Phosphorylation of beta-amyloid precursor protein (APP) cytoplasmic tail facilitates amyloidogenic processing during apoptosis.

Abstract:

:Secretion and progressive cerebral accumulation of beta-amyloid peptides (Abeta) derived by endoproteolytic ("amyloidogenic") processing of beta-amyloid precursor protein (APP) represent collectively an early and necessary event in the pathogenesis of Alzheimer's disease. We previously demonstrated that secretion of the neurotoxic species Abeta42 increases during staurosporine-induced apoptosis in undifferentiated PC12 cells, in an endocytosis-dependent manner. In the present study, we tested whether phosphorylation of the APP cytoplasmic-tail is contributory to this apoptosis-related increased Abeta-secretory response. We demonstrate that cytoplasmic-tail phosphorylation specifically at amino-acid residue T668 (APP-695 numbering) increases during staurosporine-induced apoptosis, in parallel with activation of the mitogen-activated, proline-directed serine/threonine protein kinase ERK1. We demonstrate additionally that specific ERK inhibition during staurosporine induction, with serum-free conditions, results in down-regulation of APP phosphorylation at T668, together with attenuation of the increased Abeta-secretory response. These results are consistent with APP cytoplasmic-tail phosphorylation at T668 during apoptosis as contributory to increased Abeta42 secretion originating from the endocytotic pathway, likely with cell-line restriction.

journal_name

Brain Res

journal_title

Brain research

authors

Sodhi CP,Perez RG,Gottardi-Littell NR

doi

10.1016/j.brainres.2008.01.031

subject

Has Abstract

pub_date

2008-03-10 00:00:00

pages

204-12

eissn

0006-8993

issn

1872-6240

pii

S0006-8993(08)00135-2

journal_volume

1198

pub_type

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