TY - JOUR
T1 - Amyloid precursor protein fragment and acetylcholinesterase increase with cell confluence and differentiation in a neuronal cell line
AU - Bronfman, Francisca C.
AU - Fernandez, Hugo L.
AU - Inestrosa, Nibaldo C.
N1 - Funding Information:
We thank Drs. Steven Younkin and Greg Cole for their kind gift of antibodies. This study was supported partially by a predoctoral fellowship from CONICYT to F.C.B., a Medical Research Service grant of the U.S. Department of Veterans Affairs to H.L.F., a grant from FONDECYT (Na 1940694) to N.C.I., and a Presidential Chair in Science from the Chilean Government to N.C.I.
PY - 1996/11/25
Y1 - 1996/11/25
N2 - This study addresses the developmental regulation of amyloid precursor protein (APP) fragments comprising the amyloid-β peptide (Aβ) and the amyloid-p promoting factor acetyicholinesterase (ACHE) in a mouse neuronal cell line (Neuro-2a). Results indicated that a 35-kDa amyloidogenic fragment of APP and the major molecular forms of AChE (G~1 and G~4) in Neuro-2a cells significantly increase with increasing levels of cell confluence. The foregoing molecules undergo further increases when neuroblastoma cells differentiate in the presence of dibutyryl cAMP. In contrast, a 17-kDa fragment of APP and butyrylcholinesterase were not affected by cell confluence or differentiation. These findings are the first to indicate that a selective Aβ-containing fragment of APP is subject to develop mental regulation. Moreover, our data show 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 both 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.
AB - This study addresses the developmental regulation of amyloid precursor protein (APP) fragments comprising the amyloid-β peptide (Aβ) and the amyloid-p promoting factor acetyicholinesterase (ACHE) in a mouse neuronal cell line (Neuro-2a). Results indicated that a 35-kDa amyloidogenic fragment of APP and the major molecular forms of AChE (G~1 and G~4) in Neuro-2a cells significantly increase with increasing levels of cell confluence. The foregoing molecules undergo further increases when neuroblastoma cells differentiate in the presence of dibutyryl cAMP. In contrast, a 17-kDa fragment of APP and butyrylcholinesterase were not affected by cell confluence or differentiation. These findings are the first to indicate that a selective Aβ-containing fragment of APP is subject to develop mental regulation. Moreover, our data show 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 both 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.
UR - http://www.scopus.com/inward/record.url?scp=0030601933&partnerID=8YFLogxK
U2 - 10.1006/excr.1996.0347
DO - 10.1006/excr.1996.0347
M3 - Article
C2 - 8940253
AN - SCOPUS:0030601933
SN - 0014-4827
VL - 229
SP - 93
EP - 99
JO - Experimental Cell Research
JF - Experimental Cell Research
IS - 1
ER -