title: The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer beta/A4-amyloid precursor protein: some technical notes.
abstract: 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 In this note, we review our published and unpublished data in relation to published reports from other laboratories using related systems.
authors.affiliation: Laboratory of Molecular and Cellular Neuroscience, Rockefeller University, New York, NY 10021.
authors.forename: S E
authors.initials: SE
authors.lastname: Gandy
authors.forename: J D
authors.initials: JD
authors.lastname: Buxbaum
authors.forename: T
authors.initials: T
authors.lastname: Suzuki
authors.forename: T V
authors.initials: TV
authors.lastname: Ramabhadran
authors.forename: G L
authors.initials: GL
authors.lastname: Caporaso
authors.forename: A C
authors.initials: AC
authors.lastname: Nairn
authors.forename: P
authors.initials: P
authors.lastname: Greengard
mesh_terms: D000682:Amyloid / Q000096:biosynthesis*; D016564:Amyloid beta-Protein Precursor / Q000378:metabolism*; D000818:Animals; D006801:Humans; D010446:Peptide Fragments / Q000378:metabolism*
chemical_list: D000682:Amyloid; D016564:Amyloid beta-Protein Precursor; D010446:Peptide Fragments