The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer beta/A4-amyloid precursor protein: some technical notes.
The proteolytic processing and secretion of APP are regulated by protein phosphorylation, especially via protein kinase C and protein phosphatases 1 and/or 2A. Our studies of these regulatory mechanisms have led us to perform extensive experimentation on the metabolism of APP carboxyl-terminal fragments, using as our system either untransfected, undifferentiated rat pheochromocytoma (PC12) cells or APP-baculovirus infected Sf9 cells. We have not assayed APP fragments for biological activity in either system. However, we have made potentially relevant observations regarding APP carboxyl-terminal fragment trafficking. In this note, we review our published and unpublished data in relation to published reports from other laboratories using related systems.
Gandy
S E
SE
Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.
Buxbaum
J D
JD
Suzuki
T
T
Ramabhadran
T V
TV
Caporaso
G L
GL
Nairn
A C
AC
Greengard
P
P
D000682:Amyloid / Q000096:biosynthesis*; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism*; D000818:Animals; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*
D000682:Amyloid; D016564:Amyloid beta-Protein Precursor; D010446:Peptide Fragments