RESUMEN
BACKGROUND: Splenosis is a heterotropic implantation of splenic fragments onto exposed vascularised peritoneal and intrathoracic surfaces, following splenic injury or elective splenectomy. CASE PRESENTATION: A 60 year old cirrhotic patient was referred to us with a hepatic mass, suspected to be HCC in a cirrhotic liver. A computerized tomography scan (CT) demonstrated a cirrhotic liver with a 2 x 2.7 cm focal hypervascular nodule, lying peripherally at the junction of segment 7 and 8. Diagnostic laparoscopy demonstrated a 3 cm exofitic dark brown splenunculus attached to the diaphragm and indenting the surface of segment 7 of the liver. The lesion was easily resected laparoscopically and shaved from the live surface with no need for a liver resection. The histopathological assessment confirmed the diagnosis of splenunculus, with no evidence of neoplasia. CONCLUSION: Hepatic splenosis is not a rare event and should be suspected in patients with a history of splenic trauma or splenectomy. Correct diagnosis is essential and will determine subsequent management plans. In doubtful cases laparoscopic investigation can offere essential information and should be part of the standard protocol for investigating suspected splenosis.
Asunto(s)
Carcinoma Hepatocelular/diagnóstico , Hepatitis C Crónica/complicaciones , Laparoscopía , Cirrosis Hepática/complicaciones , Neoplasias Hepáticas/diagnóstico , Esplenosis/diagnóstico , Esplenosis/cirugía , alfa-Fetoproteínas/metabolismo , Biomarcadores/sangre , Carcinoma Hepatocelular/sangre , Carcinoma Hepatocelular/cirugía , Diagnóstico Diferencial , Hepatitis C Crónica/sangre , Humanos , Cirrosis Hepática/virología , Neoplasias Hepáticas/sangre , Neoplasias Hepáticas/cirugía , Masculino , Persona de Mediana Edad , Esplenosis/sangreRESUMEN
Aneurysms of the gastric and gastroepiploic arteries account for only about 4% of all splanchnic artery aneurysms. However, rupture is associated with a mortality of up to 70% and usually warrants urgent surgical intervention. We present an interesting case of a patient who presented with haematemasis following rupture of a left gastric artery aneurysm that was successfully treated by percutaneous thrombin injections. A review of the literature for this rare condition is also presented.
Asunto(s)
Aneurisma Roto/tratamiento farmacológico , Hemostáticos/uso terapéutico , Estómago/irrigación sanguínea , Trombina/uso terapéutico , Aneurisma Roto/diagnóstico por imagen , Arterias , Femenino , Hematemesis/tratamiento farmacológico , Hemostáticos/administración & dosificación , Humanos , Inyecciones , Persona de Mediana Edad , Estómago/diagnóstico por imagen , Trombina/administración & dosificación , Tomografía Computarizada por Rayos XRESUMEN
PURPOSE: Various strategies have recently emerged to improve the diagnostic prediction of prostate cancer (CaP). One such strategy includes the mass profiling of serum protein fractions selectively adsorbed onto chemically modified probes. In the current study we further validated this approach, while offering a more versatile, less expensive and yet equally predictive alternative to existing technologies. MATERIALS AND METHODS: A solid core lipophilic C-18 resin was used to extract and enrich the low molecular weight protein fraction from patient serum for further analysis by mass spectrometry. Mass spectra generated from a 48 patient training set were data mined using multivariate analysis to identify diagnostically significant protein peaks. These peaks were then used to test a blinded study set comprising 168 patients with common statistical algorithms and commercially available software packages. RESULTS: A total of 36 peaks generated from the training set were used to test the combined set of 168 serum samples obtained from 98 healthy individuals and 70 patients with CaP. We report a sensitivity of 94.1% and a specificity of 99.0% with 1 false-positive, 4 false-negative and 5 nondiagnosed cases. CONCLUSIONS: Our results further indicate that mass profiling of serological proteins provides a means for the accurate detection of CaP. In addition, our approach was found to be superior to chip based protocols, generating rich, sharp, highly reproducible spectra attainable in a high throughput manner and at minimal cost. This technique is also scaleable for subsequent protein characterization using multidimensional protein identification technologies. Finally, analyses of mass spectra with commercially available statistical applications was found to be highly effective in generating highly discriminatory m/z values for CaP diagnosis.
