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1.
ACS Appl Mater Interfaces ; 16(6): 7860-7874, 2024 Feb 14.
Artículo en Inglés | MEDLINE | ID: mdl-38311837

RESUMEN

As the core of a solar collector, a solar selective absorbing coating has become the key material for efficient utilization and development of solar energy. In order to overcome the core scientific problem of poor high-temperature stability of optical properties caused by atomic diffusion between layers in the high-temperature environment of traditional multilayer solar absorption coatings, the multiscale lotus bionic porous structure was constructed by using a TiC/TiN-Ni/Mo material system with excellent intrinsic absorption performance. The melt foam method and laser cladding technology were combined to deposit the multiscale bionic porous structure solar selective absorption coating in situ by a laser-induced melt foaming strategy. It was found that the bubbles in the molten pool were affected by Marangoni force, gravity, buoyancy, and surface tension. The unescaped bubbles formed pores near the surface of the coating and showed a bimodal distribution. For the multiscale addition of 1.8 and 0.4 µm pore-forming agents with a mass fraction of 15 wt %, the multiscale pores enhance the scattering and secondary absorption of light and reduce the amplitude of electromagnetic wave to electron vibration; at the same time, the small-size conductor effect formed by the hole increases the surface electron concentration, strengthens the absorption of light, and enhances the magnetic field strength at the hole, and the structural absorbing effect is significant. The coating absorptivity α reaches 85%, and the temperature stability is excellent. Compared with the substrate, the coating has a smaller corrosion current density, larger polarization resistance, and strong corrosion resistance. The research shows that the laser-induced multiscale bionic porous structure coating obtains the intrinsic absorption-structural absorption composite absorption mechanism and realizes the integration of flexible design and efficient manufacturing of high-temperature solar absorption coatings.

2.
Antioxid Redox Signal ; 4(3): 509-15, 2002 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-12215219

RESUMEN

Syk has been demonstrated to play a crucial role in oxidative stress signaling in B cells. In this study, we have investigated the role of Syk in p38 activation and the regulation of cell-cycle progression upon oxidative stress. In B cells, p38 is activated by hydrogen peroxide (H(2)O(2)) stimulation. Syk is required for p38 activation following stimulation with 10-100 microM H(2)O(2), but not with 1 mM H(2)O(2). H(2)O(2)-induced p38 activation is abrogated in phospholipase C-gamma2 (PLC-gamma2)-deficient as well as Syk-deficient cells, suggesting that Syk activates p38 through PLC-gamma2 upon H(2)O(2) stimulation. Although stimulation with 20-100 microM H(2)O(2) induces cellular apoptosis in B cells, pretreatment with SB203580, a p38-specific inhibitor, has no effect on H(2)O(2)-induced apoptosis. Flow cytometric analysis reveals that B cells exposed to 10-20 microM H(2)O(2) exhibit cell-cycle profile of G2/M arrest, and pretreatment with SB203580 inhibits only a little H(2)O(2)-induced G2/M arrest. On the other hand, Syk-deficient cells show no induction of G2/M arrest following H(2)O(2) stimulation. These findings indicate that Syk plays a role in the regulation of cell-cycle progression in G2/M phase via p38-dependent and -independent pathways after oxidative stress.


Asunto(s)
Linfocitos B/metabolismo , Ciclo Celular/fisiología , Precursores Enzimáticos/metabolismo , Proteínas Quinasas Activadas por Mitógenos/metabolismo , Estrés Oxidativo , Proteínas Tirosina Quinasas/metabolismo , Animales , Apoptosis/fisiología , Linfocitos B/efectos de los fármacos , Linfocitos B/enzimología , Supervivencia Celular , Pollos , Fragmentación del ADN , Activación Enzimática , Inhibidores Enzimáticos/farmacología , Peróxido de Hidrógeno/farmacología , Imidazoles/farmacología , Péptidos y Proteínas de Señalización Intracelular , Isoenzimas/metabolismo , Proteínas Quinasas JNK Activadas por Mitógenos , Oxidantes/farmacología , Fosfolipasa C gamma , Piridinas/farmacología , Quinasa Syk , Fosfolipasas de Tipo C/metabolismo , Proteínas Quinasas p38 Activadas por Mitógenos
3.
Br J Pharmacol ; 137(6): 749-55, 2002 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-12411404

