Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 8 de 8
Filtrar
Más filtros











Base de datos
Intervalo de año de publicación
1.
J Nanosci Nanotechnol ; 19(3): 1580-1584, 2019 Mar 01.
Artículo en Inglés | MEDLINE | ID: mdl-30469226

RESUMEN

Cordierite is an alumina-magnesia-silica compound widely used as a thermal shock resistant material due to its high thermal shock resistance, low coefficient of thermal expansion (CTE), low dielectric constant, and good electrical insulation. However, its narrow sintering temperature range and low mechanical strength hinder its application in ceramic heaters. Although mullite shows excellent thermal and chemical stability, heat resistance, and mechanical strength, it has the disadvantages of high sintering temperatures (1600-1700 °C) and poor thermal shock resistance. In this study, a composite phase was prepared by mixing cordierite and mullite to expand the narrow sintering temperature range of cordierite and adjust its CTE to be similar to that of Si. Furthermore, Y2O3 was added to reduce the sintering temperature and to increase the mechanical strength. Therefore, the composite showed the highest density of 2.5 g/cm³ at 1380 °C when the ratio of mullite to cordierite was 20 wt%. When 11 wt% Y2O3 was added to this composition, the highest density was 2.8 g/cm³ for a sintering temperature of 1320 °C, and the mechanical strength was relatively good as 180 MPa of 3-points bending strength was comparatively good. The CTE was 2.6×10-6.K-1, which was similar to that of Si.

2.
Mol Med Rep ; 1(3): 343-6, 2008.
Artículo en Inglés | MEDLINE | ID: mdl-21479415

RESUMEN

The objective of this study was to examine the antitumor effect of ZD6474, an orally available inhibitor of the vascular endothelial growth factor receptor-2 (VEGFR-2) and the epidermal growth factor receptor (EGFR), on tumor growth in an orthotopic metastatic brain tumor model. In order to determine the antitumor mechanism of ZD6474 treatment, in vitro and in vivo studies were performed. Human breast carcinoma cells (MDA-MB-435) were injected using direct intracranial (IC) inoculation (5x105 cells/100 µl) and internal carotid artery (ICA) injection (5x104 cells/100 µl) in Balb/c-nu female mice. Daily oral treatment with ZD6474 (50 mg/kg) was initiated on day 14 after the establishment of micrometastasis. Mice (n=12 per group) were sacrificed on day 28. Western blot analysis revealed that the autophosphorylation of EGFR and Akt was increasingly decreased with ZD6474 treatment in lung and brain endothelial cells and the MDA-MB-435 cell line. MTT assay also showed that the in vitro antitumor activity of ZD6474 was dependent on EGFR tyrosine kinase inhibition at a higher dose. Daily oral treatment with ZD6474 led to marked inhibition of metastatic tumor growth in the ICA injection and the direct IC inoculation models (median size 3.5 mm3, range 1.6-13.9 mm3) as compared to the control group (median size 62.4 mm3, range 11.5-206.9 mm3). These results suggest that simultaneous inhibition of both the EGFR and VEGFR-2 signaling pathways has a valuable therapeutic effect through its inhibition of the growth of metastatic brain tumors.

3.
Cell Transplant ; 16(6): 629-37, 2007.
Artículo en Inglés | MEDLINE | ID: mdl-17912954

RESUMEN

Glycogen storage disease type I (GSD-I) is a group of autosomal recessive disorders with an incidence of 1 in 100,000. The two major subtypes are GSD-Ia, caused by a deficiency of glucose-6-phosphatase (G6Pase), and GSD-Ib, caused by a deficiency of glucose-6-phosphate transporter (G6PT). We report that a substantial improvement was achieved following several infusions of hepatocytes in a patient with GSD-Ib. Hepatocytes were isolated from the unused cadaveric whole livers of two donors. At the first transplantation, approximately 2 x 10(9) cells (2% of the estimated recipient's total hepatocytes) were infused. Seven days later 1 x 10(9) (1% of liver mass) cryopreserved hepatocytes from the same donor were infused, and an additional 3 x 10(9) (3% of liver mass) cells from the second donor were infused 1 month after the second transplantation. After the hepatocyte transplantation, the patient showed no hypoglycemic symptoms despite the discontinuation of cornstarch meals. Liver biopsies on posttransplantation days 20 and 250 showed a normal level of glucose-6-phosphatase activity in presolubilization assay that was very low before transplantation. This was the first and successful clinical hepatocyte transplantation in Korea. In this study, hepatocyte transplantation allowed a normal diet in a patient with GSD-Ib, with substantial improvement in their quality of life. Hepatocyte transplantation might be an alternative to liver transplantation and dietary therapy in GSD-Ib.


