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Inactivation of integrin-linked kinase induces aberrant tau phosphorylation via sustained activation of glycogen synthase kinase 3 beta in N1E-115 neuroblastoma cells OAK
Ishii, Toshiaki; Furuoka, Hidefumi; Muroi, Yoshikage; Nishimura, Masakazu; 石井, 利明; 古岡, 秀文; 室井, 喜景.
Integrin-linked kinase (ILK) is a focal adhesion serine/ threonine protein kinase with an important role in integrin and growth factor signaling pathways. Recently, we demonstrated that ILK is expressed in N1E-115 neuroblastoma cells and controls integrin-dependent neurite outgrowth in serum-starved cells grown on laminin (Ishii, T., Satoh, E., and Nishimura, M. ( 2001) J. Biol. Chem. 276, 42994 - 43003). Here we report that ILK controls tau phosphorylation via regulation of glycogen synthase kinase-3beta (GSK-3beta) activity in N1E-115 cells. Stable transfection of a kinase-deficient ILK mutant (DN-ILK) resulted in aberrant tau phosphorylation in N1E-115 cells at sites recognized by the Tau-1 antibody that are identical to some of the phosphorylation...
Palavras-chave: ALZHEIMERS-DISEASE NEURITE OUTGROWTH PROTEIN; NEURONS HYPERPHOSPHORYLATION KINASE-3-BETA ACCUMULATION BINDING ROLES.
Ano: 2003 URL: http://ir.obihiro.ac.jp/dspace/handle/10322/747
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