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Pesquisa : E01.370.225.500.620.670.770 [Categoria DeCS]
Referências encontradas : 35 [refinar]
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[PMID]:24304999
[Au] Autor:Saleem A; Thomas EC; Wilkinson A; Azher M; Saleem N
[Ad] Endereço:Department of Respiratory Medicine, Bedford Hospital NHS Trust, Bedford, UK.
[Ti] Título:Bilateral miliary shadowing on chest X-ray.
[So] Source:J Coll Physicians Surg Pak;23(12):902-3, 2013 Dec.
[Is] ISSN:1681-7168
[Cp] País de publicação:Pakistan
[La] Idioma:eng
[Ab] Resumo:A patient presented with recent onset of increasing shortness of breath, weight loss and low-grade fever. His chest X-ray revealed bilateral miliary shadowing. He was investigated with CT-scanning of thorax. Later, a biopsy from supra-clavicular node and its immunocytochemistry studies confirmed metastasis from primary lung cancer. Primary lung cancer with miliary pulmonary metastases is a rare happening and is mostly associated with lung adenocarcinoma.
[Mh] Termos MeSH primário: Adenocarcinoma/patologia
Neoplasias Pulmonares/patologia
Metástase Neoplásica
Tuberculose Miliar/diagnóstico por imagem
[Mh] Termos MeSH secundário: Adenocarcinoma/diagnóstico por imagem
Adenocarcinoma/tratamento farmacológico
Antineoplásicos
Biópsia
Evolução Fatal
Seres Humanos
Neoplasias Pulmonares/diagnóstico por imagem
Neoplasias Pulmonares/tratamento farmacológico
Masculino
Meia-Idade
Sombreamento (Histologia)
Tomografia Computadorizada por Raios X
Tuberculose Miliar/complicações
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents)
[Em] Mês de entrada:1405
[Cu] Atualização por classe:161128
[Lr] Data última revisão:
161128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131206
[St] Status:MEDLINE
[do] DOI:12.2013/JCPSP.902903


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[PMID]:20461525
[Au] Autor:Taylor MC; Laber TL; Epstein BP; Zamzow DS; Baldwin DP
[Ad] Endereço:Institute of Environmental Science and Research Limited, Christchurch, New Zealand. michael.taylor@esr.cri.nz
[Ti] Título:The effect of firearm muzzle gases on the backspatter of blood.
[So] Source:Int J Legal Med;125(5):617-28, 2011 Sep.
[Is] ISSN:1437-1596
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Injuries caused by gunshots can produce what bloodstain pattern analysts know as "backspatter." Observations about the presence or absence of backspatter on an individual may be used in court as evidence of guilt or innocence. The discharge of three firearms (.22 caliber revolver, .38 caliber revolver, and .308 caliber rifle) and the resulting impact of bullets on a blood source were recorded using high-speed digital video imaging. Blood droplets, firearm muzzle gases, and ballistic shock waves were visualized using standard reflected light and shadowgraphy imaging techniques. A significant interaction between air currents, muzzle gases, and particulate material emanating from the firearms upon discharge with backspattered blood was observed. Blood droplets, initially spattered back toward the firearm and the shooter, were observed to change direction under the influence of firearm-induced air currents and were blown forward toward and beyond their original source location. Implications for experts testifying in court and for bloodstain pattern instructors are discussed.
[Mh] Termos MeSH primário: Manchas de Sangue
Armas de Fogo
Balística Forense/legislação & jurisprudência
Gases
Homicídio/legislação & jurisprudência
Ferimentos por Arma de Fogo/patologia
[Mh] Termos MeSH secundário: Movimentos do Ar
Seres Humanos
Iluminação/instrumentação
Iluminação/legislação & jurisprudência
Sombreamento (Histologia)/instrumentação
Gravação em Vídeo/instrumentação
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Gases)
[Em] Mês de entrada:1112
[Cu] Atualização por classe:170928
[Lr] Data última revisão:
170928
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100513
[St] Status:MEDLINE
[do] DOI:10.1007/s00414-010-0462-4


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[PMID]:20688161
[Au] Autor:Patel TR; Morris GA; Zwolanek D; Keene DR; Li J; Harding SE; Koch M; Stetefeld J
[Ad] Endereço:Department of Chemistry, University of Manitoba, 144 Dysart Road, Winnipeg, Manitoba, Canada R3T 2N2.
[Ti] Título:Nano-structure of the laminin γ-1 short arm reveals an extended and curved multidomain assembly.
