Kimura H, Schubert D
Salk Institute, San Diego, CA 92186-5800.
Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7508-12. doi: 10.1073/pnas.90.16.7508.
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.
通过检测可溶性β淀粉样蛋白(ABP)与非洲爪蟾卵母细胞中表达的神经元受体的相互作用,对其生物学功能进行了研究。ABP可微弱激活速激肽受体,但在存在N-甲基-D-天冬氨酸和α-氨基-3-羟基-5-甲基异恶唑-4-丙酸型谷氨酸受体的情况下,ABP诱导的反应会大大增强。谷氨酸和ABP共同作用还可诱导三磷酸肌醇的积累并使细胞内钙离子增加。这些观察结果表明,在谷氨酸存在的情况下,ABP可激活速激肽受体并促进磷脂酰肌醇的转换。因此,ABP可能作为一种神经调节肽发挥作用。