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Pesquisa : A11.284.430.214.190.750.410 [Categoria DeCS]
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[PMID]:28935373
[Au] Autor:Chaves JM; Gupta R; Srivastava K; Srivastava O
[Ad] Endereço:Department of Optometry and Vision Science, University of Alabama at Birmingham, Birmingham, AL 35294, United States.
[Ti] Título:Human alpha A-crystallin missing N-terminal domain poorly complexes with filensin and phakinin.
[So] Source:Biochem Biophys Res Commun;494(1-2):402-408, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to determine relative importance of N-terminal domain and C-terminal extension of αA-crystallin during their in vitro complex formation with phakinin and filensin (the two lens-specific intermediate filament [IF] proteins). Cloned phakinin, filensin and vimentin were purified under a denaturing conditions by consecutive DEAE-cellulose-, hydroxyapatite- and Sephadex G-75-column chromatographic methods. WTαA-crystallin, αA-NT (N-terminal domain [residue number 1-63])-deleted and αA-CT (C-terminal terminal extension [residue number 140-173]-deleted), were cloned in pET 100 TOPO vector, expressed in BL-21 (DE3) cells using 1% IPTG, and purified using a Ni -affinity column. The following two in vitro methods were used to determine complex formation of WT-αA, αA-NT, or αA-CT with phakinin, filensin or both phakinin plus filensin together: an ultracentrifugation sedimentation (centrifugation at 80,000 × g for 30 min at 20 °C) followed by SDS-PAGE analysis, and an electron microscopic analysis. In the first method, the individual control proteins (WT-αA, αA-NT and αA-CT crystallin species) remained in the supernatant fractions whereas phakinin, filensin, and vimentin were recovered in the pellet fractions. On complex formation by individual WT-αA-, αA-NT or αA-CT-species with filensin, phakinin or both phakinin and filensin, WT-αA and αA-CT were recovered in the pellet fraction with phakinin, filensin or both filensin and phakinin, whereas αA-NT remained mostly in the supernatant, suggesting its poor complex formation property. EM-studies showed filamentous structure formation between WT-αA and αA-CT with phakinin or filensin, or with both filensin and phakinin together but relatively poor filamentous structures with αA-NT. Together, the results suggest that the N-terminal domain of αA-crystallin is required during in vitro complex formation with filensin and phakinin.
[Mh] Termos MeSH primário: Proteínas do Olho/metabolismo
Vetores Genéticos/química
Proteínas de Filamentos Intermediários/metabolismo
Cadeia A de alfa-Cristalina/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Clonagem Molecular
Escherichia coli/genética
Escherichia coli/metabolismo
Proteínas do Olho/genética
Proteínas do Olho/ultraestrutura
Expressão Gênica
Vetores Genéticos/metabolismo
Seres Humanos
Proteínas de Filamentos Intermediários/genética
Proteínas de Filamentos Intermediários/ultraestrutura
Filamentos Intermediários/metabolismo
Filamentos Intermediários/ultraestrutura
Cristalino/metabolismo
Cristalino/ultraestrutura
Microscopia Eletrônica
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Recombinantes/ultraestrutura
Cadeia A de alfa-Cristalina/genética
Cadeia A de alfa-Cristalina/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Intermediate Filament Proteins); 0 (Recombinant Proteins); 0 (alpha-Crystallin A Chain); 0 (filensin); 0 (phakinin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170923
[St] Status:MEDLINE


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[PMID]:28880872
[Au] Autor:Escobar-Aguirre M; Zhang H; Jamieson-Lucy A; Mullins MC
[Ad] Endereço:Department of Cell and Developmental Biology, University of Pennsylvania Perelman School of Medicine, 1152 BRBII/III, 421 Curie Blvd., Philadelphia, Pennsylvania, United States of America.
[Ti] Título:Microtubule-actin crosslinking factor 1 (Macf1) domain function in Balbiani body dissociation and nuclear positioning.
