a member of a new section also including A. zangii.
[Mh] Termos MeSH primário: Amanita/classificação
DNA Fúngico/análise
Micotoxinas/isolamento & purificação
[Mh] Termos MeSH secundário: Alfa-Amanitina/isolamento & purificação
Amanita/genética
Amanita/metabolismo
Cromatografia Líquida de Alta Pressão
Espectrometria de Massas
Micotoxinas/classificação
Faloidina/isolamento & purificação
Filogenia
Análise de Sequência de DNA
Tailândia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Alpha-Amanitin); 0 (DNA, Fungal); 0 (Mycotoxins); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182131


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[PMID]:28659356
[Au] Autor:Chakraborty A; Kurati SP; Mahata SK; Sundar S; Roy S; Sen M
[Ad] Endereço:Division of Cancer Biology and Inflammatory Disorder, Council of Scientific and Industrial Research-Indian Institute of Chemical Biology, Jadavpur, Kolkata 700032, India.
[Ti] Título:Wnt5a Signaling Promotes Host Defense against Infection.
[So] Source:J Immunol;199(3):992-1002, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:infects macrophages, disrupting immune homeostasis. The underlying mechanism that sustains infection remains unresolved. In view of the potential of Wnt5a signaling to support immune homeostasis, we evaluated the interrelationship of Wnt5a signaling and infection. Upon infecting macrophages separately with antimony drug-sensitive and -resistant , we noted disruption in the steady-state level of Wnt5a. Moreover, inhibition of Wnt5a signaling by small interfering RNA transfection in vitro or by use of inhibitor of Wnt production in vivo led to an increase in cellular parasite load. In contrast, treatment of macrophages with recombinant Wnt5a caused a decrease in the load of antimony-sensitive and -resistant parasites, thus confirming that Wnt5a signaling antagonizes infection. Using inhibitors of the Wnt5a signaling intermediates Rac1 and Rho kinase, we demonstrated that Wnt5a-mediated inhibition of parasite infection in macrophages is Rac1/Rho dependent. Furthermore, phalloidin staining and reactive oxygen species estimation of Wnt5a-treated macrophages suggested that a Wnt5a-Rac/Rho-mediated decrease in parasite load is associated with an increase in F- actin assembly and NADPH oxidase activity. Moreover, live microscopy of -infected macrophages treated with Wnt5a demonstrated increased endosomal/lysosomal fusions with parasite-containing vacuoles (parasitophorous vacuoles [PV]). An increase in PV-endosomal/lysosomal fusion accompanied by augmented PV degradation in Wnt5a-treated macrophages was also apparent from transmission electron microscopy of infected cells. Our results suggest that, although evades host immune response, at least in part through inhibition of Wnt5a signaling, revamping Wnt5a signaling can inhibit infection, irrespective of drug sensitivity or resistance.
[Mh] Termos MeSH primário: Leishmania donovani/imunologia
Macrófagos/imunologia
Macrófagos/parasitologia
Proteína Wnt-5a/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Antimônio/farmacologia
Antiprotozoários/farmacologia
Leishmania donovani/efeitos dos fármacos
Leishmania donovani/fisiologia
Leishmaniose Visceral/imunologia
Macrófagos/ultraestrutura
Camundongos
Camundongos Endogâmicos BALB C
Microscopia Eletrônica de Transmissão
NADPH Oxidases/metabolismo
Neuropeptídeos/metabolismo
Carga Parasitária
Faloidina/química
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
Transfecção
Vacúolos/imunologia
Vacúolos/parasitologia
Proteína Wnt-5a/genética
Proteína Wnt-5a/farmacologia
Proteínas rac1 de Ligação ao GTP/metabolismo
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Antiprotozoal Agents); 0 (Neuropeptides); 0 (RNA, Small Interfering); 0 (Rac1 protein, mouse); 0 (Reactive Oxygen Species); 0 (Wnt-5a Protein); 0 (Wnt5a protein, mouse); 17466-45-4 (Phalloidine); 9IT35J3UV3 (Antimony); EC 1.6.3.- (NADPH Oxidases); EC 2.7.11.1 (rho-Associated Kinases); EC 3.6.5.2 (rac1 GTP-Binding Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601927


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[PMID]:28241031
[Au] Autor:Smith SJ; Wang JC; Gupta VA; Dowling JJ
[Ad] Endereço:Departments of Pediatrics and Molecular Genetics, University of Toronto, Toronto, Canada.