[So] Source:Matrix Biol;29(7):565-72, 2010 Sep.
[Is] ISSN:1569-1802
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Laminins are multidomain glycoproteins that play important roles in development and maintenance of the extracellular matrix via their numerous interactions with other proteins. Several receptors for the laminin short arms revealed their importance in network formation and intercellular signaling. However, both the detailed structure of the laminin γ-1 short arm and its organization within the complexes is poorly understood due to the complexity of the molecule and the lack of a high-resolution structure. The presented data provide the first subatomic resolution structure for the laminin γ-1 short arm in solution. This was achieved using an integrated approach that combined a number of complementary biophysical techniques such as small angle X-ray scattering (SAXS), analytical ultracentrifugation, dynamic light scattering and electron microscopy. As a result of this study, we have obtained a significantly improved model for the laminin γ-1 short arm that represents a major step forward in molecular understanding of laminin-mediated complex formations.
[Mh] Termos MeSH primário: Laminina/química
Laminina/ultraestrutura
Proteínas Recombinantes/química
Proteínas Recombinantes/ultraestrutura
[Mh] Termos MeSH secundário: Seres Humanos
Hidrodinâmica
Laminina/genética
Luz
Microscopia Eletrônica de Transmissão
Modelos Moleculares
Peso Molecular
Tamanho da Partícula
Conformação Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes/genética
Espalhamento de Radiação
Espalhamento a Baixo Ângulo
Sombreamento (Histologia)/métodos
Software
Ultracentrifugação
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Laminin); 0 (Recombinant Proteins); 0 (laminin gamma 1)
[Em] Mês de entrada:1104
[Cu] Atualização por classe:101011
[Lr] Data última revisão:
101011
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:100807
[St] Status:MEDLINE
[do] DOI:10.1016/j.matbio.2010.07.004


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[PMID]:15929982
[Au] Autor:Gregory KE; Ono RN; Charbonneau NL; Kuo CL; Keene DR; Bächinger HP; Sakai LY
[Ad] Endereço:Shriners Hospital for Children, Portland, Oregon 97239, USA.
[Ti] Título:The prodomain of BMP-7 targets the BMP-7 complex to the extracellular matrix.
[So] Source:J Biol Chem;280(30):27970-80, 2005 Jul 29.
[Is] ISSN:0021-9258
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biochemical and biophysical methods are used to show that BMP-7 is secreted as a stable complex consisting of the processed growth factor dimer noncovalently associated with its two prodomain propeptide chains and that the BMP-7 complex is structurally similar to the small transforming growth factor beta (TGFbeta) complex. Because the prodomain of TGFbeta interacts with latent TGFbeta-binding proteins, a family of molecules homologous to the fibrillins, the prodomain of BMP-7 was tested for binding to fibrillin-1 or to LTBP-1. The BMP-7 prodomain and BMP-7 complex, but not the separated growth factor dimer, interact with N-terminal regions of fibrillin-1. This interaction may target the BMP-7 complex to fibrillin microfibrils in the extracellular matrix. Immunolocalization of BMP-7 in tissues like the kidney capsule and skin reveals co-localization with fibrillin. However, BMP-7 immunolocalization in other tissues known to be active sites for BMP-7 signaling is not apparent, suggesting that immunolocalization of BMP-7 in certain tissues represents specific extracellular storage sites. These studies suggest that the prodomains of TGFbeta-like growth factors are important for positioning and concentrating growth factors in the extracellular matrix. In addition, they raise the possibility that prodomains of other TGFbeta-like growth factors interact with fibrillins and/or LTBPs and are also targeted to the extracellular matrix.
