Abstract
Major progress has recently been made in the characterization of the secretases involved in endoproteolytic processing of the Alzheimer's disease (AD)-associated beta-amyloid precursor protein, betaAPP. betaAPP is the precursor of the amyloid beta-peptide, which is a major constituent of amyloid plaques in the brains of Alzheimer patients. It is now commonly believed that Abeta plays a pivotal role in the pathogenesis of AD, and that inhibiting the production of Abeta may help to treat or to prevent the disease. With beta-secretase and the presenilins, two essential factors in the proteolytic generation of Abeta have now been identified. However, very little is still known about the biological function of the long-known betaAPP. In this review we will discuss a novel putative function of betaAPP in nuclear signaling, an activity, that betaAPP may share with other presenilin substrates such as Notch.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Acetyltransferases / metabolism
-
Alzheimer Disease / metabolism*
-
Alzheimer Disease / physiopathology
-
Amyloid beta-Protein Precursor / biosynthesis
-
Amyloid beta-Protein Precursor / metabolism*
-
Animals
-
Cell Nucleus / metabolism*
-
Histone Acetyltransferases
-
Humans
-
Lysine Acetyltransferase 5
-
Membrane Proteins / metabolism*
-
Nerve Tissue Proteins / metabolism
-
Nuclear Proteins / metabolism
-
Presenilin-1
-
Protein Structure, Tertiary / physiology
-
Receptor, Notch1
-
Receptors, Cell Surface*
-
Signal Transduction / genetics*
-
Transcription Factors*
Substances
-
APBB1 protein, human
-
Amyloid beta-Protein Precursor
-
Membrane Proteins
-
NOTCH1 protein, human
-
Nerve Tissue Proteins
-
Nuclear Proteins
-
PSEN1 protein, human
-
Presenilin-1
-
Receptor, Notch1
-
Receptors, Cell Surface
-
Transcription Factors
-
Acetyltransferases
-
Histone Acetyltransferases
-
KAT5 protein, human
-
Lysine Acetyltransferase 5