Fc. Bronfman et al., AMYLOID PRECURSOR PROTEIN-FRAGMENT AND ACETYLCHOLINESTERASE INCREASE WITH CELL CONFLUENCE AND DIFFERENTIATION IN A NEURONAL CELL-LINE, Experimental cell research, 229(1), 1996, pp. 93-99
This study addresses the developmental regulation of amyloid precursor
protein (APP) fragments comprising the amyloid-beta peptide (A beta)
and the amyloid-promoting factor acetylcholinesterase (AChE) in a mous
e neuronal cell line (Neuro-2a). Results indicate that a 35-kDa amyloi
dogenic fragment of APP and the major molecular forms of AChE (G(1) an
d G(4)) in Neuro-2a cells significantly increase with increasing level
s of cell confluence. The foregoing molecules undergo further increase
s when neuroblastoma cells differentiate in the presence of dibutyryl
cAMP. In contrast, a 17-kDa fragment of APP and butyrylcholinesterase
mere not affected by cell confluence or differentiation. These finding
s are the first to indicate that a selective A beta-containing fragmen
t of APP is subject to developmental regulation. Moreover, our data sh
ow that the 35-kDa fragment and AChE forms respond in parallel to the
same developmental stimuli, i.e., cell confluence and differentiation.
This points to the existence of a functional relationship between bot
h molecules, a notion that is consistent with the potential role that
has been ascribed to AChE in both APP processing and the formation of
amyloid deposits in Alzheimer's brains. (C) 1996 Academic Press, Inc.