[So] Source:PLoS Genet;13(9):e1006983, 2017 Sep.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Animal-vegetal (AV) polarity of most vertebrate eggs is established during early oogenesis through the formation and disassembly of the Balbiani Body (Bb). The Bb is a structure conserved from insects to humans that appears as a large granule, similar to a mRNP granule composed of mRNA and proteins, that in addition contains mitochondria, ER and Golgi. The components of the Bb, which have amyloid-like properties, include germ cell and axis determinants of the embryo that are anchored to the vegetal cortex upon Bb disassembly. Our lab discovered in zebrafish the only gene known to function in Bb disassembly, microtubule-actin crosslinking factor 1a (macf1a). Macf1 is a conserved, giant multi-domain cytoskeletal linker protein that can interact with microtubules (MTs), actin filaments (AF), and intermediate filaments (IF). In macf1a mutant oocytes the Bb fails to dissociate, the nucleus is acentric, and AV polarity of the oocyte and egg fails to form. The cytoskeleton-dependent mechanism by which Macf1a regulates Bb mRNP granule dissociation was unknown. We found that disruption of AFs phenocopies the macf1a mutant phenotype, while MT disruption does not. We determined that cytokeratins (CK), a type of IF, are enriched in the Bb. We found that Macf1a localizes to the Bb, indicating a direct function in regulating its dissociation. We thus tested if Macf1a functions via its actin binding domain (ABD) and plectin repeat domain (PRD) to integrate cortical actin and Bb CK, respectively, to mediate Bb dissociation at the oocyte cortex. We developed a CRISPR/Cas9 approach to delete the exons encoding these domains from the macf1a endogenous locus, while maintaining the open reading frame. Our analysis shows that Macf1a functions via its ABD to mediate Bb granule dissociation and nuclear positioning, while the PRD is dispensable. We propose that Macf1a does not function via its canonical mechanism of linking two cytoskeletal systems together in dissociating the Bb. Instead our results suggest that Macf1a functions by linking one cytoskeletal system, cortical actin, to another structure, the Bb, where Macf1a is localized. Through this novel linking process, it dissociates the Bb at the oocyte cortex, thus specifying the AV axis of the oocyte and future egg. To our knowledge, this is also the first study to use genome editing to unravel the module-dependent function of a cytoskeletal linker.
[Mh] Termos MeSH primário: Polaridade Celular/genética
Oogênese/genética
Plaquinas/genética
Proteínas de Peixe-Zebra/genética
Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/genética
Animais
Células Germinativas/crescimento & desenvolvimento
Complexo de Golgi/genética
Seres Humanos
Filamentos Intermediários/genética
Microtúbulos/genética
Microtúbulos/metabolismo
Oócitos/crescimento & desenvolvimento
Oócitos/metabolismo
Peixe-Zebra/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MACF1 protein, zebrafish); 0 (Plakins); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006983


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[PMID]:28833372
[Au] Autor:Gesslbauer B; Hruby LA; Roche AD; Farina D; Blumer R; Aszmann OC
[Ad] Endereço:Christian Doppler Laboratory for Restoration of Extremity Function, Medical University of Vienna, Vienna, Austria.
[Ti] Título:Axonal components of nerves innervating the human arm.
[So] Source:Ann Neurol;82(3):396-408, 2017 Sep.
