Induction of rat L-phosphoserine phosphatase by amyloid-beta (1-42) is inhibited by interleukin-11.

Abstract:

:Alzheimer's disease (AD) is characterized by the presence of beta-amyloid (Abeta) protein deposits in the brain and increased Abeta (1-42) peptide production is thought to be one of the early events in the pathogenesis of AD that leads to progressive neurodegenerative processes and dementia. Using cDNA subtraction and reverse transcription-polymerase chain reaction, we examined the Abeta (1-42) peptide-induced gene expression in rat neuroblastoma B104 cells. In addition we hypothesized that interleukin-11 (IL-11) supports neuronal survival. We found that Abeta (1-42) activates L-phosphoserine phosphatase in neuronal cells which is inhibited by IL-11. Moreover, IL-11 inhibits Abeta (1-42)-induced neurotoxicity in a dose-dependent manner. Our study suggests that L-phosphoserine phosphatase may play a role in altered neuronal function in AD via enhancing glutamate-induced neurotoxicity by D-serine and the IL-11 receptor system may act as a neuroprotective cytokine in human brain.

journal_name

Neurosci Lett

journal_title

Neuroscience letters

authors

Heese K,Nagai Y,Sawada T

doi

10.1016/s0304-3940(00)01197-6

keywords:

subject

Has Abstract

pub_date

2000-07-07 00:00:00

pages

37-40

issue

1

eissn

0304-3940

issn

1872-7972

pii

S0304-3940(00)01197-6

journal_volume

288

pub_type

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