[Mh] Termos MeSH primário: Proteínas Morfogenéticas Ósseas/química
Matriz Extracelular/metabolismo
Fator de Crescimento Transformador beta/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Proteína Morfogenética Óssea 7
Proteínas Morfogenéticas Ósseas/fisiologia
Linhagem Celular
DNA Complementar/metabolismo
Dimerização
Ensaio de Imunoadsorção Enzimática
Fibrilina-1
Fibrilinas
Glucosídeos/farmacologia
Histidina/química
Seres Humanos
Concentração de Íons de Hidrogênio
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Rim/embriologia
Proteínas de Ligação a TGF-beta Latente
Luz
Camundongos
Camundongos Endogâmicos BALB C
Proteínas dos Microfilamentos/química
Proteínas dos Microfilamentos/metabolismo
Microscopia Eletrônica
Microscopia de Fluorescência
Dados de Sequência Molecular
Ligação Proteica
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Espalhamento de Radiação
Sombreamento (Histologia)
Transdução de Sinais
Fator de Crescimento Transformador beta/metabolismo
Fator de Crescimento Transformador beta/fisiologia
Raios Ultravioleta
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (BMP7 protein, human); 0 (Bone Morphogenetic Protein 7); 0 (Bone Morphogenetic Proteins); 0 (DNA, Complementary); 0 (FBN1 protein, human); 0 (Fbn1 protein, mouse); 0 (Fibrillin-1); 0 (Fibrillins); 0 (Glucosides); 0 (Intracellular Signaling Peptides and Proteins); 0 (LTBP1 protein, human); 0 (Latent TGF-beta Binding Proteins); 0 (Ltbp1 protein, mouse); 0 (Microfilament Proteins); 0 (Recombinant Proteins); 0 (Transforming Growth Factor beta); 29836-26-8 (octyl-beta-D-glucoside); 4QD397987E (Histidine)
[Em] Mês de entrada:0509
[Cu] Atualização por classe:161124
[Lr] Data última revisão:
161124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050603
[St] Status:MEDLINE


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[PMID]:15764287
[Au] Autor:Kumar V
[Ad] Endereço:Electron Microscopy Department, Central JALMA Institute for Leprosy & other Mycobacterial Diseases, Indian Council of Medical Research, Taj Ganj, Agra 282001, India. vkjalma@yahoo.com
[Ti] Título:High resolution shadowing of Mycobacterium leprae.
[So] Source:Biotech Histochem;79(5-6):197-201, 2004 Oct-Dec.
[Is] ISSN:1052-0295
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Metal shadow casting techniques for transmission electron microscopic examination was used to determine the morphological characteristics of Mycobacterium leprae in untreated and treated patients. This technique is used to visualize bacterial surface structures by thermal evaporation of platinum alloys under moderate vacuum. This method gives a high contrast image at relatively low resolution and is useful for correlating micro-morphology quantitatively to early therapeutic effects of anti-leprosy drugs. Using these techniques in untreated cases, the surface structures of M. leprae were uniformly filled with relatively homogenous protoplasm surrounded by a cell wall. Most of the bacilli had thick cell walls with prominent banded and fibrous structures on the surface of the cell body. The cell wall was not detached in any of the solid bacilli in untreated cases. The bacilli varied in size and some of them were swollen in their mid-portion. Some bacilli were very short and completely filled with cytoplasm; therefore, these short bacilli were counted as solid bacilli in electron microscopic morphological index (EM-MI) determination. During treatment, mainly the cytoplasms of the bacilli were affected, and degeneration was observed. Ultrastructurally, the cytoplasm was shrunken and detached from the cell wall indicating mild degeneration. After moderate degeneration, the cytoplasm appeared fragmented. In advanced degeneration, all structures except the cell walls collapsed completely and no fibrous or band structures were visible on the surfaces of the cell walls. Therefore, these bacilli were counted as non-solid bacilli for EM-MI determination. This study shows that transmission electron shadowing gives more accurate counts than standard light microscopy of intact M. leprae bacilli in patient specimens.
[Mh] Termos MeSH primário: Mycobacterium leprae/ultraestrutura
[Mh] Termos MeSH secundário: Seres Humanos
Hansenostáticos/uso terapêutico
Hanseníase Virchowiana/tratamento farmacológico
Hanseníase Virchowiana/microbiologia
Microscopia Eletrônica
Mycobacterium leprae/efeitos dos fármacos
Sombreamento (Histologia)
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Leprostatic Agents)
[Em] Mês de entrada:0506
[Cu] Atualização por classe:050314
[Lr] Data última revisão:
050314
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:050315
[St] Status:MEDLINE


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[PMID]:12884020
[Au] Autor:Oliveira-Menezes A; De Souza W; Lanfredi RM
[Ad] Endereço:Laboratório de Helmintologia, Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Centro de Ciências da Saúde, Bloco G, 21949-900 Ilha do Fundão, Rio de Janeiro, RJ, Brazil.
[Ti] Título:Cuticular Architecture of Hassalstrongylus epsilon (Nematoda: Trichostrongyloidea).
[So] Source:Parasitol Res;90(4):280-6, 2003 Jul.