[Is] ISSN:1531-8249
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: Axons traveling within the brachial plexus are responsible for the dexterous control of human arm and hand movements. Despite comprehensive knowledge on the topographical anatomy of nerves innervating the human upper limbs, the definite quantity of sensory and motor axons within this neural network remains elusive. Our aim was to perform a quantitative analysis of the axonal components of human upper limb nerves based on highly specific molecular features from spinal cord level to the terminal nerves at wrist level. METHODS: Nerve specimen harvest at predefined harvesting sites (plexus roots and cords as well as major nerves originating from the brachial plexus innervating the arm and hand) was performed in 9 human heart-beating organ donors. Double immunofluorescence staining using antibodies against choline-acetyltransferase and neurofilament was performed to differentiate motor and sensory axons on nerve cross sections. RESULTS: Three hundred fifty thousand axons emerge from the spinal cord to innervate the human upper limb, of which 10% are motor neurons. In all nerves studied, sensory axons outnumber motor axons by a ratio of at least 9:1. The sensory axon contribution increases when moving distally, whereas only 1,700 motor axons reach the hand to innervate the intrinsic musculature. INTERPRETATION: Our results suggest that upper limb motor execution, and particularly dexterous coordination of hand movement, require an unexpectedly low number of motor neurons, with a large convergence of afferent input for feedback control. Ann Neurol 2017;82:396-408.
[Mh] Termos MeSH primário: Braço/inervação
Axônios/fisiologia
Neurônios Motores/fisiologia
Células Receptoras Sensoriais/fisiologia
[Mh] Termos MeSH secundário: Colina O-Acetiltransferase/metabolismo
Seres Humanos
Filamentos Intermediários/metabolismo
Células Receptoras Sensoriais/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.6 (Choline O-Acetyltransferase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1002/ana.25018


  4 / 3590 MEDLINE  
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[PMID]:28793217
[Au] Autor:Even C; Abramovici G; Delort F; Rigato AF; Bailleux V; de Sousa Moreira A; Vicart P; Rico F; Batonnet-Pichon S; Briki F
[Ad] Endereço:Laboratoire de Physique des Solides, CNRS, Université Paris Sud, Université Paris-Saclay, Orsay, France. Electronic address: catherine.even@u-psud.fr.
[Ti] Título:Mutation in the Core Structure of Desmin Intermediate Filaments Affects Myoblast Elasticity.
[So] Source:Biophys J;113(3):627-636, 2017 Aug 08.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Elastic properties of cells are mainly derived from the actin cytoskeleton. However, intermediate filaments are emerging as major contributors to the mechanical properties of cells. Using atomic force microscopy, we studied the elasticity of mouse myoblasts expressing a mutant form of the gene encoding for desmin intermediate filaments, p.D399Y. This variant produces desmin aggregates, the main pathological symptom of myofibrillar myopathies. Here we show that desmin-mutated cells display a 39% increased median elastic modulus compared to wild-type cells. Desmin-mutated cells required higher forces than wild-type cells to reach high indentation depths, where desmin intermediate filaments are typically located. In addition, heat-shock treatment increased the proportion of cells with aggregates and induced a secondary peak in the distribution of Young's moduli. By performing atomic force microscopy mechanical mapping combined with fluorescence microscopy, we show that higher Young's moduli were measured where desmin aggregates were located, indicating that desmin aggregates are rigid. Therefore, we provide evidence that p.D399Y stiffens mouse myoblasts. Based on these results, we suggest that p.D399Y-related myofibrillar myopathy is at least partly due to altered mechanical properties at the single-cell scale, which are propagated to the tissue scale.
[Mh] Termos MeSH primário: Desmina/química
Desmina/metabolismo
Elasticidade
Filamentos Intermediários/metabolismo
Mutação
Mioblastos/citologia
[Mh] Termos MeSH secundário: Linhagem Celular
Desmina/genética
Seres Humanos
Agregados Proteicos
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Desmin); 0 (Protein Aggregates)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE


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[PMID]:28666985
[Au] Autor:Silvander JSG; Kvarnström SM; Kumari-Ilieva A; Shrestha A; Alam CM; Toivola DM
[Ad] Endereço:Cell Biology, Biosciences, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.
[Ti] Título:Keratins regulate ß-cell mitochondrial morphology, motility, and homeostasis.
