The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein: Some technical notes

Samuel E. Gandy; Joseph D. Buxbaum; Toshiharu Suzuki; Triprayar V. Ramabhadran; Gregg L. Caporaso; Angus C. Nairn; Paul Greengard

doi:10.1016/0197-4580(92)90063-4

The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein: Some technical notes

Samuel E. Gandy, Joseph D. Buxbaum, Toshiharu Suzuki, Triprayar V. Ramabhadran, Gregg L. Caporaso, Angus C. Nairn, Paul Greengard

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

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 S19 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 In this note, we review our published and unpublished data in relation to published reports from other laboratories using related systems.

Original language	English
Pages (from-to)	601-603
Number of pages	3
Journal	Neurobiology of Aging
Volume	13
Issue number	5
DOIs	https://doi.org/10.1016/0197-4580(92)90063-4
State	Published - 1992
Externally published	Yes

Keywords

APP secretion
Carboxyl-terminal fragments
Protein phosphorylation

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10.1016/0197-4580(92)90063-4

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title = "The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-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 S19 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.",

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T1 - The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein

T2 - Some technical notes

AU - Gandy, Samuel E.

AU - Buxbaum, Joseph D.

AU - Suzuki, Toshiharu

AU - Ramabhadran, Triprayar V.

AU - Caporaso, Gregg L.

AU - Nairn, Angus C.

AU - Greengard, Paul

PY - 1992

Y1 - 1992

N2 - 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 S19 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.

AB - 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 S19 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.

KW - APP secretion

KW - Carboxyl-terminal fragments

KW - Protein phosphorylation

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The nature and metabolism of potentially amyloidogenic carboxyl-terminal fragments of the Alzheimer βA4-amyloid precursor protein: Some technical notes

Abstract

Keywords

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