Secretion kinetics of Alzheimer's amyloid beta-protein differs from secreted beta-amyloid precursor protein

Amyloid beta-protein (A beta) and secreted beta-amyloid precursor protein (sAPP), derived from beta-amyloid precursor protein (APP), are normally released by cultured mammalian cells. We investigated by pulse-chase analysis the secretion kinetics of these two APP derivatives using mouse cholinergic...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1995-09, Vol.214 (2), p.490-495
Main Authors: Araki, W, Kunishita, T, Takahashi, K, Ikeda, S, Tabira, T
Format: Article
Language:English
Subjects:
Amyloid beta-Peptides - biosynthesis
Amyloid beta-Peptides - isolation & purification
Amyloid beta-Protein Precursor - biosynthesis
Amyloid beta-Protein Precursor - isolation & purification
Animals
Autoradiography
Cell Line
Kinetics
Methionine - metabolism
Mice
Recombinant Proteins - biosynthesis
Recombinant Proteins - isolation & purification
Sulfur Radioisotopes
Transfection
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Summary:Amyloid beta-protein (A beta) and secreted beta-amyloid precursor protein (sAPP), derived from beta-amyloid precursor protein (APP), are normally released by cultured mammalian cells. We investigated by pulse-chase analysis the secretion kinetics of these two APP derivatives using mouse cholinergic SN49 cell lines stably transfected with mouse APP695 cDNA. After both A beta and sAPP peaked at about the second hour, sAPP decreased with a half-life of approximately 5 hours, but A beta remained almost unchanged for at least 14 hours. These results indicate that A beta is more stable than sAPP in the SN49 conditioned medium.
ISSN:0006-291X
DOI:10.1006/bbrc.1995.2313