THE NATURE AND METABOLISM OF POTENTIALLY AMYLOIDOGENIC CARBOXYL-TERMINAL FRAGMENTS OF THE ALZHEIMER BETA A4-AMYLOID PRECURSOR PROTEIN - SOME TECHNICAL NOTES

被引:11
作者
GANDY, SE
BUXBAUM, JD
SUZUKI, T
RAMABHADRAN, TV
CAPORASO, GL
NAIRN, AC
GREENGARD, P
机构
[1] Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, NY 10021
关键词
APP SECRETION; PROTEIN PHOSPHORYLATION; CARBOXYL-TERMINAL FRAGMENTS;
D O I
10.1016/0197-4580(92)90063-4
中图分类号
R592 [老年病学]; C [社会科学总论];
学科分类号
03 ; 0303 ; 100203 ;
摘要
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 In this note, we review our published and unpublished data in relation to published reports from other laboratories using related systems.
引用
收藏
页码:601 / 603
页数:3
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