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1.
Eur Radiol ; 21(2): 318-25, 2011 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-20694795

RESUMO

OBJECTIVE: Agreement rate between magnetic resonance imaging (MRI) and Doppler ultrasound (DUS) for the detection of deep vein thrombosis (DVT) in the lower extremities was attempted by using the intravascular MRI contrast agent gadofosveset trisodium. The potential of this method to detect pulmonary embolism (PE) was also evaluated. MATERIAL AND METHODS: Forty-three consecutive inpatients with ultrasound-confirmed DVT but no clinical signs of PE were prospectively enrolled in this feasibility study. MRI was performed after a single injection of gadofosveset trisodium. The pulmonary arteries were imaged using a 3D Fast Low Angle Shot (FLASH) gradient recalled echo sequence. Additionally, pulmonary arteries, abdominal veins, pelvic and leg veins were imaged using a fat-suppressed 3D gradient echo Volume Interpolated Breath-hold Examination (VIBE FS). RESULTS: Gadofosveset trisodium-enhanced MRI detected more thrombi in the pelvic region, upper leg and lower leg than the initial DUS. In addition, PE was detected in 16 of the 43 DVT patients (37%). CONCLUSION: This study shows the feasibility of a combined protocol for the MRI diagnosis of DVT and PE using gadofosveset trisodium. This procedure is not only more sensitive in detecting DVT compared to standard DUS, but is also able to detect PE in asymptomatic patients.


Assuntos
Gadolínio/administração & dosagem , Angiografia por Ressonância Magnética/métodos , Compostos Organometálicos/administração & dosagem , Embolia Pulmonar/complicações , Embolia Pulmonar/patologia , Trombose Venosa/complicações , Trombose Venosa/patologia , Adulto , Idoso , Idoso de 80 Anos ou mais , Meios de Contraste/administração & dosagem , Feminino , Humanos , Injeções Intra-Arteriais , Masculino , Pessoa de Meia-Idade , Artéria Pulmonar/patologia , Reprodutibilidade dos Testes , Sensibilidade e Especificidade
2.
BMC Res Notes ; 3: 7, 2010 Jan 18.
Artigo em Inglês | MEDLINE | ID: mdl-20180968

RESUMO

BACKGROUND: The isolation of intact RNA can be very difficult when tissues are used that contain many RNAses or that are hard to homogenize, e.g. cartilage samples. Additionally, cartilaginous tissues are characterized by a low cellularity and an abundance of extracellular matrix (ECM) molecules. But given the growing interest in understanding pathogenesis of degenerative diseases, e.g. osteoarthritis (OA) and rheumatoid arthritis (RA), studies have to consider expression pattern of cells in its natural environment. FINDINGS: We compared the current RNA isolation methods for the extraction of high-quality RNA of snap-frozen biopsies from limited amounts of hypocellular cartilaginous tissue. The focus of the study was to gather information about procedure-related differences in RNA quality and yield. Here, we describe two protocols, the phenol/chloroform-free filter-based method (RNAqueous kit) and the combined protocol (TRIzol(R)/RNeasy Mini kit), working in a reproducible and reliable manner. CONCLUSIONS: We conclude that preparation, storage, homogenization, and quality control are altogether critical steps for in-depth analysis of differential gene expression, especially in hypocellular tissues with highly crosslinked ECM like cartilage.

3.
Dev Cell ; 11(2): 191-201, 2006 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-16890159

RESUMO

Many viruses modify cellular processes for their own benefit. The enterovirus 3A protein inhibits endoplasmic reticulum (ER)-to-Golgi transport, a function previously suggested to be important for viral suppression of immune responses. Here, we show that a virus carrying a 3A protein defective in inhibiting ER-to-Golgi transport is indeed less virulent in mice, and we unravel the mechanism by which 3A inhibits this trafficking step. Evidence is provided that 3A inhibits the activation of the GTPase ADP-ribosylation factor 1 (Arf1), which regulates the recruitment of the COP-I coat complex to membranes. 3A specifically inhibits the function of GBF1, a guanine nucleotide exchange factor for Arf1, by interacting with its N terminus. By specifically interfering with GBF1-mediated Arf1 activation, 3A may prove a valuable tool in dissecting the early steps of the secretory pathway.


Assuntos
Fator 1 de Ribosilação do ADP/antagonistas & inibidores , Complexo I de Proteína do Envoltório/metabolismo , Fatores de Troca do Nucleotídeo Guanina/antagonistas & inibidores , Proteínas Virais/farmacologia , Fator 1 de Ribosilação do ADP/metabolismo , Animais , Linhagem Celular , Membrana Celular/efeitos dos fármacos , Membrana Celular/fisiologia , Membrana Celular/ultraestrutura , Chlorocebus aethiops , Complexo I de Proteína do Envoltório/efeitos dos fármacos , Retículo Endoplasmático/efeitos dos fármacos , Retículo Endoplasmático/fisiologia , Complexo de Golgi/efeitos dos fármacos , Complexo de Golgi/fisiologia , Fatores de Troca do Nucleotídeo Guanina/biossíntese , Fatores de Troca do Nucleotídeo Guanina/fisiologia , Camundongos , Modelos Animais , Transporte Proteico/efeitos dos fármacos , Transporte Proteico/fisiologia
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