Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells

M. Di Stefano, G. Aleppo, G. Casabona, A. A. Genazzani, U. Scapagnini, F. Nicoletti

Research output: Contribution to journalArticle

Abstract

We have tested the interaction between amyloid β protein (AβP) and tachykinin receptors in cultured UC-11MG astrocytoma cells, which express high affinity substance P receptors and respond to substance P with an unusually large stimulation of polyphosphoinositide hydrolysis. Both the full-length AβP (AβP1-40) and the fragment 25-35 (AβP25-35) did not affect the stimulation of [3H]inositolmonophosphate (InsP) formation by substance P. AβP25-35 was also inactive when applied to the cultures 18 or 72 h prior to the assay. In addition, AβP25-35 did not displace specifically bound [3H]SarMet substance P from its recognition sites in intact UC-11MG cells. These results suggest that, at least in this specific cell type, amyloid peptides do not interact with substance P receptors.

Original languageEnglish
Pages (from-to)166-168
Number of pages3
JournalBrain Research
Volume600
Issue number1
DOIs
Publication statusPublished - Jan 8 1993

Keywords

  • Amyloid β protein
  • Phosphoinositide hydrolysis
  • Substance P
  • UC-11MG astrocytoma cell

ASJC Scopus subject areas

  • Developmental Biology
  • Molecular Biology
  • Clinical Neurology
  • Neuroscience(all)

Fingerprint Dive into the research topics of 'Amyloid β protein does not interact with tachykinin receptors coupled to inositol phospholipid hydrolysis in human astrocytoma cells'. Together they form a unique fingerprint.

  • Cite this