[Ti] Título:A novel early onset phenotype in a zebrafish model of merosin deficient congenital muscular dystrophy.
[So] Source:PLoS One;12(2):e0172648, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Merosin deficient congenital muscular dystrophy (MDC1A) is a severe neuromuscular disorder with onset in infancy that is associated with severe morbidities (particularly wheelchair dependence) and early mortality. It is caused by recessive mutations in the LAMA2 gene that encodes a subunit of the extracellular matrix protein laminin 211. At present, there are no treatments for this disabling disease. The zebrafish has emerged as a powerful model system for the identification of novel therapies. However, drug discovery in the zebrafish is largely dependent on the identification of phenotypes suitable for chemical screening. Our goal in this study was to elucidate novel, early onset abnormalities in the candyfloss (caf) zebrafish, a model of MDC1A. We uncovered and characterize abnormalities in spontaneous coiling, the earliest motor movement in the zebrafish, as a fully penetrant change specific to caf mutants that is ideal for future drug testing.
[Mh] Termos MeSH primário: Modelos Animais de Doenças
Laminina/genética
Distrofias Musculares/genética
[Mh] Termos MeSH secundário: Animais
Animais Geneticamente Modificados
Heterozigoto
Laminina/metabolismo
Músculo Esquelético/metabolismo
Distrofias Musculares/metabolismo
Mutação
Faloidina/biossíntese
Fenótipo
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Laminin); 0 (laminin alpha2, zebrafish); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172648


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[PMID]:27693909
[Au] Autor:Ostrowska Z; Robaszkiewicz K; Moraczewska J
[Ad] Endereço:Department of Biochemistry and Cell Biology, Faculty of Natural Sciences, Kazimierz Wielki University in Bydgoszcz, Ks. J. Poniatowskiego 12 Str., 85-671 Bydgoszcz, Poland.
[Ti] Título:Regulation of actin filament turnover by cofilin-1 and cytoplasmic tropomyosin isoforms.
[So] Source:Biochim Biophys Acta;1865(1):88-98, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Tropomyosin and cofilin are actin-binding proteins which control dynamics of actin assembly and disassembly. Tropomyosin isoforms can either inhibit or enhance cofilin activity, but the mechanism of this diverse regulation is not well understood. In this work mechanisms of actin dynamics regulation by four cytoskeletal tropomyosin isoforms and cofilin-1 were studied with the use of biochemical and fluorescent microscopy assays. The recombinant tropomyosin isoforms were products of two genes: TPM1 (Tpm1.6 and Tpm1.8) and TPM3 (Tpm3.2 and Tpm3.4). Tpm1.6/1.8 bound to F-actin with higher apparent binding constants and lower cooperativities than Tpm3.2/3.4. In consequence, subsaturating concentrations of cofilin-1 removed 50% of Tpm3.2/3.4 from F-actin. By contrast, 2 and 5.5 molar excess of cofilin-1 over actin was required to dissociate 50% of Tpm1.6/1.8. All tropomyosins inhibited the rate of spontaneous polymerization of actin, which was reversed by cofilin-1. Products of TPM1 favored longer filaments and protected them from cofilin-induced depolymerization. This was in contrast to the isoforms derived from TPM3, which facilitated depolymerization. Tpm3.4 was the only isoform, which increased frequency of the filament severing by cofilin-1. Tpm1.6/1.8 inhibited, but Tpm3.2/3.4 enhanced cofilin-induced conformational changes leading to accelerated release of rhodamine-phalloidin from the filament. We concluded that the effects were executed through different actin affinities of tropomyosin isoforms and cooperativities of tropomyosin and cofilin-1 binding. The results obtained in vitro were in good agreement with localization of tropomyosin isoforms in stable or highly dynamic filaments demonstrated before in various cells.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Cofilina 1/metabolismo
Tropomiosina/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/química
Sequência de Aminoácidos
Animais
Cofilina 1/química
Citoplasma/metabolismo
Seres Humanos
Camundongos
Faloidina/análogos & derivados
Faloidina/química
Polimerização
Ligação Proteica
Isoformas de Proteínas/química
Isoformas de Proteínas/metabolismo
Ratos
Rodaminas/química
Tropomiosina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cofilin 1); 0 (Protein Isoforms); 0 (Rhodamines); 0 (Tropomyosin); 0 (rhodamine-phalloidin); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161004
[St] Status:MEDLINE


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[PMID]:27473595
[Au] Autor:Torkamani N; Rufaut N; Jones L; Sinclair R
[Ad] Endereço:Department of Dermatology, School of Medicine, Health and Dentistry, University of Melbourne, Melbourne, VIC, Australia. torkamani_niloufar@yahoo.com.
