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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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 (US)
Pages (from-to)166-168
Number of pages3
JournalBrain research
Volume600
Issue number1
DOIs
StatePublished - Jan 8 1993

Keywords

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

ASJC Scopus subject areas

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

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