Cofilin
Mostrando 1-12 de 67 artigos, teses e dissertações.
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1. Detection of sputum cofilin-1 as indicator of malignancy
Cofilin-1 (CFL1), a small protein of 18 kDa, has been studied as a biomarker due to its involvement in tumor cell migration and invasion. Our aim was to evaluate CFL1 as an indicator of malignancy and aggressiveness in sputum samples. CFL1 was analyzed by ELISA immunoassay in the sputum of 73 lung cancer patients, 13 cancer-free patients, and 6 healthy volun
Braz J Med Biol Res. Publicado em: 28/05/2018
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2. Identificação e desenvolvimento de biomarcador para câncer de pulmão de não-pequenas células : o potencial prognóstico da cofilina-1
O câncer de pulmão é responsável por aproximadamente 13% do total de casos de neoplasias malignas e por cerca de 1.4 milhões de mortes por ano em todo mundo. Esta neoplasia apresenta-se sob dois principais subtipos: câncer de pulmão de pequenas células (CPPC) e câncer de pulmão de não-pequenas células (CPNPC). Cerca de 85% dos casos de câncer de
IBICT - Instituto Brasileiro de Informação em Ciência e Tecnologia. Publicado em: 2012
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3. Validação do uso da proteína cofilina como biomarcador preditivo do prognóstico de carcinoma de pulmão de não-pequenas células
Câncer de Pulmão de Não-pequenas células (CPNPC) é o maior problema de saúde pública atualmente no mundo.Encontramos em nossas pesquisas que os níveis de mRNA da CFL-1 (cofilina) podem ser usados como um biomarcador prognóstico em biópsias de tumores de CPNPC. Em nossos estudos, estabelecemos e optimizamos um método simples de imunohistoquímica s
Publicado em: 2010
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4. Coronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway
Coronins are conserved F-actin-binding proteins that are important for motility and actin dynamics. Unlike type I coronins, coronin 2A localizes to stress fibers and some focal adhesions, and is excluded from the leading edge. Depletion of coronin 2A in MTLn3 cells decreases cell motility and turnover of focal adhesions. Surprisingly, none of the pathway
Company of Biologists.
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5. Cofilin is a component of intranuclear and cytoplasmic actin rods induced in cultured cells.
Incubation of cultured cells under specific conditions induces a dramatic change in the actin organization: induction of intranuclear and/or cytoplasmic actin rods (actin paracrystal-like intracellular structures). We have found that cofilin, a 21-kDa actin-binding protein, is a component of these rods. Antibodies directed against cofilin labeled intranuclea
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6. Essential Role of Cofilin-1 in Regulating Thrombin-induced RelA/p65 Nuclear Translocation and Intercellular Adhesion Molecule 1 (ICAM-1) Expression in Endothelial Cells*
Activation of RhoA/Rho-associated kinase (ROCK) pathway and the associated changes in actin cytoskeleton induced by thrombin are crucial for activation of NF-κB and expression of its target gene ICAM-1 in endothelial cells. However, the events acting downstream of RhoA/ROCK to mediate these responses remain unclear. Here, we show a central role of cofilin-1
American Society for Biochemistry and Molecular Biology.
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7. Cofilin Phosphorylation by Protein Kinase Testicular Protein Kinase 1 and Its Role in Integrin-mediated Actin Reorganization and Focal Adhesion Formation
Testicular protein kinase 1 (TESK1) is a serine/threonine kinase with a structure composed of a kinase domain related to those of LIM-kinases and a unique C-terminal proline-rich domain. Like LIM-kinases, TESK1 phosphorylated cofilin specifically at Ser-3, both in vitro and in vivo. When expressed in HeLa cells, TESK1 stimulated the formation of actin s
The American Society for Cell Biology.
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8. Cofilin 1 Is Revealed as an Inhibitor of Glucocorticoid Receptor by Analysis of Hormone-Resistant Cells
Significant knowledge about glucocorticoid signaling has accumulated, yet many aspects remain unknown. We aimed to discover novel factors involved in glucocorticoid receptor regulation that do not necessarily require direct receptor interaction. We achieved this by using a functional genetic screen: a stable cell line which cannot survive hormone treatment w
American Society for Microbiology.
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9. The Three Mouse Actin-depolymerizing Factor/Cofilins Evolved to Fulfill Cell-Type–specific Requirements for Actin Dynamics
Actin-depolymerizing factor (ADF)/cofilins are essential regulators of actin filament turnover. Several ADF/cofilin isoforms are found in multicellular organisms, but their biological differences have remained unclear. Herein, we show that three ADF/cofilins exist in mouse and most likely in all other mammalian species. Northern blot and in situ hybridi
The American Society for Cell Biology.
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10. The ADF/cofilin family: actin-remodeling proteins
The ADF/cofilins are a family of actin-binding proteins that remodel the actin cytoskeleton, for example during cytokinesis, by severing actin filaments and also increasing the rate at which monomers leave the filament's pointed end. Plants and animals have multiple ADF/cofilin genes and other eukaryotes have a single ADF/cofilin gene.
BioMed Central.
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11. Actin-depolymerizing Factor and Cofilin-1 Play Overlapping Roles in Promoting Rapid F-Actin Depolymerization in Mammalian Nonmuscle CellsD⃞V⃞
Actin-depolymerizing factor (ADF)/cofilins are small actin-binding proteins found in all eukaryotes. In vitro, ADF/cofilins promote actin dynamics by depolymerizing and severing actin filaments. However, whether ADF/cofilins contribute to actin dynamics in cells by disassembling “old” actin filaments or by promoting actin filament assembly through their
The American Society for Cell Biology.
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12. Ca2+/Calmodulin-dependent Protein Kinase IV-mediated LIM Kinase Activation Is Critical for Calcium Signal-induced Neurite Outgrowth*
Actin cytoskeletal remodeling is essential for neurite outgrowth. LIM kinase 1 (LIMK1) regulates actin cytoskeletal remodeling by phosphorylating and inactivating cofilin, an actin filament-disassembling factor. In this study, we investigated the role of LIMK1 in calcium signal-induced neurite outgrowth. The calcium ionophore ionomycin induced LIMK1 activati
American Society for Biochemistry and Molecular Biology.