β-amyloid induced hyperphosphorylation of tau in human neuroblastoma cells involves map kinase

β-amyloid induced hyperphosphorylation of tau in human neuroblastoma cells involves map kinase

Treatment of retinoic acid‐differentiated SH‐SY‐5Y human neuroblastoma cells with a sublethal concentration (22μM) β‐amyloid (βA) in the presence of 1.8mM extracellular calcium induced a marked increase in PHF‐1 immunoreactivity. The βA‐induced increase in PHF‐1 immunoreactivity was prevented by the...

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Veröffentlicht in:Neuroscience research communications 1998-01, Vol.22 (1), p.45-49
Hauptverfasser: Shea, Thomas B., Dergay, Amie N., Ekinci, Fatma J.
Format: Artikel
Sprache:eng
Schlagworte:
Alzheimer's disease
MAP kinase
PHF-1
phosphorylation
protein kinase C
tau
β-amyloid
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Zusammenfassung:Treatment of retinoic acid‐differentiated SH‐SY‐5Y human neuroblastoma cells with a sublethal concentration (22μM) β‐amyloid (βA) in the presence of 1.8mM extracellular calcium induced a marked increase in PHF‐1 immunoreactivity. The βA‐induced increase in PHF‐1 immunoreactivity was prevented by the MAP kinase kinase inhibitor PD 89059. These data indicate that βA‐induced tau hyperphosphorylation is mediated via activation of the MAP kinase pathway.
ISSN:0893-6609
1520-6769
DOI:10.1002/(SICI)1520-6769(199801/02)22:1<45::AID-NRC7>3.0.CO;2-S