Amyloid β protein-induced irreversible current in rat cortical neurones

Katsutoshi Furukawa, Yumiko Abe, Norio Akaike

Research output: Contribution to journalArticlepeer-review

63 Citations (Scopus)


THE effect of amyloid β protein (AβP) was examined in neurones dissociated from rat cortex using the nystatin perforated patch-clamp technique. AjSP at concentrations >10 nM induced an irreversible slow inward current associated with an increase in membrane conductance. The time lag until the appearance of the effect of AβP shortened in a concentration-dependent manner. When extracellular Na+ and Cl-, and intracellular K+ were replaced by equimolar N-methyl glucamine, isothionate and Cs+, respectively, the membrane conductance and the reversal potential were not affected. Even when an internal solution including 1,2-bis(0-aminophenoxy)eth- ane-N,N,N’N’-tetraacetic acid (20 mM) was used, the effect of AβP did not alter. It is suggested that AβP binds to the neuronal membrane and opens non-selective ion channels, resulting in neuronal degeneration.

Original languageEnglish
Pages (from-to)2016-2018
Number of pages3
Issue number16
Publication statusPublished - 1994 Oct


  • Amyloid β protein
  • Cortical neurone
  • Neuronal degeneration
  • Patch-clamp
  • Rat

ASJC Scopus subject areas

  • Neuroscience(all)


Dive into the research topics of 'Amyloid β protein-induced irreversible current in rat cortical neurones'. Together they form a unique fingerprint.

Cite this