[Is] ISSN:0932-0113
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Hassalstrongylus epsilon is a small nematode, whose adult forms are found among the intestinal microvilli of the water rat Nectomys squamipes, Brants 1827 (Rodentia: Muridae). The external appearance of the cuticle, which presents transversal striations and longitudinal ridges, is described using scanning electron microscopy. Transmission electron microscopy of thin sections and replicas of quick-frozen, freeze-fractured, deep-etched and rotatory shadowed samples showed the presence in the cuticle of struts that arise from the fluid median layer, extending outward to the epicuticle. The cuticle showed the presence of five layers: epicuticle, cortical, fibril-rich, fluid median and fibrous. The cuticle layers were made of an assemblage of fibers that create compartments, which were larger in the fluid region than in the fibril-rich median layer.
[Mh] Termos MeSH primário: Intestino Delgado/parasitologia
Muridae/parasitologia
Trichostrongyloidea/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Técnica de Congelamento e Réplica/métodos
Técnica de Fratura por Congelamento/métodos
Intestino Delgado/citologia
Microscopia Eletrônica
Microscopia Eletrônica de Varredura
Microvilosidades/parasitologia
Microvilosidades/ultraestrutura
Ratos
Sombreamento (Histologia)/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Em] Mês de entrada:0310
[Cu] Atualização por classe:171007
[Lr] Data última revisão:
171007
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:030729
[St] Status:MEDLINE


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[PMID]:12524616
[Au] Autor:Dijkgraaf LC; Zardeneta G; Cordewener FW; Liem RS; Schmitz JP; de Bont LG; Milam SB
[Ad] Endereço:Department of Oral and Maxillofacial Surgery, Groningen University Hospital, The Netherlands. l.c.digkgraaf@kchir. azg.nl
[Ti] Título:Crosslinking of fibrinogen and fibronectin by free radicals: a possible initial step in adhesion formation in osteoarthritis of the temporomandibular joint.
[So] Source:J Oral Maxillofac Surg;61(1):101-11, 2003 Jan.
[Is] ISSN:0278-2391
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Adhesion formation in osteoarthritis (OA) of the temporomandibular joint (TMJ) typically results in a sustained limitation of joint movement. We propose the hypothesis that free-radical-mediated crosslinking of proteins underlies this adhesion formation in affected joints. Free radicals may cause oxidative modification of proteins, creating an opportunity for the formation of intramolecular and intermolecular crosslinks via covalent bonds. This may stabilize protein aggregates, rendering them more resistant to degradation. In this study, the free-radical-mediated crosslinking of model proteins (fibrinogen and fibronectin) was investigated to test our hypothesis that free radicals contribute to adhesion formation via this mechanism in OA of the TMJ. MATERIALS AND METHODS: Physiological clot formation of fibrinogen by thrombin and free-radical-induced crosslinking of fibrinogen and of fibronectin were analyzed using spectrophotometric turbidity measurements, light-scattering techniques, polyacrylamide gel electrophoresis (PAGE), and rotary shadowing. RESULTS: Fibrinogen was shown to aggregate after free radical treatment, as detected using turbidity measurements and light-scattering techniques. Using PAGE, fibrinogen as well as fibronectin was shown to degrade under low oxidative stress. Under high oxidative stress, however, fragments from both proteins were found to be covalently crosslinked, resulting in high-molecular-weight protein aggregates. The aggregation was shown to be at random with rotary shadowing. CONCLUSION: The study shows that high oxidative stress contributes to the formation of crosslinked proteins that may serve as an initial scaffolding for the development of adhesions frequently seen in OA of the TMJ.
[Mh] Termos MeSH primário: Fibrinogênio/química
Fibronectinas/química
Osteoartrite/etiologia
Transtornos da Articulação Temporomandibular/etiologia
[Mh] Termos MeSH secundário: Reagentes para Ligações Cruzadas/química
Densitometria
Eletroforese em Gel de Poliacrilamida
Compostos Ferrosos/química
Radicais Livres/química
Seres Humanos
Luz
Microscopia Eletrônica
Nefelometria e Turbidimetria
Oxirredução
Estresse Oxidativo
Ligação Proteica
Espécies Reativas de Oxigênio/química
Espalhamento de Radiação
Sombreamento (Histologia)
Espectrofotometria
Aderências Teciduais/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cross-Linking Reagents); 0 (Ferrous Compounds); 0 (Fibronectins); 0 (Free Radicals); 0 (Reactive Oxygen Species); 39R4TAN1VT (ferrous sulfate); 9001-32-5 (Fibrinogen)
[Em] Mês de entrada:0301
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:AIM; D; IM
[Da] Data de entrada para processamento:030114
[St] Status:MEDLINE


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[PMID]:12473462
[Au] Autor:Zampighi GA; Kreman M; Lanzavecchia S; Turk E; Eskandari S; Zampighi L; Wright EM
[Ad] Endereço:Department of Neurobiology, UCLA School of Medicine, Los Angeles, CA 90095-1763, USA. gzampighi@mednet.ucla.edu
[Ti] Título:Structure of functional single AQP0 channels in phospholipid membranes.
