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Role of amyloid precursor protein (APP): Study with antisense transfection of human neuroblastoma cells
Author(s) -
LeBlanc A. C.,
Kovacs D. M.,
Chen H. Y.,
Villaré F.,
Tykocinski M.,
AutilioGambetti L.,
Gambetti P.
Publication year - 1992
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490310407
Subject(s) - transfection , neurite , neuroblastoma , amyloid precursor protein , cell adhesion , microbiology and biotechnology , neural cell adhesion molecule , cell growth , biology , cell culture , messenger rna , cell , gene , in vitro , medicine , biochemistry , alzheimer's disease , genetics , disease
Abstract The function of amyloid precursor protein (APP) was investigated in human neuroblastoma La‐N‐1 cells by stable transfection with a DNA construct encoding antisense APP mRNA. Levels of APP mRNA, as well as proteins, were reduced by 80–90% in antisense APP transfected (ASAT) cells. ASAT cells exhibited three main features as a result of APP gene expression deprivation: (1) a 30% reduction in cell proliferation, (2) reduced cell adhesion that could be reversed by the addition of La‐N‐1 conditioned media as a source of secreted APP, and (3) a two‐ and four fold increase in neurite‐bearing cells suggesting that; cellular APP may be involved in neurite extension. The first two features confirm previously reported functions for APP in proliferation and adhesion of non‐neuronal cell types but the use of neuroblastoma cells in this study disclose a novel role for cellular APP in neurite extension.