Amyloid beta-protein activates tachykinin receptors and inositol trisphosphate accumulation by synergy with glutamate.
basic_science · Level V
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- Record sourced from PubMed, PMID 7689220.
- Also identified by PMC identifier 47171.
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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.
Medical subject headings
- Amyloid beta-Peptides
- Glutamates
- Inositol 1,4,5-Trisphosphate
- Oocytes
- Receptors, Glutamate
- Receptors, N-Methyl-D-Aspartate
- Receptors, Neurotransmitter