[Ti] Título:The arrector pili muscle, the bridge between the follicular stem cell niche and the interfollicular epidermis.
[So] Source:Anat Sci Int;92(1):151-158, 2017 Jan.
[Is] ISSN:1447-073X
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Proximally, the arrector pili muscle (APM) attaches to the follicular stem cell niche in the bulge, but its distal properties are comparatively unclear. In this work, a novel method employing an F-actin probe, phalloidin, was employed to visualize the APM anatomy. Phalloidin staining of the APM was validated by comparison with conventional antibodies/stains and by generating three-dimensional reconstructions. The proximal attachment of the APM to the bulge in 8 patients with androgenic alopecia was studied using Masson's trichrome stain. Phalloidin visualized extensive branching of the APM. The distal end of the human APM exhibits a unique "C"-shaped structure connecting to the dermal-epidermal junction. The proximal APM attachment was observed to be lost or extremely miniaturized in androgenic alopecia. The unique shape, location, and attachment sites of the APM suggest a significant role for this muscle in maintaining follicular integrity. Proximally, the APM encircles the follicular unit and only attaches to the primary hair follicle in the bulge; this attachment is lost in irreversible hair loss. The APM exhibits an arborized morphology as it ascends toward the epidermis, and anchors to the basement membrane.
[Mh] Termos MeSH primário: Anatomia/métodos
Epiderme/anatomia & histologia
Folículo Piloso/anatomia & histologia
Folículo Piloso/citologia
Músculo Liso/anatomia & histologia
Couro Cabeludo/anatomia & histologia
Nicho de Células-Tronco
[Mh] Termos MeSH secundário: Actinas
Alopecia/patologia
Membrana Basal/anatomia & histologia
Membrana Basal/patologia
Epiderme/patologia
Folículo Piloso/patologia
Seres Humanos
Músculo Liso/patologia
Faloidina
Couro Cabeludo/citologia
Couro Cabeludo/patologia
Coloração e Rotulagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170302
[Lr] Data última revisão:
170302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160731
[St] Status:MEDLINE


  6 / 1467 MEDLINE  
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[PMID]:27906446
[Au] Autor:Axrap A; Wang J; Liu Y; Wang M; Yusuf A
[Ad] Endereço:Micro Repair and Reconstructive Surgery Department of Orthopedic Center, The First Affiliated Hospital of Xinjiang Medical University, Urumqi, Xinjiang, China. ahmat_yusuf1@163.com.
[Ti] Título:Study on adhesion, proliferation and differentiation of osteoblasts promoted by new absorbable bioactive glass injection in vitro.
[So] Source:Eur Rev Med Pharmacol Sci;20(22):4677-4681, 2016 Nov.
[Is] ISSN:2284-0729
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: The objective of this study was to evaluate adhesion, proliferation and differentiation of osteoblasts grown on absorbable bioactive glass-calcium phosphate cement injection (BG-CPC) materials in vitro. MATERIALS AND METHODS: BG-CPC composite biomaterial samples were prepared in vitro, for culture with MC3T3-E1 rat osteoblasts. Cells were divided into CPC, BG and BG-CPC treated groups. After cultivation for 3d, cells were stained with rhodamine-phalloidin and 4',6-diamidino-2-phenylindole (DAPI) and observed by fluorescence microscopy for osteoblast morphology on the surface of biomaterials. At 24h, 48h and 72h, MTT assay was used to test adhesion and proliferation, and bicinchoninic acid assay (BCA) method was carried out to test ALP activity; ELISA was used to test bone morphogenetic protein (BMP) and TGF-ß expression levels at day 3. RESULTS: Compared with the other two groups, cells in the BG-CPC group had more attachments; the DAPI labelled nuclei were clearer and nuclear shape was more complete and full. Adhesion and proliferation, as well as alkaline phosphatase (ALP) activity of cells for all time points in the BG-CPC group were higher than those in the other two groups and differences were of statistically significant (p<0.05); BMP and TGF-ß expression levels were higher than those in the other two groups and the differences were statistically significant (p<0.05). CONCLUSIONS: In vitro use of new absorbable bioactive glass is able to promote adhesion, proliferation and differentiation of osteoblasts, which may be related to increased BMP and TGF-ß expression.
