Presenilin regulates extracellular regulated kinase (Erk) activity by a protein kinase C alpha dependent mechanism.

@article{Dehvari2008PresenilinRE,
  title={Presenilin regulates extracellular regulated kinase (Erk) activity by a protein kinase C alpha dependent mechanism.},
  author={Nodi Dehvari and Ola Isacsson and Bengt Winblad and Angel Cedazo-M{\'i}nguez and Richard F. Cowburn},
  journal={Neuroscience letters},
  year={2008},
  volume={436 1},
  pages={77-80}
}
Presenilin (PS1 and PS2) mutations cause early-onset familial Alzheimer's disease (AD). In addition to affecting beta-amyloid precursor protein (APP) processing and Abeta generation, PSs regulate a number of signaling pathways. We previously showed that PSs regulate both phospholipase C (PLC) and protein kinase C (PKC) alpha and gamma activities. We also reported that PS double knockout mouse embryonic fibroblasts (MEFs) have reduced levels of PKCalpha and enhanced levels of PKCdelta. Here, we… CONTINUE READING