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A more recent version of this article appeared on June 9, 2000
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Papers In Press, published online ahead of print April 6, 2000
J. Biol. Chem, 10.1074/jbc.M000040200
Submitted on January 3, 2000
Revised on April 3, 2000
Accepted on April 6, 2000

Presenilin-1 Mutations Increase Levels of Ryanodine Receptors and Calcium Release in PC12 Cells and Cortical Neurons

Sic L Chan, Michael Mayne, Clark P Holden, Jonathan D Geiger, and Mark p Mattson

Laboratory of Neurosciences, National Institute on Aging, Baltimore, MD 21224

Corresponding Author: mattsonm{at}grc.nia.nih.gov

Many cases of early-onset inherited Alzheimer's disease (AD) are caused by mutations in the presenilin-1 (PS1) gene. PS1 mutations may perturb cellular Ca2+ homeostasis and thereby render neurons vulnerable to excitotoxicity and apoptosis. We now report that PC12 cells expressing PS1 mutations and primary hippocampal neurons from PS1 mutant knockin mice exhibit greatly increased levels of ryanodine receptors (RyR) and enhanced Ca2+ release following stimulation with caffeine. Double-labeling immunostaining and co-immunoprecipitation analyses indicate that PS1 and RyR are colocalized and interact. Caffeine treatment sensitizes neurons expressing mutant PS1 to apoptosis induced by amyloid b-peptide (Ab25-35), glutamate and iron, three insults relevant to the pathogenesis of AD. When taken together with recent evidence for alterations in RyR in brains of AD patients, our data suggest that PS1 mutations may promote neuronal degeneration in AD by increasing the number of ryanodine receptors available for calcium Ca2+ release.


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