[Mh] Termos MeSH primário: Fosfatos de Cálcio
Osteoblastos/fisiologia
[Mh] Termos MeSH secundário: Fosfatase Alcalina/metabolismo
Animais
Cimentos para Ossos/química
Regeneração Óssea
Adesão Celular
Diferenciação Celular
Vidro/química
Osteoblastos/metabolismo
Faloidina/análogos & derivados
Ratos
Rodaminas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bone Cements); 0 (Calcium Phosphates); 0 (Rhodamines); 0 (rhodamine-phalloidin); 17466-45-4 (Phalloidine); 97Z1WI3NDX (calcium phosphate); EC 3.1.3.1 (Alkaline Phosphatase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170802
[Lr] Data última revisão:
170802
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE


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[PMID]:27705769
[Au] Autor:Bengtsson E; Persson M; Rahman MA; Kumar S; Takatsuki H; Månsson A
[Ad] Endereço:Department of Chemistry and Biomedical Sciences, Faculty of Health and Life Sciences, Linnaeus University, Kalmar, Sweden.
[Ti] Título:Myosin-Induced Gliding Patterns at Varied [MgATP] Unveil a Dynamic Actin Filament.
[So] Source:Biophys J;111(7):1465-1477, 2016 Oct 04.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Actin filaments have key roles in cell motility but are generally claimed to be passive interaction partners in actin-myosin-based motion generation. Here, we present evidence against this static view based on an altered myosin-induced actin filament gliding pattern in an in vitro motility assay at varied [MgATP]. The statistics that characterize the degree of meandering of the actin filament paths suggest that for [MgATP] ≥ 0.25 mM, the flexural rigidity of heavy meromyosin (HMM)-propelled actin filaments is similar (without phalloidin) or slightly lower (with phalloidin) than that of HMM-free filaments observed in solution without surface tethering. When [MgATP] was reduced to ≤0.1 mM, the actin filament paths in the in vitro motility assay became appreciably more winding in both the presence and absence of phalloidin. This effect of lowered [MgATP] was qualitatively different from that seen when HMM was mixed with ATP-insensitive, N-ethylmaleimide-treated HMM (NEM-HMM; 25-30%). In particular, the addition of NEM-HMM increased a non-Gaussian tail in the path curvature distribution as well as the number of events in which different parts of an actin filament followed different paths. These effects were the opposite of those observed with reduced [MgATP]. Theoretical modeling suggests a 30-40% lowered flexural rigidity of the actin filaments at [MgATP] ≤ 0.1 mM and local bending of the filament front upon each myosin head attachment. Overall, the results fit with appreciable structural changes in the actin filament during actomyosin-based motion generation, and modulation of the actin filament mechanical properties by the dominating chemomechanical actomyosin state.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/química
Trifosfato de Adenosina/química
Subfragmentos de Miosina/química
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Trifosfato de Adenosina/metabolismo
Animais
Transporte Biológico
Elasticidade
Modelos Moleculares
Músculo Esquelético/química
Músculo Esquelético/metabolismo
Subfragmentos de Miosina/metabolismo
Dinâmica não Linear
Faloidina/química
Conformação Proteica
Soluções/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Myosin Subfragments); 0 (Solutions); 17466-45-4 (Phalloidine); 8L70Q75FXE (Adenosine Triphosphate)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161006
[St] Status:MEDLINE


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[PMID]:27480605
[Au] Autor:Borovikov YS; Rysev NA; Chernev AA; Avrova SV; Karpicheva OE; Borys D; Sliwinska M; Moraczewska J
[Ad] Endereço:Institute of Cytology, Tikhoretsky Pr., 4, Saint Petersburg, 194064, Russia. Electronic address: borovikov@incras.ru.
[Ti] Título:Abnormal movement of tropomyosin and response of myosin heads and actin during the ATPase cycle caused by the Arg167His, Arg167Gly and Lys168Glu mutations in TPM1 gene.
