PMID: 8466596Jan 1, 1993Paper

PC12 cells release stimulatory factors after transfection with beta/A4-C-terminal DNA of the Alzheimer amyloid precursor protein

Molecular and Chemical Neuropathology
R E MajochaC A Marotta

Abstract

The beta/A4 region of the amyloid precursor protein (APP) accumulates in brains of victims of Alzheimer disease (AD) where it is a major component of senile plaques. We examined the pathophysiological consequences of overexpression of the beta/A4-C-terminal DNA in PC12 cells. Serum-free conditioned media (SFCM) from positive transfectants stimulated control PC12 cells to extend neurites and increase in size. Unlike the factor that affected cell size, neurite lengthening activity was significantly decreased after immunoabsorption with anti-beta/A4 monoclonal antibodies (MAb) and changes in pH. The data support the view that among the consequences of beta/A4-C-terminal DNA overexpression in PC12 cells is the release of factors that stimulate nontransfected cells to undergo morphological transformations that include differentiation to a neuronal phenotype. It is hypothesized that similar activities that may contribute to the molecular pathophysiology of the disorder may be present in the AD brain.

References

Jul 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·L A Greene, A S Tischler
Aug 1, 1992·Proceedings of the National Academy of Sciences of the United States of America·B TateC A Marotta
Jan 1, 1992·Journal of Molecular Neuroscience : MN·C A MarottaB Tate
Aug 15, 1991·Proceedings of the National Academy of Sciences of the United States of America·N W KowallB A Yankner
Mar 14, 1990·Neuroscience Letters·J S WhitsonC W Cotman
Jul 14, 1989·Biochemical and Biophysical Research Communications·D SchubertT Oltersdorf
Feb 1, 1988·Proceedings of the National Academy of Sciences of the United States of America·S B ZainC A Marotta
Jun 1, 1987·Proceedings of the National Academy of Sciences of the United States of America·N K RobakisH M Wisniewski
Oct 1, 1986·The Journal of Cell Biology·J A Wagner, P A D'Amore
Feb 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·M Klagsbrun, Y Shing
Aug 16, 1984·Biochemical and Biophysical Research Communications·G G Glenner, C W Wong
Jun 1, 1983·Brain Research·G FerrariA Gorio
Apr 1, 1984·Proceedings of the National Academy of Sciences of the United States of America·G M Church, W Gilbert
May 16, 1984·Biochemical and Biophysical Research Communications·G G Glenner, C W Wong
Dec 1, 1983·The Journal of Cell Biology·M ManthorpeS Varon

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