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1.
Rev Infirm ; 71(284): 43-45, 2022 Oct.
Artigo em Francês | MEDLINE | ID: mdl-36509482

RESUMO

Teamwork, an essential component of quality care, is not always self-evident. Working together requires trust and shared objectives. As part of their preparation for the health service, aiming at learning to work in project mode, it is proposed to nursing students in their second year of training to use a pedagogical tool, the coat of arms, to work on group dynamics and the sharing of common values. The aim is to bring the team to give life to its collective identity, in the service of the implementation of its project, based on the individual characteristics of each of its members.


Assuntos
Coesão Social , Estudantes de Enfermagem , Humanos , Aprendizagem , Equipe de Assistência ao Paciente
2.
Exp Cell Res ; 285(1): 59-71, 2003 Apr 15.
Artigo em Inglês | MEDLINE | ID: mdl-12681287

RESUMO

In this work, we report that type IV collagen, mainly via alpha2beta1-integrin ligation, was able to induce cyclin expression and G1/S transition in a colic adenocarcinoma cell line (Caco-2) cultured without soluble growth factors or fetal bovine serum. This process involved Erk 1/2 activation and the production of reactive oxygen species (ROS) by a membrane-bound NADPH oxidase. Data presented here show that NADPH oxidase-dependent production of ROS increased following alpha2beta1-integrin ligation with type IV collagen or with a specific monoclonal antibody (Gi9 mAb). NADPH oxidase activation and, therefore, the production of ROS were shown to be involved in the increase of alpha2beta1-integrin plasma membrane expression, p38 MAPK phosphorylation, cyclin expression, and G1/S transition. We thus identified in this work a new integrin-signaling pathway in colon tumor cells involved in cell cycle regulation by the extracellular matrix.


Assuntos
Ciclo Celular/fisiologia , Colágeno Tipo IV/metabolismo , Integrina alfa2beta1/metabolismo , NADPH Oxidases/metabolismo , Espécies Reativas de Oxigênio/metabolismo , Transdução de Sinais/fisiologia , Adenocarcinoma/metabolismo , Animais , Células CACO-2 , Ciclina A/metabolismo , Ciclina D , Ciclina E/metabolismo , Ciclinas/metabolismo , Ativação Enzimática , Inibidores Enzimáticos/metabolismo , Citometria de Fluxo , Quinase 1 de Adesão Focal , Proteína-Tirosina Quinases de Adesão Focal , Humanos , Proteínas Quinases Ativadas por Mitógeno/metabolismo , Proteínas Tirosina Quinases/metabolismo
3.
Bull Cancer ; 89(2): 227-33, 2002 Feb.
Artigo em Francês | MEDLINE | ID: mdl-11888861

RESUMO

We have previously shown that microtubule disruption results in an increase in cell adhesion to ECM proteins. In this work we show that this enhanced cell attachment was completely abolished by specific inhibitors of tyrosine-kinases, PI3-K and PKCs. Microtubule depolymerisation was associated with an important increased in tyrosine phosphorylation of FAK and paxilline, as well as with subcellular localisation of PKCgamma, delta and epsilon. We also observed significant alterations in actin cytoskeleton leading to reduced cell spreading. Thus, microtubule depolymerisation appears to activate various intracellular kinases that lead to actin cytoskeletal changes and to an increase of integrin-dependent adhesion. Whether this enhanced attachment is due to intracellular events resulting in changes in integrin affinity or avidity remains to be determined.


Assuntos
Adesão Celular/efeitos dos fármacos , Microtúbulos/efeitos dos fármacos , Fosfatidilinositol 3-Quinases/fisiologia , Proteína Quinase C/fisiologia , Proteínas Tirosina Quinases/fisiologia , Vimblastina/análogos & derivados , Antineoplásicos/farmacologia , Adesão Celular/fisiologia , Quinase 2 de Adesão Focal , Células HT29/efeitos dos fármacos , Humanos , Microtúbulos/fisiologia , Nocodazol/farmacologia , Paclitaxel/farmacologia , Vimblastina/farmacologia , Vinorelbina
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