[So] Source:FASEB J;31(10):4578-4587, 2017 Oct.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Loss of the epithelial intermediate filament protein keratin 8 (K8) in murine ß cells leads to irregular insulin vesicles and decreased insulin levels. Because mitochondria are central in glucose-stimulated insulin secretion, the relationship between keratins and ß-cell mitochondrial function and morphology was investigated. ß cells in murine K8-knockout (K8 ) islets of Langerhans have increased numbers of mitochondria, which are rounder and have diffuse cristae, as seen by electron microscopy. The mitochondrial network in primary cultured K8 ß cells is more fragmented compared with K8 mitochondria, correlating with decreased levels of mitofusin 2 and the mitofusin 2- and keratin-binding protein trichoplein. K8 ß-cell mitochondria have decreased levels of total and mitochondrial cytochrome , which correlates with a reduction in electron transport complexes I and IV. This provokes loss of mitochondrial membrane potential and reduction of ATP and insulin amount, as seen in K8 ß cells. Mitochondria in K8 wild-type ß cells and MIN6 insulinoma cells overexpressing K8 and 18 are more stationary compared with mitochondria in keratin-deficient cells. In conclusion, keratins, likely through trichoplein-mitofusin interactions, regulate both structural and dynamic functions of ß-cell mitochondria, which could have implications for downstream insulin secretion.-Silvander, J. S. G., Kvarnström, S. M., Kumari-Ilieva, A., Shrestha, A., Alam, C. M., Toivola, D. M. Keratins regulate ß-cell mitochondrial morphology, motility, and homeostasis.
[Mh] Termos MeSH primário: Movimento Celular/fisiologia
Homeostase/fisiologia
Células Secretoras de Insulina/citologia
Células Secretoras de Insulina/metabolismo
Queratina-8/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Animais
Forma Celular
Células Cultivadas
Citocromos c/metabolismo
Hepatócitos/metabolismo
Proteínas de Filamentos Intermediários/metabolismo
Filamentos Intermediários/metabolismo
Queratina-8/deficiência
Camundongos Knockout
Mitocôndrias/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Intermediate Filament Proteins); 0 (Keratin-8); 9007-43-6 (Cytochromes c)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170702
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201700095R


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[PMID]:28654681
[Au] Autor:Zhao J; Brown K; Liem RKH
[Ad] Endereço:Department of Pathology and Cell Biology, Columbia University College of Physicians & Surgeons, New York, New York, United States of America.
[Ti] Título:Abnormal neurofilament inclusions and segregations in dorsal root ganglia of a Charcot-Marie-Tooth type 2E mouse model.
[So] Source:PLoS One;12(6):e0180038, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Charcot-Marie-Tooth (CMT) disease or hereditary motor and sensory neuropathy is the most prevalent inherited peripheral neuropathy and is associated with over 90 causative genes. Mutations in neurofilament light polypeptide gene, NEFL cause CMT2E, an axonal form of CMT that results in abnormal structures and/or functions of peripheral axons in spinal cord motor neurons and dorsal root ganglion neurons. We have previously generated and characterized a knock-in mouse model of CMT2E with the N98S mutation in Nefl that presented with multiple inclusions in spinal cord neurons. In this report, we conduct immunofluorescence studies of cultured dorsal root ganglia (DRG) from NeflN98S/+ mice, and show that inclusions found in DRG neurites can occur in embryonic stages. Ultrastructural analyses reveal that the inclusions are disordered neurofilaments packed in high density, segregated from other organelles. Immunochemical studies show decreased NFL protein levels in DRG, cerebellum and spinal cord in NeflN98S/+ mice, and total NFL protein pool is shifted toward the triton-insoluble fraction. Our findings reveal the nature of the inclusions in NeflN98S/+ mice, provide useful information to understand mechanisms of CMT2E disease, and identify DRG from NeflN98S/+ mice as a useful cell line model for therapeutic discoveries.