RESUMEN

1. 2-amino-4, 4alpha-dihydro-4alpha, 7-dimethyl-3H-phenoxazine-3-one (Phx) has been demonstrated to be an actinomycin D-like phenoxazine, and to display anti-tumour activity. 2. In this study, we report on the effect of Phx on B cell antigen receptor (BCR) and receptor-mediated signalling in DT40 B cells. 3. Treatment of B cells with Phx for 12 h inhibited BCR-stimulated tyrosine phosphorylation of cellular proteins. 4. B cells exposed to Phx exhibited down-regulation of surface IgM which is part of BCR. In contracts with actinomycin D, Phx rapidly reduced the expression of IgM without decreasing the expression of other signalling molecules. 5. Analysis with confocal microscopy demonstrated that Phx treatment reduced IgM expression both at the cell surface and inside the cell. 6. Treatment of B cells with Phx resulted in the reduction of IgM secretion. Since MG-132, a proteasomal inhibitor, restored IgM contents to the control levels, Phx has the specific effect of accelerating IgM degradation. 7. These results suggest that Phx down-regulates the expression of IgM and inhibits BCR-mediated signalling and IgM secretion. Phx may be useful as an immunosuppressive agent for therapeutic purposes.


Asunto(s)
Inmunoglobulina M/efectos de los fármacos , Oxazinas/farmacología , Animales , División Celular/efectos de los fármacos , Membrana Celular/efectos de los fármacos , Membrana Celular/metabolismo , Inhibidores de Cisteína Proteinasa/farmacología , Relación Dosis-Respuesta a Droga , Inmunoglobulina M/biosíntesis , Leupeptinas/farmacología , Receptores de Antígenos de Linfocitos B/fisiología , Transducción de Señal/efectos de los fármacos , Factores de Tiempo , Células Tumorales Cultivadas
4.
Artículo en Inglés | MEDLINE | ID: mdl-15328769

RESUMEN

Abnormal scars result in distressing symptoms and disfiguring blemishes; an understanding of the molecular events that cause such scars, particularly keloids, would make possible the optimisation of both wound healing and treatment. Extracellular signal-regulated protein kinase (ERK) has a crucial role in distinct signalling pathways in different cells, but to date we know of no study on its signalling events in keloid fibroblasts. The purpose of this study was to characterise the expression of tyrosine phosphorylation kinases, particularly that of ERK, in keloids at the protein level by immunoblotting analysis. Studies on phosphorylation were made on cell lysates of three cultures of five different keloid fibroblasts (n = 5), their relatively 'normal' fibroblasts in adjacent skin (rNHDF, n = 5), and normal human dermal fibroblasts (n = 1, standard control). The result showed that ERK signalling molecular protein was more highly phosphorylated in keloid fibroblast culture than in the other two cultures.


Asunto(s)
Quinasas MAP Reguladas por Señal Extracelular/metabolismo , Fibroblastos/metabolismo , Queloide/metabolismo , Factor de Crecimiento Derivado de Plaquetas/farmacología , Adolescente , Adulto , Becaplermina , Western Blotting , Células Cultivadas , Femenino , Humanos , Queloide/patología , Masculino , Persona de Mediana Edad , Fosforilación , Proteínas Proto-Oncogénicas c-sis
5.
Bing Du Xue Bao ; 28(6): 689-98, 2012 Nov.
Artículo en Zh | MEDLINE | ID: mdl-23367571

RESUMEN

Porcine reproductive and respiratory syndrome virus (PRRSV) continues to be a threat, causing economically significant impacts on the swine industry worldwide. Unfortunately, the traditional control strategies and conventional vaccines fail to provide sustainable disease control, in particular against genetically diverse strains, as they suffer from both antigenic heterogeneity and various immune evasion strategies of PRRSV. In this paper, latest research progress in immunology and immune evasion of PRRSVis summarized to provide a referenc for PRSSV prevention and control as well as the design of new vaccines.


