AMYLOID BETA-PROTEIN ACTIVATES TACHYKININ RECEPTORS AND INOSITOL TRISPHOSPHATE ACCUMULATION BY SYNERGY WITH GLUTAMATE

被引:54
作者
KIMURA, H
SCHUBERT, D
机构
[1] Salk Institute, San Diego, CA 92186-5800
关键词
SUBSTANCE-P RECEPTOR; GLUTAMATE RECEPTORS;
D O I
10.1073/pnas.90.16.7508
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The biological function of the soluble form of the amyloid beta-protein (ABP) was examined by assaying its interaction with neuronal receptors expressed in Xenopus oocytes. ABP weakly activated tachykinin receptors, but in the presence of N-methyl-D-aspartate and alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate-type glutamate receptors ABP-induced responses were greatly enhanced. Glutamate and ABP together also induced accumulation of inositol trisphosphate and increases in intracellular Ca2+. These observations suggest that in the presence of glutamate, ABP can activate tachykinin receptors and phosphatidylinositol turnover. ABP may therefore act as a neuromodulatory peptide.
引用
收藏
页码:7508 / 7512
页数:5
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