[Mh] Termos MeSH primário: Doença de Charcot-Marie-Tooth/patologia
Gânglios Espinais/patologia
Corpos de Inclusão/patologia
Filamentos Intermediários/patologia
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Cerebelo/metabolismo
Cerebelo/patologia
Doença de Charcot-Marie-Tooth/metabolismo
Modelos Animais de Doenças
Gânglios Espinais/metabolismo
Gânglios Espinais/ultraestrutura
Corpos de Inclusão/metabolismo
Corpos de Inclusão/ultraestrutura
Filamentos Intermediários/metabolismo
Filamentos Intermediários/ultraestrutura
Camundongos
Proteínas de Neurofilamentos/metabolismo
Medula Espinal/metabolismo
Medula Espinal/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neurofilament Proteins); 0 (neurofilament protein L)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180038


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[PMID]:28623820
[Au] Autor:Khmelinskii I; Golubeva T; Korneeva E; Inyushin M; Zueva L; Makarov V
[Ad] Endereço:Universidade do Algarve, FCT, DQF and CIQA, 8005-139 Faro, Portugal.
[Ti] Título:Spectral selectivity model for light transmission by the intermediate filaments in Müller cells.
[So] Source:J Photochem Photobiol B;173:282-290, 2017 Aug.
[Is] ISSN:1873-2682
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Presently we continue our studies of the quantum mechanism of light energy transmission in the form of excitons by axisymmetric nanostructures with electrically conductive walls. Using our theoretical model, we analyzed the light energy transmission by biopolymers forming optical channels within retinal Müller cells. There are specialized intermediate filaments (IF) 10-18nm in diameter, built of electrically conductive polypeptides. Presently, we analyzed the spectral selectivity of these nanostructures. We found that their transmission spectrum depends on their diameter and wall thickness. We also considered the classical approach, comparing the results with those predicted by the quantum mechanism. We performed experimental measurements on model quantum waveguides, made of rectangular nanometer-thick chromium (Cr) tracks. The optical spectrum of such waveguides varied with their thickness. We compared the experimental absorption/transmission spectra with those predicted by our model, with good agreement between the two. We report that the observed spectra may be explained by the same mechanisms as operating in metal nanolayers. Both the models and the experiment show that Cr nanotracks have high light transmission efficiency in a narrow spectral range, with the spectral maximum dependent on the layer thickness. Therefore, a set of intermediate filaments with different geometries may provide light transmission over the entire visible spectrum with a very high (~90%) efficiency. Thus, we believe that high contrast and visual resolution in daylight are provided by the quantum mechanism of energy transfer in the form of excitons, whereas the ultimate retinal sensitivity of the night vision is provided by the classical mechanism of photons transmitted by the Müller cell light-guides.
[Mh] Termos MeSH primário: Células Ependimogliais/classificação
Filamentos Intermediários/efeitos da radiação
Luz
Modelos Biológicos
[Mh] Termos MeSH secundário: Células Ependimogliais/efeitos da radiação
Filamentos Intermediários/metabolismo
Teoria Quântica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170618
[St] Status:MEDLINE


  8 / 3590 MEDLINE  
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[PMID]:28551375
[Au] Autor:Killilea AN; Csencsits R; Le EBNT; Patel AM; Kenny SJ; Xu K; Downing KH
[Ad] Endereço:Molecular Biophysics and Integrated Biomaging Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. Electronic address: ankillilea@berkeley.edu.
[Ti] Título:Cytoskeletal organization in microtentacles.