[So] Source:Arch Biochem Biophys;606:157-66, 2016 Sep 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Amino acid substitutions: Arg167His, Arg167Gly and Lys168Glu, located in a consensus actin-binding site of the striated muscle tropomyosin Tpm1.1 (TM), were used to investigate mechanisms of the thin filament regulation. The azimuthal movement of TM strands on the actin filament and the responses of the myosin heads and actin subunits during the ATPase cycle were studied using fluorescence polarization of muscle fibres. The recombinant wild-type and mutant TMs labelled with 5-IAF, 1,5-IAEDANS-labelled S1and FITC-phalloidin F-actin were incorporated into the ghost muscle fibres to acquire information on the orientation of the probes relative to the fibre axis. The substitutions Arg167Gly and Lys168Glu shifted TM strands into the actin filament centre, whereas Arg167His moved TM towards the periphery of the filament. In the presence of Arg167Gly-TM and Lys168Glu-TM the fraction of actin monomers that were switched on and the number of the myosin heads strongly bound to F-actin were abnormally high even under conditions close to relaxation. In contrast, Arg167His-TM decreased the fraction of switched on actin and reduced the formation of strongly bound myosin heads throughout the ATPase cycle. We concluded that the altered TM-actin contacts destabilized the thin filament and affected the actin-myosin interactions.
[Mh] Termos MeSH primário: Adenosina Trifosfatases/química
Miosinas/química
Tropomiosina/química
Tropomiosina/genética
[Mh] Termos MeSH secundário: Actinas/química
Animais
Arginina/química
Glutamina/química
Glicina/química
Histidina/química
Lisina/química
Masculino
Microscopia de Fluorescência
Mutação
Nucleotídeos
Faloidina/química
Coelhos
Proteínas Recombinantes/química
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Nucleotides); 0 (Recombinant Proteins); 0 (Tropomyosin); 0RH81L854J (Glutamine); 17466-45-4 (Phalloidine); 4QD397987E (Histidine); 94ZLA3W45F (Arginine); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.4.1 (Myosins); K3Z4F929H6 (Lysine); TE7660XO1C (Glycine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160803
[St] Status:MEDLINE


  9 / 1467 MEDLINE  
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[PMID]:27464628
[Au] Autor:Li M; Fang Y; Yao M; Yu WR; Ni T; Gu C; Yang PG; Mao ZG
[Ad] Endereço:Department of Burns and Plastic Surgery, Shanghai Ninth People's Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 201999, China.
[Ti] Título:[Effects of transforming growth factor ß1 receptor inhibitor SD-208 on human hypertrophic scar].
[So] Source:Zhonghua Shao Shang Za Zhi;32(7):389-95, 2016 Jul 20.
[Is] ISSN:1009-2587
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To investigate the effects of transforming growth factor ß1 (TGF-ß1) receptor inhibitor SD-208 on human hypertrophic scar and its mechanisms. METHODS: Scar fibroblasts were isolated from deprecated human hypertrophic scar tissue and then sub-cultured. Cells of the fifth passage were used in the following experiments. (1) Cells were divided into blank control group (BC) and 0.5, 1.0, 3.0, and 5.0 µmol/L SD-208 groups according to the random number table (the same grouping method below), with 6 wells in each group. Cells in group BC were added with 1 µL phosphate buffer solution, while cells in the latter four groups were added with 0.5, 1.0, 3.0, and 5.0 µmol/L SD-208, respectively. After being cultured for 12 hours, the proliferation activity of cells was detected by cell counting kit 8 and microplate reader (denoted as absorbance value). Suitable amount of substance concentration of SD-208 according to the results of proliferation activity of cells was chosen for the following experiments. (2) Another batch of cells were divided into group BC and 1, 3 µmol/L SD-208 groups and treated as in (1), with 8 wells in each group. The number of migration cells was detected by transwell method. (3) Another batch of cells were grouped and treated as in (2), and the microfilament morphology of cells was observed by rhodamine-phalloidin staining. (4) Another batch of cells were grouped and treated as in (2), and the protein expression of TGF-ß1 was assessed with Western blotting. (5) Forty-eight BALB/c nude mice were divided into normal saline group (NS) and 1 µmol/L SD-208 group, and one longitudinal incision with length of 1 cm was made on their back. Then human hypertrophic scar tissue was embedded into the incision. On post injury day 7, multipoint injection of NS in a volume of 0.05 mL was performed in wounds of rats in group NS, while rats in 1 µmol/L SD-208 group