Registro completo |
Provedor de dados: |
BJMBR
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País: |
Brazil
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Título: |
Changes in cell shape, cytoskeletal proteins and adhesion sites of cultured cells after extracellular Ca2+ chelation
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Autores: |
Mermelstein,C.S.
Rebello,M.I.L.
Amaral,L.M.
Costa,M.L.
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Data: |
2003-08-01
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Ano: |
2003
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Palavras-chave: |
Cytoskeleton
Extracellular Ca2+
Cell shape
Microfilaments
Microtubules
Integrin
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Resumo: |
Although much is known about the molecules involved in extracellular Ca2+ regulation, the relationship of the ion with overall cell morphology is not understood. The objective of the present study was to determine the effect of the Ca2+ chelator EGTA on the major cytoskeleton components, at integrin-containing adhesion sites, and their consequences on cell shape. Control mouse cell line C2C12 has a well-spread morphology with long stress fibers running in many different directions, as detected by fluorescence microscopy using rhodamine-phalloidin. In contrast, cells treated with EGTA (1.75 mM in culture medium) for 24 h became bipolar and showed less stress fibers running in one major direction. The adhesion plaque protein alpha5-integrin was detected by immunofluorescence microscopy at fibrillar adhesion sites in both control and treated cells, whereas a dense labeling was seen only inside treated cells. Microtubules shifted from a radial arrangement in control cells to a longitudinal distribution in EGTA-treated cells, as analyzed by immunofluorescence microscopy. Desmin intermediate filaments were detected by immunofluorescence microscopy in a fragmented network dispersed within the entire cytoplasm in EGTA-treated cells, whereas a dense network was seen in the whole cytoplasm of control cells. The present results suggest that the role of extracellular Ca2+ in the regulation of C2C12 cell shape can be mediated by actin-containing stress fibers and microtubules and by intermediate filament reorganization, which may involve integrin adhesion sites.
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Tipo: |
Info:eu-repo/semantics/article
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Idioma: |
Inglês
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Identificador: |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000800018
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Editor: |
Associação Brasileira de Divulgação Científica
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Relação: |
10.1590/S0100-879X2003000800018
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Formato: |
text/html
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Fonte: |
Brazilian Journal of Medical and Biological Research v.36 n.8 2003
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Direitos: |
info:eu-repo/semantics/openAccess
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