| Registro completo |
| Provedor de dados: |
OAK
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| País: |
Japan
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| Título: |
Integrin-linked kinase is involved in lactoferrin-induced anchorage-independent cell growth and survival in PC12 cells
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| Autores: |
Ishii, Toshiaki
Uto, Tomoka
Mori, Kaori
Fujikawa, Ryu
石井, 利明
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| Data: |
2009-04-10
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| Ano: |
2009
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| Palavras-chave: |
Bovine lactoferrin
PC12 cell
Integrin-linked kinase
Integrin
P38 MAPK
Cell suspension
Cell adhesion
Cell growth
Cell viability
Dominant-negative mutant
Anchorage-independent growth
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| Resumo: |
Aims: Bovine lactoferrin (bLf) causes anchorage-independent cell growth in PC12 cells. The present study investigated the mechanisms involved in bLf-induced anchorage-independent cell growth and survival in PC12 cells. Main methods: The number of adherent cells and suspended cells was estimated separately by using a methyl thiazol tetrazolium (MTT) assay, and the sum of both optical density (O.D.) (570 nm) values was used as a measure of the total number of cells. Key findings: Integrin-linked kinase (ILK) plays an important role in integrin and growth factor signaling pathways. Stable transfection of PC12 cells with a dominant negative kinase-deficient mutant of ILK (DN-ILK) inhibited bLf-induced anchorage-independent cell growth. The ILK activity in the parental cells was transiently activated after addition of bLf, whereas bLf-induced activation of ILK was blocked in DN-ILK-transfected cells. bLf also activated p38 mitogen-activated protein kinase (MAPK); however, the p38 MAPK activation was inhibited by stable DN-ILK transfection. Moreover, cell viability in the suspended cells by bLf strongly decreased after treatment with SB203580, an inhibitor of p38 MAPK. Significance: These results suggest that ILK is involved in bLf-induced anchorage-independent cell growth and viability via activation of p38 MAPK.
http://www.sciencedirect.com/science/journal/00243205
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| Idioma: |
Inglês
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| Identificador: |
http://ir.obihiro.ac.jp/dspace/handle/10322/2675
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| Editor: |
Elsevier
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| Formato: |
application/pdf
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| Direitos: |
Elsevier
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