were given 0.05 mL 1 µmol/L SD-208, once a day. On the day 0 (the same day), 2, 4, 6, 8, 10, 12, 14, 16, 18, and 20 post first time of injection, the weight of 8 nude mice was weighed by electronic scale, and scar area was measured by vernier caliper and the ratio of rest scar area was calculated. (6) In week 1, 2, and 3 post first time of injection, the protein expression of TGF-ß1 of human hypertrophic scar tissue was assessed with Western blotting. Data were processed with one-way analysis of variance and two independent-sample t test. RESULTS: (1) The proliferation activity of cells in group BC, 0.5, 1.0, 3.0, and 5.0 µmol/L SD-208 groups was respectively 1.00±0.03, 0.90±0.08, 0.68±0.11, 0.54±0.04, and 0.42±0.09, and the proliferation activity of cells in 0.5, 1.0, 3.0, and 5.0 µmol/L SD-208 groups was significantly lower than that in group BC (with t values from 2.9 to 22.1, P<0.05 or P<0.01). (2) The number of migration cells in 1, 3 µmol/L SD-208 groups was significantly less than that in group BC (with t values respectively 6.5 and 6.4, P values below 0.01). (3) Compared with that in group BC, fluorescence intensity of microfilaments of cells in 1, 3 µmol/L SD-208 groups was attenuated, and the pseudopod extended less. (4) The protein expressions of TGF-ß1 of cells in group BC and 1, 3 µmol/L SD-208 groups were respectively 1.00±0.08, 0.80±0.08, and 0.61±0.05, and the protein expressions of TGF-ß1 of cells in 1, 3 µmol/L SD-208 groups were significantly lower than those in group BC (with t values respectively 4.0 and 9.2, P values below 0.01). (5) The weights of nude mice in group NS and 1 µmol/L SD-208 group were similar on each time day (with t values from 0.2 to 1.1, P values above 0.05). The ratios of rest scar area of nude mice in two groups were decreased along with the injection time, and the ratios of rest scar area of nude mice in 1 µmol/L SD-208 group were significantly less than those in group NS from the day 6 to 20 post first time of injection (with t values from 1.8 to 15.9, P<0.05 or P<0.01). In week 1, 2, and 3 post first time of injection, the protein expressions of TGF-ß1 of human hypertrophic scar tissue in nude mice in two groups showed a tendency of decrease, and the protein expressions of TGF-ß1 of human hypertrophic scar tissue in nude mice in 1 µmol/L SD-208 group were significantly lower than those in group NS (with t values from 6.2 to 19.1, P values below 0.01). CONCLUSIONS: SD-208 has significant inhibition effect on human hypertrophic scars, and the mechanism is correlated to the inhibition of protein expression of endogenous TGF-ß1.
[Mh] Termos MeSH primário: Cicatriz Hipertrófica
Pteridinas/farmacologia
Fator de Crescimento Transformador beta1
[Mh] Termos MeSH secundário: Animais
Movimento Celular
Fibroblastos
Seres Humanos
Camundongos Nus
Faloidina/análogos & derivados
Ratos
Rodaminas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pteridines); 0 (Rhodamines); 0 (SD-208); 0 (Transforming Growth Factor beta1); 0 (rhodamine-phalloidin); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160729
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1009-2587.2016.07.002


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[PMID]:27250943
[Au] Autor:Hagan IM
[Ad] Endereço:CRUK Cell Division Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, United Kingdom.
[Ti] Título:Staining Fission Yeast Filamentous Actin with Fluorescent Phalloidin Conjugates.
[So] Source:Cold Spring Harb Protoc;2016(6):pdb.prot091033, 2016 Jun 01.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Schizosaccharomyces pombe filamentous (F)-actin cytoskeleton drives cell growth, morphogenesis, endocytosis, and cytokinesis. The protocol described here reveals the distribution of F-actin in fixed cells through the use of fluorescently conjugated phalloidin. Simultaneous staining of cell wall landmarks (with calcofluor) and chromatin (with 4',6-diamidino-2-phenylindole, or DAPI) makes this rapid staining procedure highly effective for staging cell cycle progression, monitoring morphogenetic abnormalities, and assessing the impact of environmental and genetic changes on the integrity of the F-actin cytoskeleton.
[Mh] Termos MeSH primário: Actinas/análise
Corantes Fluorescentes/metabolismo
Microscopia de Fluorescência/métodos
Faloidina/metabolismo
Schizosaccharomyces/citologia
Coloração e Rotulagem/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Fluorescent Dyes); 17466-45-4 (Phalloidine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160603
[St] Status:MEDLINE
[do] DOI:10.1101/pdb.prot091033



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