Cation selective channels formed by a C-terminal fragment of β-amyloid precursor protein

Heejeong Kim, Yoo Hun Suh, Mun Han Lee, Pan Dong Ryu

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The C-terminal 105 amino acid fragment of β-amyloid precursor protein (CT105) is highly neurotoxic. To obtain insights into its cytotoxic effect, we examined the ionophoric effects of CT105 (10-1000 nM) on artificial lipid membranes. Macroscopic membrane conductance increased with CT105 concentration and its ionophoric effect was comparable to that of amyloid protein. The mean unitary conductance of CT105-induced channels was 120 pS and open-state probability was close to 1 at voltages from -80 to +80 mV. CT105-induced channels were selective to cations (P(K)/P(Cl) = 10.2), being most selective to Ca2+. These findings suggest that CT105 can cause direct neurotoxic effects by forming Ca2+ permeable cation channels on neuronal membranes.

Original languageEnglish (US)
Pages (from-to)1427-1431
Number of pages5
JournalNeuroReport
Volume10
Issue number7
DOIs
StatePublished - May 14 1999

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Amyloid beta-Protein Precursor
Cations
Artificial Membranes
Amyloidogenic Proteins
Membranes
Lipids
Amino Acids

Keywords

  • Alzheimer's disease
  • Amyloid β-precursor protein
  • C-terminal fragment
  • Cation selective
  • Ion channels
  • Planar lipid bilayer

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Cation selective channels formed by a C-terminal fragment of β-amyloid precursor protein. / Kim, Heejeong; Suh, Yoo Hun; Lee, Mun Han; Ryu, Pan Dong.

In: NeuroReport, Vol. 10, No. 7, 14.05.1999, p. 1427-1431.

Research output: Contribution to journalArticle

Kim, Heejeong ; Suh, Yoo Hun ; Lee, Mun Han ; Ryu, Pan Dong. / Cation selective channels formed by a C-terminal fragment of β-amyloid precursor protein. In: NeuroReport. 1999 ; Vol. 10, No. 7. pp. 1427-1431.
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