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Alterations of Cyclin dependent kinase 5 expression and phosphorylation in Amyloid precursor protein (APP)‐transfected PC12 cells
Author(s) -
Czapski Grzegorz A.,
Gąssowska Magdalena,
Songin Martyna,
Radecka Urszula D.,
Strosznajder Joanna B.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.03.058
Subject(s) - cyclin dependent kinase 5 , phosphorylation , gsk 3 , hyperphosphorylation , transfection , kinase , microbiology and biotechnology , cyclin dependent kinase , gsk3b , chemistry , amyloid precursor protein , glycogen synthase , protein kinase a , cyclin dependent kinase 2 , biology , biochemistry , cell cycle , cell , alzheimer's disease , gene , medicine , disease
The aim of the present study was to analyse the alterations of Cyclin dependent kinase 5 (Cdk5) expression and phosphorylation in PC12 cells overexpressing Amyloid precursor protein (APP). Our results demonstrated enhanced cell death and increased levels of mRNA for the Cdk5 gene in APP‐transfected cells. Significantly decreased phosphorylation of Cdk5 at Tyr15 was observed in APPsw cells, which is responsible for a reduction in Cdk5 activity. Cdk5‐dependent phosphorylation of Glycogen synthase kinase‐3β (Gsk‐3β) at Ser9 was also decreased, which can lead to the increase of Gsk‐3β activity and hyperphosphorylation of MAP tau. Our results demonstrate for the first time, a deregulation of Cdk5 phosphorylation in APP‐transfected cells.