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Amyloid Peptide Channels

Authors
  • Kagan, B.L.1
  • Azimov, R.1
  • Azimova, R.1
  • 1 UCLA, Department of Psychiatry, Neuropsychiatric Institute, David Geffen School of Medicine, Los Angeles, California, 90024-1759, USA , Los Angeles
Type
Published Article
Journal
The Journal of Membrane Biology
Publisher
Springer-Verlag
Publication Date
Nov 01, 2004
Volume
202
Issue
1
Pages
1–10
Identifiers
DOI: 10.1007/s00232-004-0709-4
Source
Springer Nature
Keywords
License
Yellow

Abstract

At least 16 distinct clinical syndromes including Alzheimer’s disease (AD), Parkinson’s disease (PD), rheumatoid arthritis, type II diabetes mellitus (DM), and spongiform encephelopathies (prion diseases), are characterized by the deposition of amorphous, Congo red-staining deposits known as amyloid. These “misfolded” proteins adopt β-sheet structures and aggregate spontaneously into similar extended fibrils despite their widely divergent primary sequences. Many, if not all, of these peptides are capable of forming ion-permeable channels in vitro and possibly in vivo. Common channel properties include irreversible, spontaneous insertion into membranes, relatively large, heterogeneous single-channel conductances, inhibition of channel formation by Congo red, and blockade of inserted channels by Zn2+. Physiologic effects of amyloid, including Ca2+ dysregulation, membrane depolarization, mitochondrial dysfunction, inhibition of long-term potentiation (LTP), and cytotoxicity, suggest that channel formation in plasma and intracellular membranes may play a key role in the pathophysiology of the amyloidoses.

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