[So] Source:J Mol Biol;325(1):201-10, 2003 Jan 03.
[Is] ISSN:0022-2836
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aquaporin-0 (AQP0) is the most prevalent intrinsic protein in the plasma membrane of lens fiber cells where it functions as a water selective channel and also participates in fiber-fiber adhesion. We report the 3D envelope of purified AQP0 reconstituted with random orientation in phospholipid bilayers as single particles. The envelope was obtained by combining freeze-fracture, shadowing and random conical tilt electron microscopy followed by single particle image processing. Two-dimensional analysis of 2547 untilted images produced eight class averages exhibiting "square" and "octagonal" shapes with a continuum of variation. We reconstructed in 3D five class averages that best described the data set. The reconstructions ("molds") appeared as metal cups exhibiting external and internal surfaces. We used the internal surface of the mold to calculate the "imprints" that represent the AQP0 particles protruding from the hydrophobic core of the phospholipid bilayer. The complete envelope of the channel, formed by joining the square and octagonal imprints, described accurately the size, shape, oligomeric state, orientation, and molecular weight of the AQP0 channel inserted in the phospholipid bilayer. Rigid body docking of the atomic model of the aquaporin-1 (AQP1) tetramer showed that the freeze-fracture envelope accounted for the conserved transmembrane domain (approximately 73% similarity between AQP0 and AQP1) but not for the amino and carboxyl termini. We suggest that the discrepancy might reflect differences in the location of the amino and carboxyl termini in the crystal and in the phospholipid bilayer.
[Mh] Termos MeSH primário: Membrana Celular/química
Membrana Celular/metabolismo
Proteínas do Olho/química
Proteínas do Olho/metabolismo
Glicoproteínas de Membrana/química
Glicoproteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Aquaporina 1
Aquaporinas/química
Bovinos
Cristalografia por Raios X
Proteínas do Olho/ultraestrutura
Técnica de Fratura por Congelamento
Imagem Tridimensional
Cristalino/química
Glicoproteínas de Membrana/ultraestrutura
Microscopia Eletrônica de Varredura
Modelos Moleculares
Estrutura Quaternária de Proteína
Sombreamento (Histologia)
Eletricidade Estática
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Aquaporins); 0 (Eye Proteins); 0 (Membrane Glycoproteins); 0 (aquaporin 0); 146410-94-8 (Aquaporin 1)
[Em] Mês de entrada:0301
[Cu] Atualização por classe:081121
[Lr] Data última revisão:
081121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:021211
[St] Status:MEDLINE


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PubMed Central Texto completo
[PMID]:12006649
[Au] Autor:Rybakova IN; Patel JR; Davies KE; Yurchenco PD; Ervasti JM
[Ad] Endereço:Department of Physiology, University of Wisconsin Medical School, Madison 53706, USA.
[Ti] Título:Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle.
[So] Source:Mol Biol Cell;13(5):1512-21, 2002 May.
[Is] ISSN:1059-1524
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dystrophin is widely thought to mechanically link the cortical cytoskeleton with the muscle sarcolemma. Although the dystrophin homolog utrophin can functionally compensate for dystrophin in mice, recent studies question whether utrophin can bind laterally along actin filaments and anchor filaments to the sarcolemma. Herein, we have expressed full-length recombinant utrophin and show that the purified protein is fully soluble with a native molecular weight and molecular dimensions indicative of monomers. We demonstrate that like dystrophin, utrophin can form an extensive lateral association with actin filaments and protect actin filaments from depolymerization in vitro. However, utrophin binds laterally along actin filaments through contribution of acidic spectrin-like repeats rather than the cluster of basic repeats used by dystrophin. We also show that the defective linkage between costameric actin filaments and the sarcolemma in dystrophin-deficient mdx muscle is rescued by overexpression of utrophin. Our results demonstrate that utrophin and dystrophin are functionally interchangeable actin binding proteins, but that the molecular epitopes important for filament binding differ between the two proteins. More generally, our results raise the possibility that spectrin-like repeats may enable some members of the plakin family of cytolinkers to laterally bind and stabilize actin filaments.
