Induction of rat l-phosphoserine phosphatase by amyloid-β (1–42) is inhibited by interleukin-11

Abstract

Alzheimer's disease (AD) is characterized by the presence of beta-amyloid (Aβ) protein deposits in the brain and increased Aβ (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 Aβ (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 Aβ (1–42) activates l-phosphoserine phosphatase in neuronal cells which is inhibited by IL-11. Moreover, IL-11 inhibits Aβ (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.