@article{oai:obihiro.repo.nii.ac.jp:00000674,
 author = {Ishii, Toshiaki and Uto, Tomoka and Mori, Kaori and Fujikawa, Ryu},
 issue = {15-16},
 journal = {Life Sciences},
 month = {Apr},
 note = {application/pdf, 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.},
 pages = {530--536},
 title = {Integrin-linked kinase is involved in lactoferrin-induced anchorage-independent cell growth and survival in PC12 cells},
 volume = {84},
 year = {2009}
}