Asunto(s)
Biomarcadores de Tumor/análisis , Proteínas Sanguíneas/análisis , Neoplasias de la Próstata/diagnóstico , Proteoma/análisis , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción/métodos , Humanos , Procesamiento de Imagen Asistido por Computador , Masculino , Persona de Mediana Edad , Análisis Multivariante , Análisis por Matrices de Proteínas , Pruebas SerológicasRESUMEN
Quantification of the relationship between strain and excitation velocity in cardiac muscle gives important insights into the significance and contribution of microstructure and several transmembrane proteins to cardiac electrophysiology. In this study we introduce a measurement and analysis system for quantification of the relationship in papillary muscle of small mammals, superfused and kept in a physiological environment. A novelty of the approach is the extensive automation and computerization of the measurement and analysis procedure. Initial results indicate that the conduction velocity is strain dependent in such a manner that several components contribute to establish this relationship. Further studies will help to quantify the relationship and importance of the components.
Asunto(s)
Electrocardiografía/métodos , Procesamiento de Señales Asistido por Computador , Amplificadores Electrónicos , Conversión Analogo-Digital , Animales , Arritmias Cardíacas/fisiopatología , Mapeo del Potencial de Superficie Corporal/instrumentación , Mapeo del Potencial de Superficie Corporal/métodos , Sistemas de Computación , Enfermedad Coronaria/fisiopatología , Modelos Animales de Enfermedad , Perros , Suministros de Energía Eléctrica , Electrocardiografía/instrumentación , Diseño de Equipo , Frecuencia Cardíaca , Humanos , Almacenamiento y Recuperación de la Información , Infarto del Miocardio/fisiopatología , Isquemia Miocárdica/fisiopatología , Procesamiento de Señales Asistido por Computador/instrumentaciónAsunto(s)
Enfermedades del Sistema Digestivo/tratamiento farmacológico , Antagonistas de los Receptores H2 de la Histamina/uso terapéutico , Sucralfato/uso terapéutico , Método Doble Ciego , Quimioterapia Combinada , Úlcera Duodenal/tratamiento farmacológico , Femenino , Reflujo Gastroesofágico/tratamiento farmacológico , Humanos , Masculino , Persona de Mediana Edad , Estudios Multicéntricos como Asunto , Ensayos Clínicos Controlados Aleatorios como Asunto , Úlcera Gástrica/tratamiento farmacológicoRESUMEN
Employing a combination of static and dynamic light scattering, as well as differential scanning calorimetry (DSC), the structural changes which appear in alpha 2-macroglobulin (alpha 2M) upon trypsin binding have been further characterized. Light-scattering measurements suggest that a 15% reduction in both the hydrodynamic radius and radius of gyration occurs when two molecules of trypsin complex to alpha 2M. Approx. 85% of this trypsin-induced compaction results from the binding of the first proteinase. A complementary result was obtained from DSC measurements in which the major fraction of the trypsin-induced conversion of alpha 2M to a single more thermally stable form results from interaction with the first proteinase molecule. These observations support a functionally asymmetric model of trypsin binding to alpha 2M in which the significant reduction in size of the complex is primarily due to the initial interaction of alpha 2M with a single proteinase molecule.
Asunto(s)
Tripsina/metabolismo , alfa-Macroglobulinas/química , Rastreo Diferencial de Calorimetría , Humanos , Luz , Conformación Proteica , Dispersión de Radiación , alfa-Macroglobulinas/metabolismoRESUMEN
The effect of surface adsorption on the structure and stability of proteins is a matter of increasing interest in biotechnology. Therefore, we have examined the effect of adsorption to silica on the thermal stability of 7 proteins employing differential scanning calorimetry (DSC) and front surface fluorescence (FSF) spectroscopy. In general, it was found that surface adsorption decreased the thermal stability of the bound protein. Using lysozyme for further studies, DSC, FSF, and FTIR spectroscopies, as well as enzymatic activity measurements, were used to explore the effect of decreasing surface apolarity on stability. It was observed that increasing surface apolarity produced decreasing stability and increasing structural alteration of the adsorbed protein.
RESUMEN
A plunge electrode is made from a hypodermic needle with one side cut open and multiple electrodes exposed from tip to base. A method for constructing chlorided silver electrode plunge needles is explained as well as problems associated with electrode chloriding. The small surface area of these electrodes makes empirical methods of chloriding difficult to use. A monitor was constructed for the testing and chloriding of a twelve-electrode plunge needle. This system continuously measures the impedance of the electrodes during chloriding.