[Mh] Termos MeSH primário: Actinas/metabolismo
Proteínas do Citoesqueleto/metabolismo
Distrofina/metabolismo
Proteínas de Membrana/metabolismo
Sarcolema/metabolismo
[Mh] Termos MeSH secundário: Animais
Proteínas do Citoesqueleto/genética
Proteínas do Citoesqueleto/isolamento & purificação
Proteínas de Membrana/genética
Proteínas de Membrana/isolamento & purificação
Camundongos
Camundongos Endogâmicos mdx
Músculo Esquelético/metabolismo
Ligação Proteica
Sombreamento (Histologia)
Utrofina
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Actins); 0 (Cytoskeletal Proteins); 0 (Dystrophin); 0 (Membrane Proteins); 0 (Utrn protein, mouse); 0 (Utrophin)
[Em] Mês de entrada:0211
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020515
[St] Status:MEDLINE


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[PMID]:11703654
[Au] Autor:Kajava AV; Cheng N; Cleaver R; Kessel M; Simon MN; Willery E; Jacob-Dubuisson F; Locht C; Steven AC
[Ad] Endereço:Center for Molecular Modeling, National Institute of Arthritis, Musculoskeletal and Skin Diseases, National Institutes of Health, Bldg 6, Room B2-34, MSC 2717, Bethesda, MD 20892-2717, USA.
[Ti] Título:Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins.
[So] Source:Mol Microbiol;42(2):279-92, 2001 Oct.
[Is] ISSN:0950-382X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bordetella pertussis establishes infection by attaching to epithelial cells of the respiratory tract. One of its adhesins is filamentous haemagglutinin (FHA), a 500-A-long secreted protein that is rich in beta-structure and contains two regions, R1 and R2, of tandem 19-residue repeats. Two models have been proposed in which the central shaft is (i) a hairpin made up of a pairing of two long antiparallel beta-sheets; or (ii) a beta-helix in which the polypeptide chain is coiled to form three long parallel beta-sheets. We have analysed a truncated variant of FHA by electron microscopy (negative staining, shadowing and scanning transmission electron microscopy of unstained specimens): these observations support the latter model. Further support comes from detailed sequence analysis and molecular modelling studies. We applied a profile search method to the sequences adjacent to and between R1 and R2 and found additional "covert" copies of the same motifs that may be recognized in overt form in the R1 and R2 sequence repeats. Their total number is sufficient to support the tenet of the beta-helix model that the shaft domain--a 350 A rod--should consist of a continuous run of these motifs, apart from loop inserts. The N-terminus, which does not contain such repeats, was found to be weakly homologous to cyclodextrin transferase, a protein of known immunoglobulin-like structure. Drawing on crystal structures of known beta-helical proteins, we developed structural models of the coil motifs putatively formed by the R1 and R2 repeats. Finally, we applied the same profile search method to the sequence database and found several other proteins--all large secreted proteins of bacterial provenance--that have similar repeats and probably also similar structures.
[Mh] Termos MeSH primário: Adesinas Bacterianas/química
Bordetella pertussis/química
Hemaglutininas/química
Fatores de Virulência de Bordetella
[Mh] Termos MeSH secundário: Adesinas Bacterianas/metabolismo
Adesinas Bacterianas/ultraestrutura
Motivos de Aminoácidos
Sequência de Aminoácidos
Antígenos de Bactérias/química
Antígenos de Bactérias/ultraestrutura
Vacinas Bacterianas
Hemaglutininas/metabolismo
Hemaglutininas/ultraestrutura
Microscopia Eletrônica de Transmissão e Varredura
Modelos Moleculares
Dados de Sequência Molecular
Peso Molecular
Coloração Negativa
Estrutura Secundária de Proteína
Estrutura Terciária de Proteína
Sequências Repetitivas de Aminoácidos
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Sombreamento (Histologia)
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; RESEARCH SUPPORT, U.S. GOV'T, P.H.S.
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antigens, Bacterial); 0 (Bacterial Vaccines); 0 (Hemagglutinins); 0 (Virulence Factors, Bordetella); 0 (filamentous hemagglutinin adhesin, Bordetella pertussis)
[Em] Mês de entrada:0207
[Cu] Atualização por classe:071114
[Lr] Data última revisão:
071114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:011113
[St] Status:MEDLINE



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