[So] Source:Exp Cell Res;357(2):291-298, 2017 Aug 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microtentacles are thin, flexible cell protrusions that have recently been described and whose presence enhances efficient attachment of circulating cells. They are found on circulating tumor cells and can be induced on a wide range of breast cancer cell lines, where they are promoted by factors that either stabilize microtubules or destabilize the actin cytoskeleton. Evidence suggests that they are relevant to the metastatic spread of cancer, so understanding their structure and formation may lead to useful therapies. Microtentacles are formed by microtubules and contain vimentin intermediate filaments, but beyond this, there is little information about their ultrastructure. We have used electron microscopy of high pressure frozen sections and tomography of cryo-prepared intact cells, along with super resolution fluorescence microscopy, to provide the first ultrastructural insights into microtubule and intermediate filament arrangement within microtentacles. By scanning electron microscopy it was seen that microtentacles form within minutes of addition of drugs that stabilize microtubules and destabilize actin filaments. Mature microtentacles were found to be well below one micrometer in diameter, tapering gradually to below 100nm at the distal ends. They also contained frequent branches and bulges suggestive of heterogeneous internal structure. Super resolution fluorescence microscopy and examination of sectioned samples showed that the microtubules and intermediate filaments can occupy different areas within the microtentacles, rather than interacting intimately as had been expected. Cryo-electron tomography of thin regions of microtentacles revealed densely packed microtubules and absence of intermediate filaments. The number of microtubules ranged from several dozen in some areas to just a few in the thinnest regions, with none of the regular arrangement found in axonemes. Improved understanding of the mechanism of microtentacle formation, as well as the resultant structure, will be valuable in developing therapies against metastasis, if the hypothesized role of microtentacles in metastasis is confirmed. This work provides a significant step in this direction.
[Mh] Termos MeSH primário: Fenômenos Fisiológicos Celulares/fisiologia
Filamentos Intermediários/metabolismo
Microtúbulos/metabolismo
Microtúbulos/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Seres Humanos
Filamentos Intermediários/ultraestrutura
Microscopia Eletrônica/métodos
Microscopia de Fluorescência/métodos
Vimentina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Vimentin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170529
[St] Status:MEDLINE


  9 / 3590 MEDLINE  
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Tilbery, Charles Peter
Texto completo SciELO Brasil
[PMID]:28444098
[Au] Autor:Domingues RB; Fernandes GBP; Leite FBVM; Tilbery CP; Thomaz RB; Silva GS; Mangueira CLP; Soares CAS
[Ad] Endereço:Senne Liquor Diagnóstico, São Paulo, SP, Brazil.
[Ti] Título:The cerebrospinal fluid in multiple sclerosis: far beyond the bands.
[So] Source:Einstein (Sao Paulo);15(1):100-104, 2017 Jan-Mar.
[Is] ISSN:2317-6385
[Cp] País de publicação:Brazil
[La] Idioma:eng; por
[Ab] Resumo:The cerebrospinal fluid analysis has been employed for supporting multiple sclerosis diagnosis and ruling out the differential diagnoses. The most classical findings reflect the inflammatory nature of the disease, including mild pleocytosis, mild protein increase, intrathecal synthesis of immunoglobulin G, and, most typically, the presence of oligoclonal bands. In recent years, new biomarkers have emerged in the context of multiple sclerosis. The search for new biomarkers reflect the need of a better evaluation of disease activity, disease progression, and treatment efficiency. A more refined evaluation of disease and therapy status can contribute to better therapeutic choices, particularly in escalation of therapies. This is very relevant taking into account the availability of a greater number of drugs for multiple sclerosis treatment in recent years. In this review, we critically evaluate the current literature regarding the most important cerebrospinal fluid biomarkers in multiple sclerosis. The determination of biomarkers levels, such as chemokine ligand 13, fetuin A, and mainly light neurofilament has shown promising results in the evaluation of this disease, providing information that along with clinical and neuroimaging data may contribute to better therapeutic decisions. RESUMO A análise do líquido cefalorraquidiano tem sido empregada para avaliação diagnóstica da esclerose múltipla e a exclusão dos diagnósticos diferenciais. Os achados clássicos refletem a natureza inflamatória da doença, incluindo discreta pleocitose, leve hiperproteinorraquia, aumento da síntese intratecal de imunoglobulina G e, mais tipicamente, a presença de bandas oligoclonais. Nos últimos anos, surgiram novos biomarcadores para esclerose múltipla, e esta busca por marcadores reflete a necessidade de melhor avaliar a atividade e a progressão da doença, bem como a eficácia terapêutica. Uma avaliação mais refinada da atividade da doença e da resposta aos medicamentos pode contribuir para melhores decisões terapêuticas, particularmente no que se refere à troca de medicação. Isto é muito importante nos dias de hoje, quando surgem novas opções medicamentosas. Neste artigo de revisão, avaliamos criticamente a literatura atual referente aos novos marcadores liquóricos na esclerose múltipla. A mensuração destes marcadores, como a quimiocina CXCL13, fetuína A e, principalmente, o neurofilamento de cadeia leve, demonstrou resultados promissores na avaliação da doença, provendo informações que, em conjunto com dados clínicos e de neuroimagem, podem contribuir para melhores decisões terapêuticas.
