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1.
Int J Mol Sci ; 20(23)2019 Dec 02.
Artigo em Inglês | MEDLINE | ID: mdl-31810176

RESUMO

Microcellular foamed plastic has a cell size of approximately 0.1 to 10 microns inside a foamed polymer and a cell density in the range of 109 to 1015 cells/cm3. Typically, the formation of numerous uniform cells inside a polymer can be effectively used for various purposes, such as lightweight materials, insulation and sound absorbing materials. However, it has recently been reported that these dense cell structures, which are induced through microcellular foaming, can affect the light passing through the medium, which affects the haze and permeability and causes the diffused reflection of light to achieve high diffuse reflectivity. In this study, the effects of cell size, foaming ratio and refractive index on the optical performance were investigated by applying the microcellular foaming process to three types of amorphous polymer materials. Thus, this study experimentally confirmed that the advantages of porous materials can be implemented as optical properties by providing a high specific surface area as a small and uniform cell formed by inducing a high foaming ratio through a microcellular foaming process.


Assuntos
Tamanho Celular , Poliésteres/química , Polímeros/química , Dióxido de Carbono/química , Microscopia Eletrônica de Varredura , Plásticos/química , Porosidade , Refratometria , Temperatura
2.
J Electron Microsc (Tokyo) ; 61(5): 321-6, 2012.
Artigo em Inglês | MEDLINE | ID: mdl-22872282

RESUMO

Atomic force microscopy (AFM) combined with unroofing techniques enabled clear imaging of the intracellular cytoskeleton and the cytoplasmic surface of the cell membrane under aqueous condition. Many actin filaments were found to form a complex meshwork on the cytoplasmic surface of the membrane, as observed in freeze-etching electron microscopy. Characteristic periodic striations of about 5 nm formed by the assembly of G-actin were detected along actin filaments at higher magnification. Actin filaments aggregated and dispersed at several points, thereby dividing the cytoplasmic surface of the membrane into several large domains. Microtubules were also easily detected and were often tethered to the membrane surface by fine filaments. Furthermore, clathrin coats on the membrane were clearly visualized for the first time in water by AFM. Although the resolution of these images is lower than electron micrographs of freeze-etched samples processed similarly, the measurement capabilities of the AFM in a more biologically relevant conditions demonstrate that it is an important tool for imaging intracellular structures and cell surfaces in the native, aqueous state.


Assuntos
Citoplasma/ultraestrutura , Citoesqueleto/ultraestrutura , Microscopia de Força Atômica/métodos , Citoesqueleto de Actina , Actinas/ultraestrutura , Animais , Linhagem Celular , Membrana Celular/ultraestrutura , Técnica de Congelamento e Réplica/métodos , Processamento de Imagem Assistida por Computador/métodos , Microscopia Eletrônica/métodos , Ratos , Propriedades de Superfície , Água/metabolismo
3.
Immunol Lett ; 98(2): 303-10, 2005 May 15.
Artigo em Inglês | MEDLINE | ID: mdl-15860232

RESUMO

Heterogeneous nuclear ribonucleoprotein K protein (hnRNP K) has diverse molecular partners implicated in signal transduction pathways, and is tyrosine-phosphorylated in response to growth factors and oxidative stress. Among the structurally distinct domains of hnRNP K, an SH3-binding domain (SH3BD) has been known to promote the association of SH3-containing tyrosine kinases and protooncoprotein Vav, which are involved in B cell receptor (BCR) signalling. In this study, we analyzed proteins of Ramos B cell line that are altered upon BCR activation with anti-IgM antibody, revealing that a certain hnRNP K isoform is up-regulated in response to anti-IgM treatment. We also showed that hnRNP K is tyrosine-phosphorylated after BCR ligation. HnRNP K lacking the SH3BD is shown not to interact with phosphorylated Vav, and Ramos cells stably expressing this mutant protein are less susceptible to anti-IgM-induced apoptosis, indicating that hnRNP K is coupled to BCR-mediated signalling and its SH3BD is required for proper signal propagation. Our results provide the first evidence that hnRNP K is involved in BCR signalling pathway.


Assuntos
Anticorpos Anti-Idiotípicos/farmacologia , Linfócitos B/efeitos dos fármacos , Linfócitos B/metabolismo , Ribonucleoproteínas Nucleares Heterogêneas Grupo K/metabolismo , Fosfotirosina/metabolismo , Regulação para Cima/efeitos dos fármacos , Apoptose/imunologia , Linhagem Celular Tumoral , Eletroforese em Gel Bidimensional , Ribonucleoproteínas Nucleares Heterogêneas Grupo K/genética , Humanos , Imunoglobulina M/imunologia , Fosforilação/efeitos dos fármacos
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