Elevated amyloid beta protein(1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (Erk1/2)-dependent pathway in rat pheochromocytoma PC12 cells.

@article{Sato1997ElevatedAB,
  title={Elevated amyloid beta protein(1-40) level induces CREB phosphorylation at serine-133 via p44/42 MAP kinase (Erk1/2)-dependent pathway in rat pheochromocytoma PC12 cells.},
  author={Naoaki Sato and Kouzin Kamino and K Nakamura Tateishi and Tsuyoshi Satoh and Yasunobu Nishiwaki and Aoi Yoshiiwa and Tsuneharu Miki and Takeshi Ogihara},
  journal={Biochemical and biophysical research communications},
  year={1997},
  volume={232 3},
  pages={
          637-42
        }
}
The deposition of amyloid beta protein (A beta) in the cerebral cortex is the pathological characteristic of Alzheimer's disease (AD), and patients with AD suffer from progressive memory loss. Transgenic experiments have revealed that long-term memory is dependent on cyclic AMP-response element binding protein, CREB. CREB phosphorylation at serine-133 is essential for its transcriptional activity. Here we demonstrated that A beta(1-40), at a concentration more than 1 microM, induced CREB… CONTINUE READING

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