Asunto(s)
Glucosa-6-Fosfatasa/metabolismo , Glucosa-6-Fosfato/metabolismo , Enfermedad del Almacenamiento de Glucógeno Tipo I/metabolismo , Enfermedad del Almacenamiento de Glucógeno Tipo I/terapia , Hepatocitos/trasplante , Adolescente , Cadáver , Estudios de Seguimiento , Glucosa-6-Fosfato/deficiencia , Enfermedad del Almacenamiento de Glucógeno Tipo I/patología , Hepatocitos/enzimología , Humanos , Inmunosupresores/uso terapéutico , Corea (Geográfico) , Hígado/citología , Hígado/inmunología , Masculino , Calidad de Vida , Inmunología del Trasplante/efectos de los fármacos , Trasplantes , Resultado del Tratamiento
4.
Liver Transpl ; 11(3): 331-5, 2005 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-15719385

RESUMEN

During liver transplantation for hepatocellular carcinoma (HCC) patients, HCC could theoretically be introduced into the systemic circulation when salvaged blood is used with an autotransfusion device. Several reports have shown that some types of leukocyte depletion filters (LDFs) could completely reduce the risk for reintroducing some types of tumor cells. In this study, we tested the ability of the LDF (RCEZ1T, Pall Biomedical Co, NY, USA) to reduce the risk for reintroducing HCC cells in vitro by using a very sensitive detection method. We divided the test group into 6 groups: group I was 10 cells, group II was 20 cells, group III was 2 x 10(3) cells, group IV was 2 x 10(5) cells, group V was 2 x 10(6) cells, and group VI was 2 x 10(7) cells. The counted cells in 200 mL saline were passed through the RCEZ1T using the force of gravity. To identify the presence of cells, the pellet was resuspended, and polymerase chain reaction (PCR) was performed. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a housekeeping gene, was used as a primer. In groups I and II, the HCC cells were completely filtered in all experiments. However, in groups III, IV, and V, the HCC cells were not completely filtered in a few of the repeated experiments, with the unfiltered rate of tumor cells being between 8% and 20%. In group VI, the HCC cells were not completely filtered in all the repeated experiments. In conclusion, the RCEZ1T filter markedly reduced the risk for reintroduction of HCC cells. However, at high HCC cell load the filter cannot completely remove all the tumor cells. Further studies are required to assess the impact in clinical settings.


Asunto(s)
Carcinoma Hepatocelular/cirugía , Filtración/métodos , Procedimientos de Reducción del Leucocitos , Neoplasias Hepáticas/cirugía , Trasplante de Hígado/métodos , Carcinoma Hepatocelular/diagnóstico , Línea Celular Tumoral , Gliceraldehído-3-Fosfato Deshidrogenasas/análisis , Gliceraldehído-3-Fosfato Deshidrogenasas/genética , Humanos , Neoplasias Hepáticas/diagnóstico , Reacción en Cadena de la Polimerasa , Recurrencia , Sensibilidad y Especificidad
5.
Eur J Biochem ; 271(17): 3470-80, 2004 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-15317582

RESUMEN

We show that epigallocatechin-3 gallate (EGCG), a major component of green tea, stimulates phospholipase D (PLD) activity in U87 human astroglioma cells. EGCG-induced PLD activation was abolished by the phospholipase C (PLC) inhibitor and a lipase inactive PLC-gamma1 mutant, which is dependent on intracellular or extracellular Ca(2+), with the possible involvement of Ca(2+)/calmodulin-dependent protein kinase II (CaM kinase II). EGCG induced translocation of PLC-gamma1 from the cytosol to the membrane and PLC-gamma1 interaction with PLD1. EGCG regulates the activity of PLD by modulating the redox state of the cells, and antioxidants reverse this effect. Moreover, EGCG-induced PLD activation was reduced by PKC inhibitors or down-regulation of PKC. Taken together, these results show that, in human astroglioma cells, EGCG regulates PLD activity via a signaling pathway involving changes in the redox state that stimulates a PLC-gamma1 [Ins(1,4,5)P(3)-Ca(2+)]-CaM kinase II-PLD pathway and a PLC-gamma1 (diacylglycerol)-PKC-PLD pathway.


