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β-淀粉样蛋白通过与谷氨酸协同作用激活速激肽受体并促进三磷酸肌醇积累。

Amyloid beta-protein activates tachykinin receptors and inositol trisphosphate accumulation by synergy with glutamate.

作者信息

Kimura H, Schubert D

机构信息

Salk Institute, San Diego, CA 92186-5800.

出版信息

Proc Natl Acad Sci U S A. 1993 Aug 15;90(16):7508-12. doi: 10.1073/pnas.90.16.7508.

Abstract

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.

摘要

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。

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