Asunto(s)
Electrodos , Ensayo de Materiales , Compuestos de Plata , Plata , Conductividad Eléctrica , Diseño de EquipoRESUMEN
Differential scanning calorimetry was performed on the five major lens crystallin fractions [HM-alpha, alpha, beta H, beta L, and (beta s + gamma)] of the bovine lens as well as on more purified forms of alpha- and gamma-crystallins. All were found to be relatively thermally stable although the alpha-crystallin were found to at least partially unfold at an approximately 10 degrees C lower temperature than the beta and gamma fractions. Increasing protein concentration had little effect on gamma-crystallin thermograms but had marked effects on those of the alpha- and beta-crystallins. Increases in the thermal stability with increasing protein concentration for the beta-crystallins can be explained most simply by the known beta L/beta H equilibrium, but, in the case of the alpha-crystallins, excluded volume effects may be an important factor. In both cases, the increased stability at high concentrations could be of physiological relevance. As well as the expected endothermic unfolding transitions, all of the lens crystallins revealed exothermic peaks that correlate with protein precipitation. Interestingly, this phenomenon occurs only after extensive structural alteration in the case of the alpha-crystallins but is present very early in the initial stages of structural perturbation of the beta- and gamma-crystallins.
Asunto(s)
Rastreo Diferencial de Calorimetría/métodos , Calorimetría/métodos , Cristalino , Animales , Bovinos , Conformación Proteica , TermodinámicaRESUMEN
Structures of four related neurotoxins and their purified subunits from the venoms of Crotalus durissus terrificus, C. vegrandis, C. s. scutulatus and C. viridis concolor were examined by circular dichroism (CD), deconvolution Fourier-transform infrared (FTIR) and fluorescence spectroscopy. CD spectra suggest that in general, the isolated subunits were decreased slightly in alpha-helix, while they were increased in beta-sheet structure, relative to intact toxins. These results were consistent with FTIR results. Fluorescence quenching (50-80%) was also observed in three of the four intact toxins as compared to spectra predicted by summation of free acidic and basic subunit spectra. It was tempting to conclude from these results that major conformational changes occur in individual subunits upon formation of the dimeric toxins. Intact crotoxin, however, when exposed to urea, yields spectra (CD, FTIR and fluorescence) that are virtually identical to control intact crotoxin. These findings suggest that the enhanced fluorescence exhibited by the isolated subunits, as well as the secondary structural changes in alpha-helix and beta-sheet, are artifacts resulting from irreversible structural changes that occur during subunit isolation by urea ion-exchange chromatography. In spite of these structural changes, LD50 values of intact crotoxin reassembled from isolated subunits are unaltered from those of native crotoxin.
Asunto(s)
Venenos de Crotálidos , Crotoxina , Animales , Dicroismo Circular , Venenos de Crotálidos/aislamiento & purificación , Crotoxina/aislamiento & purificación , Análisis de Fourier , Conformación Proteica , Serpientes , Especificidad de la Especie , Espectrometría de Fluorescencia , Espectrofotometría InfrarrojaRESUMEN
The interaction of three monoclonal rheumatoid factor IgM molecules with IgG antigens has been studied utilizing immunoglobulins isolated from three mixed cryoglobulins. Static light scattering measurements show that the stoichiometry of these immune complexes changes in a temperature-dependent manner from IgM(IgG)0-2 at temperatures greater than 37 degrees C to IgM(IgG)5 complexes at temperatures below 15 degrees C. These results were confirmed by the analysis of the composition of polyethyleneglycol-precipitated complexes. For one mixed cryoglobulin (Glo), temperature-dependent changes in stoichiometry were also verified by chemical cross-linking studies. Binding constants were determined by Scatchard analysis of light scattering data and by fluorescence polarization measurements. Values on the order of 10(5) M-1 were obtained for three monoclonal rheumatoid factor IgM molecules. Glo was further investigated by dynamic light scattering and partial specific volume measurements. Both dynamic light scattering and partial specific volume measurements provided evidence for surprising shape changes of the IgM X IgG complex as a function of temperature and IgG stoichiometry. Collectively, the data support the simple hypothesis that cryoprecipitation of mixed cryoglobulins occurs as a consequence of increases in the size (stoichiometry) of the complexes that are formed at low temperatures.
Asunto(s)
Crioglobulinemia/inmunología , Crioglobulinas/metabolismo , Crioglobulinas/aislamiento & purificación , Humanos , Cinética , Luz , Concentración Osmolar , Dispersión de Radiación , TermodinámicaRESUMEN
To test the hypothesis that conformational alterations might be involved in the elution of proteins from reversed-phase HPLC columns, the conformations of proteins bound onto a C-8 alkyl-bonded silica surface have been examined in the presence of increasing concentrations of the commonly employed eluent, 1-propanol. Using a combination of photoacoustic, diffuse reflectance deconvolution Fourier transform infrared and front face fluorescence spectroscopic techniques (to minimize interference from light scattering), the existence of surface-associated protein conformational changes induced by propanol is unequivocally demonstrated. The linear relationship found between the amount of propanol needed to elute proteins from C-8 columns and the midpoint of spectrally observed structural transitions is consistent with a role for conformational changes in the elution process.