Asunto(s)
Antineoplásicos/metabolismo , Proteínas Quinasas Dependientes de Calcio-Calmodulina/metabolismo , Catequina/análogos & derivados , Catequina/metabolismo , Fosfolipasa D/metabolismo , Proteína Quinasa C/metabolismo , Fosfolipasas de Tipo C/metabolismo , Antioxidantes/metabolismo , Astrocitoma/metabolismo , Neoplasias Encefálicas/metabolismo , Calcio/metabolismo , Proteína Quinasa Tipo 2 Dependiente de Calcio Calmodulina , Línea Celular Tumoral , Activación Enzimática , Inhibidores Enzimáticos/metabolismo , Humanos , Oxidación-Reducción , Fosfolipasa C gamma , Especies Reactivas de Oxígeno/metabolismo , Té/química
6.
J Biol Chem ; 279(37): 38125-33, 2004 Sep 10.
Artículo en Inglés | MEDLINE | ID: mdl-15210717

RESUMEN

Little is known about the effect of epigallocatechin-3 gallate (EGCG), a major constituent of green tea, on the expression of cyclooxygenase (COX)-2. Here, we studied the role of phospholipase D (PLD) isozymes in EGCG-induced COX-2 expression. Stimulation of human astrocytoma cells (U87) with EGCG induced formation of phosphatidylbutanol, a specific product of PLD activity, and synthesis of COX-2 protein and its product, prostaglandin E(2) (PGE(2)). Pretreatment of cells with 1-butanol, but not 3-butanol, suppressed EGCG-induced COX-2 expression and PGE synthesis. Furthermore, evidence that PLD was involved in EGCG-induced COX-2 expression was provided by the observations that COX-2 expression was stimulated by overexpression of PLD1 or PLD2 isozymes and treatment with phosphatidic acid (PA), and that prevention of PA dephosphorylation by 1-propranolol significantly potentiated COX-2 expression induced by EGCG. EGCG induced activation of p38 mitogen-activated protein kinase (p38 MAPK), and specific inhibition of p38 MAPK dramatically abolished EGCG-induced PLD activation, COX-2 expression, and PGE(2) formation. Moreover, protein kinase C (PKC) inhibition suppressed EGCG-induced p38 MAPK activation, COX-2 expression, and PGE(2) accumulation. The same pathways as those obtained (2)in the astrocytoma cells were active in primary rat astrocytes, suggesting the relevance of the findings. Collectively, our results demonstrate for the first time that PLD isozymes mediate EGCG-induced COX-2 expression through PKC and p38 in immortalized astroglial line and normal astrocyte cells.


Asunto(s)
Astrocitos/metabolismo , Catequina/análogos & derivados , Catequina/farmacología , Isoenzimas/biosíntesis , Fosfolipasa D/farmacología , Prostaglandina-Endoperóxido Sintasas/biosíntesis , 1-Butanol/farmacología , Animales , Astrocitoma/metabolismo , Western Blotting , Carbazoles/farmacología , Línea Celular Tumoral , Células Cultivadas , Ciclooxigenasa 2 , Dinoprostona/metabolismo , Relación Dosis-Respuesta a Droga , Activación Enzimática , Inhibidores Enzimáticos/farmacología , Humanos , Indoles/farmacología , Proteínas de la Membrana , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Ácidos Fosfatidicos/metabolismo , Ácidos Fosfatidicos/farmacología , Fosfolipasa D/química , Fosfolipasa D/metabolismo , Fosforilación , Isoformas de Proteínas , Proteína Quinasa C/metabolismo , Ratas , Ratas Sprague-Dawley , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Factores de Tiempo , Transfección , Proteínas Quinasas p38 Activadas por Mitógenos
7.
Mol Cell Biol ; 23(9): 3103-15, 2003 May.
Artículo en Inglés | MEDLINE | ID: mdl-12697812

