Amyloid-beta causes memory impairment by disturbing the JAK2/STAT3 axis in hippocampal neurons

Mol Psychiatry. 2009 Feb;14(2):206-22. doi: 10.1038/mp.2008.105. Epub 2008 Sep 23.

Abstract

Elevation of intracranial soluble amyloid-beta (Abeta) levels has been implicated in the pathogenesis of Alzheimer's disease (AD). Intracellular events in neurons, which lead to memory loss in AD, however, remain elusive. Humanin (HN) is a short neuroprotective peptide abolishing Abeta neurotoxicity. Recently, we found that HN derivatives activate the Janus kinase 2 (JAK2)/signal transducer and activator of transcription 3 (STAT3) signaling axis. We here report that an HN derivative named colivelin completely restored cognitive function in an AD model (Tg2576) by activating the JAK2/STAT3 axis. In accordance, immunofluorescence staining using a specific antibody against phospho- (p-) STAT3 revealed that p-STAT3 levels in hippocampal neurons age-dependently decreased in both AD model mice and AD patients. Intracerebroventricular administration of Abeta1-42 downregulated p-STAT3 whereas passive immunization with anti-Abeta antibody conversely restored hippocampal p-STAT3 levels in Tg2576 mice, paralleling the decrease in the brain Abeta burden. Abeta1-42 consistently modulated p-STAT3 levels in primary neurons. Pharmacological inhibition of the JAK2/STAT3 axis not only induced significant loss of spatial working memory by downregulating an acetylcholine-producing enzyme choline acetyltransferase but also desensitized the M(1)-type muscarinic acetylcholine receptor. Thus, we propose a novel theory accounting for memory impairment related to AD: Abeta-dependent inactivation of the JAK2/STAT3 axis causes memory loss through cholinergic dysfunction. Our findings provide not only a novel pathological hallmark in AD but also a novel target in AD therapy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Age Factors
  • Alzheimer Disease / complications
  • Alzheimer Disease / pathology
  • Amyloid beta-Peptides / metabolism
  • Amyloid beta-Peptides / toxicity
  • Amyloid beta-Protein Precursor / genetics
  • Animals
  • Disease Models, Animal
  • Enzyme Inhibitors / pharmacology
  • Exploratory Behavior / drug effects
  • Exploratory Behavior / physiology
  • Gene Expression Regulation / drug effects
  • Gene Expression Regulation / physiology
  • Hippocampus / drug effects
  • Hippocampus / enzymology
  • Hippocampus / pathology*
  • Humans
  • Intracellular Signaling Peptides and Proteins / therapeutic use
  • Janus Kinase 2 / metabolism*
  • Maze Learning / drug effects
  • Maze Learning / physiology
  • Memory Disorders / chemically induced
  • Memory Disorders / drug therapy
  • Memory Disorders / metabolism*
  • Mice
  • Mice, Inbred ICR
  • Mice, Transgenic
  • Mutation
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Neurons / drug effects
  • Neurons / enzymology*
  • Peptide Fragments / metabolism
  • Presenilin-1 / genetics
  • Receptor, Muscarinic M1 / metabolism
  • STAT3 Transcription Factor / metabolism*

Substances

  • Amyloid beta-Peptides
  • Amyloid beta-Protein Precursor
  • Colivelin
  • Enzyme Inhibitors
  • Intracellular Signaling Peptides and Proteins
  • Nerve Tissue Proteins
  • Peptide Fragments
  • Presenilin-1
  • Receptor, Muscarinic M1
  • STAT3 Transcription Factor
  • Stat3 protein, mouse
  • amyloid beta-protein (1-40)
  • amyloid beta-protein (1-42)
  • Jak2 protein, mouse
  • Janus Kinase 2