[Mh] Termos MeSH primário: Esclerose Múltipla/líquido cefalorraquidiano
[Mh] Termos MeSH secundário: Biomarcadores/líquido cefalorraquidiano
Citocinas/líquido cefalorraquidiano
Progressão da Doença
Seres Humanos
Filamentos Intermediários
Proteína Básica da Mielina/líquido cefalorraquidiano
alfa-2-Glicoproteína-HS/líquido cefalorraquidiano
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers); 0 (Cytokines); 0 (Myelin Basic Protein); 0 (alpha-2-HS-Glycoprotein)
[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:170427
[St] Status:MEDLINE


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[PMID]:28432079
[Au] Autor:Leduc C; Etienne-Manneville S
[Ad] Endereço:Institut Pasteur Paris, Cell Polarity, Migration and Cancer Unit, UMR 3691, Equipe Labellisée Ligue Contre le Cancer, Centre National de la Recherché Scientifique, 75724 Paris, France.
[Ti] Título:Regulation of microtubule-associated motors drives intermediate filament network polarization.
[So] Source:J Cell Biol;216(6):1689-1703, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intermediate filaments (IFs) are key players in the control of cell morphology and structure as well as in active processes such as cell polarization, migration, and mechanoresponses. However, the regulatory mechanisms controlling IF dynamics and organization in motile cells are still poorly understood. In this study, we investigate the mechanisms leading to the polarized rearrangement of the IF network along the polarity axis. Using photobleaching and photoconversion experiments in glial cells expressing vimentin, glial fibrillary acidic protein, and nestin, we show that the distribution of cytoplasmic IFs results from a continuous turnover based on the cooperation of an actin-dependent retrograde flow and anterograde and retrograde microtubule-dependent transports. During wound-induced astrocyte polarization, IF transport becomes directionally biased from the cell center toward the cell front. Such asymmetry in the transport is mainly caused by a Cdc42- and atypical PKC-dependent inhibition of dynein-dependent retrograde transport. Our results show how polarity signaling can affect the dynamic turnover of the IF network to promote the polarization of the network itself.
[Mh] Termos MeSH primário: Astrócitos/metabolismo
Movimento Celular
Polaridade Celular
Filamentos Intermediários/metabolismo
Microtúbulos/metabolismo
Neuroglia/metabolismo
Proteína Quinase C/metabolismo
Proteína cdc42 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Astrócitos/patologia
Linhagem Celular Tumoral
Dineínas/genética
Dineínas/metabolismo
Proteína Glial Fibrilar Ácida/metabolismo
Seres Humanos
Microscopia de Vídeo
Nestina/metabolismo
Neuroglia/patologia
Imagem Óptica
Proteína Quinase C/genética
Interferência de RNA
Ratos
Transdução de Sinais
Fatores de Tempo
Transfecção
Vimentina/metabolismo
Cicatrização
Proteína cdc42 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Actins); 0 (Glial Fibrillary Acidic Protein); 0 (NES protein, human); 0 (Nestin); 0 (Vimentin); EC 2.7.11.13 (PKC-3 protein); EC 2.7.11.13 (Protein Kinase C); EC 3.6.4.2 (Dyneins); EC 3.6.5.2 (cdc42 GTP-Binding Protein)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170913
[Lr] Data última revisão:
170913
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170423
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201607045



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