RESUMEN

Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src synergistically enhances cellular proliferation compared with expression of either molecule. While PLD activity as a lipid-hydrolyzing enzyme is not affected by c-Src, wild-type PLDs but not catalytically inactive PLD mutants significantly increase c-Src kinase activity, up-regulating c-Src-mediated paxillin phosphorylation and extracellular signal-regulated kinase activity. These results demonstrate the critical role of PLD catalytic activity in the stimulation of Src signaling. In conclusion, we provide the first evidence that c-Src acts as a kinase of PLD and PLD acts as an activator of c-Src. This transmodulation between c-Src and PLD may contribute to the promotion of cellular proliferation via amplification of mitogenic signaling pathways.


Asunto(s)
Fosfolipasa D/metabolismo , Proteínas Tirosina Quinasas/metabolismo , Animales , Proteína Tirosina Quinasa CSK , Carcinoma de Células Escamosas/metabolismo , Dominio Catalítico , División Celular/fisiología , Células Cultivadas , Proteínas del Citoesqueleto/metabolismo , Activación Enzimática , Factor de Crecimiento Epidérmico/farmacología , Femenino , Humanos , Ratones , Ratones Endogámicos BALB C , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Mutación , Paxillin , Fosfolipasa D/efectos de los fármacos , Fosfolipasa D/genética , Fosfoproteínas/metabolismo , Fosforilación/efectos de los fármacos , Estructura Terciaria de Proteína , Proteínas Tirosina Quinasas/genética , Ratas , Transducción de Señal , Tirosina/metabolismo , Familia-src Quinasas
8.
J Biol Chem ; 277(14): 12334-42, 2002 Apr 05.
Artículo en Inglés | MEDLINE | ID: mdl-11821392

RESUMEN

alpha-Synuclein has been implicated in the pathogenesis of many neurodegenerative diseases, including Parkinson's disease and Alzheimer's disease. Although the function of alpha-synuclein remains largely unknown, recent studies have demonstrated that this protein can interact with phospholipids. To address the role of alpha-synuclein in neurodegenerative disease, we have investigated whether it binds phospholipase D (PLD) and affects PLD activity in human embryonic kidney (HEK)-293 cells overexpressing wild type alpha-synuclein or the mutant forms of alpha-synuclein (A53T, A30P) associated with Parkinson's disease. Tyrosine phosphorylation of alpha-synuclein appears to play a modulatory role in the inhibition of PLD, because mutation of Tyr(125) to Phe slightly increases inhibitory effect of alpha-synuclein on PLD activity. Treatment with pervanadate or phorbol myristate acetate inhibits PLD more in HEK 293 cells overexpressing alpha-synuclein than in control cells. Binding of alpha-synuclein to PLD requires phox and pleckstrin homology domain of PLD and the amphipathic repeat region and non-Abeta component of alpha-synuclein. Although biologically important, co-transfection studies indicate that the interaction of alpha-synuclein with PLD does not influence the tendency of alpha-synuclein to form pathological inclusions. These results suggest that the association of alpha-synuclein with PLD, and modulation of PLD activity, is biologically important, but PLD does not appear to play an essential role in the pathophysiology of alpha-synuclein.


Asunto(s)
Proteínas del Tejido Nervioso/química , Proteínas del Tejido Nervioso/metabolismo , Fosfolipasa D/química , Vanadatos/farmacología , Animales , Proteínas Sanguíneas/química , Western Blotting , Encéfalo/metabolismo , Línea Celular , Citoplasma/metabolismo , ADN Complementario/metabolismo , Activación Enzimática , Inhibidores Enzimáticos/farmacología , Eosinófilos/metabolismo , Glutatión Transferasa/metabolismo , Humanos , Microscopía Fluorescente , Mutación , Fosfolipasa D/metabolismo , Fosfoproteínas/química , Fosforilación , Pruebas de Precipitina , Unión Proteica , Isoformas de Proteínas , Estructura Terciaria de Proteína , Ratas , Proteínas Recombinantes de Fusión/metabolismo , Sinucleínas , Acetato de Tetradecanoilforbol/farmacología , Factores de Tiempo , Transfección , Tirosina/metabolismo , alfa-Sinucleína
SELECCIÓN DE REFERENCIAS
DETALLE DE LA BÚSQUEDA