Integrin-linked kinase is involved in lactoferrin-induced anchorage-independent cell growth and survival in PC12 cells.
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.[1]References
- Integrin-linked kinase is involved in lactoferrin-induced anchorage-independent cell growth and survival in PC12 cells. Ishii, T., Uto, T., Mori, K., Fujikawa, R. Life Sci. (2009) [Pubmed]
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