Asunto(s)
Evasión Inmune , Síndrome Respiratorio y de la Reproducción Porcina/inmunología , Virus del Síndrome Respiratorio y Reproductivo Porcino/inmunología , Animales , Síndrome Respiratorio y de la Reproducción Porcina/virología , Virus del Síndrome Respiratorio y Reproductivo Porcino/genética , Porcinos , Proteínas Virales/genética , Proteínas Virales/inmunología
6.
Appl Biochem Biotechnol ; 163(7): 845-50, 2011 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-20844984

RESUMEN

During the last 10 years, with the development of loop-mediated isothermal amplification (LAMP) method, it has been widely applied in nucleic acid analysis because of its simplicity, rapidity, high efficiency, and outstanding specificity. This method employs a DNA polymerase and a set of four specially designed primers that recognize a total of six distinct sequences on the target DNA. Expensive equipment are not necessary to acquire a high level of precision, and there are fewer preparation steps compared to conventional PCR and real-time PCR assays. This paper briefly summarized the applications of LAMP method in pathogenic microorganisms, genetically modified ingredients, tumor detection, and embryo sex identification.


Asunto(s)
Cartilla de ADN/genética , ADN Polimerasa Dirigida por ADN/metabolismo , ADN/análisis , Técnicas de Amplificación de Ácido Nucleico , Animales , ADN/genética , Cartilla de ADN/química , ADN Polimerasa Dirigida por ADN/genética , Diagnóstico Precoz , Femenino , Feto , Alimentos Modificados Genéticamente , Humanos , Tipificación Molecular/métodos , Neoplasias/diagnóstico , Técnicas de Amplificación de Ácido Nucleico/métodos , Sensibilidad y Especificidad , Análisis para Determinación del Sexo
7.
J Biol Chem ; 280(43): 36318-25, 2005 Oct 28.
Artículo en Inglés | MEDLINE | ID: mdl-16103110

RESUMEN

Sphingosine kinase (SPHK) 1 is implicated in the regulation of cell proliferation and anti-apoptotic processes by catalyzing the formation of an important bioactive messenger, sphingosine 1-phosphate. Unlike the proliferative action of SPHK1, another isozyme, SPHK2, has been shown to possess anti-proliferative or pro-apoptotic action. Molecular mechanisms of SPHK2 action, however, are largely unknown. The present studies were undertaken to characterize the N-terminal-extended form of SPHK2 (SPHK2-L) by comparing it with the originally reported form, SPHK2-S. Real-time quantitative PCR analysis revealed that SPHK2-L mRNA is the major form in several human cell lines and tissues. From sequence analyses it was concluded that SPHK2-L is a species-specific isoform that is expressed in human but not in mouse. At the protein level it has been demonstrated by immunoprecipitation studies that SPHK2-L is the major isoform in human hepatoma HepG2 cells. SPHK2-L, when expressed in human embryonic kidney (HEK) 293 cells, did not show any inhibition of DNA synthesis in the presence of serum, whereas it showed marked inhibition in the absence of serum. Moreover, serum deprivation resulted in the translocation of SPHK2-L into the nuclei. In addition, serum deprivation induced SPHK2-L expression in HEK293 cells. Furthermore, suppression of SPHK2 by small interfering RNA treatment prevented serum deprivation- or drug-induced apoptosis in HEK293 cells. Taken together, these results indicate that a major form of SPHK2 splice variant, SPHK2-L, in human cells does not inhibit DNA synthesis under normal conditions and that SPHK2-L accumulation in the nucleus induced by serum deprivation may be involved in the cessation of cell proliferation or apoptosis depending on the cell type.


Asunto(s)
Apoptosis , Fosfotransferasas (Aceptor de Grupo Alcohol)/química , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Línea Celular , Núcleo Celular/metabolismo , Proliferación Celular , Clonación Molecular , ADN/metabolismo , ADN Complementario/metabolismo , Relación Dosis-Respuesta a Droga , Exones , Células HeLa , Humanos , Inmunohistoquímica , Ratones , Datos de Secuencia Molecular , Fosfotransferasas (Aceptor de Grupo Alcohol)/fisiología , Unión Proteica , Isoformas de Proteínas , Estructura Terciaria de Proteína , ARN Mensajero/metabolismo , ARN Interferente Pequeño/metabolismo , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Especificidad de la Especie , Distribución Tisular
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