PHOSPHOLIPASE-A(2) ACTIVATION INFLUENCES THE PROCESSING AND SECRETION OF THE AMYLOID PRECURSOR PROTEIN

被引：74

作者：

EMMERLING, MR

MOORE, CJ

DOYLE, PD

CARROLL, RT

DAVIS, RE

机构：

[1] Parke-Davis Pharmaceutical Research, Division of Warner-Lambert Co., Ann Arbor, MI 48106

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 197卷 / 01期

关键词：

D O I：

10.1006/bbrc.1993.2474

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The phospholipase A2 (PLA2) inhibitors quinacrine, manoalide and scalaradial inhibit the carbachol-stimulated secretion of the amyloid precursor protein (APP) from cells transfected with the human m1 muscarinic receptor. Conversely, activation of PLA2 by melittin increases secretion of an apparently immature species of APP from these cells. These results implicate PLA2 in regulating APP processing and secretion, which may have important implications for understanding the pathogenesis of Alzheimer's disease. © 1993 Academic Press, Inc.

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页码：292 / 297

页数：6

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