Nuclear signaling: a common function of presenilin substrates?
J Mol Neurosci 17(2): 193-8
| Authors/Editors: |
Steiner H Haass C |
|---|---|
| Publication Date: | 2001 |
| Type of Publication: | Review |
Major progress has recently been made in the characterization of the secretases involved in endoproteolytic processing of the Alzheimer's disease (AD)-associated β-amyloid precursor protein, βAPP. βAPP is the precursor of the amyloid β-peptide, which is a major constituent of amyloid plaques in the brains of Alzheimer patients. It is now commonly believed that Aβ plays a pivotal role in the pathogenesis of AD, and that inhibiting the production of Aβ may help to treat or to prevent the disease. With β-secretase and the presenilins, two essential factors in the proteolytic generation of Aβ have now been identified. However, very little is still known about the biological function of the long-known βAPP. In this review we will discuss a novel putative function of βAPP in nuclear signaling, an activity, that βAPP may share with other presenilin substrates such as Notch.
