ArticleBiophysical journal1997
Alzheimer's disease amyloid beta-protein forms Zn(2+)-sensitive, cation-selective channels across excised membrane patches from hypothalamic neurons.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed, 217 citations in OpenAlex.
- Decoding the mechanisms of amyloid-β in synaptic toxicity.Journal of Alzheimer's disease : JAD · 2026Review
- The structure of tyrosine-10 favors ionic conductance of Alzheimer's disease-associated full-length amyloid-β channels.Nature communications · 2024Article
- Current understanding of metal-dependent amyloid-β aggregation and toxicity.RSC chemical biology · 2023Review
- Endogenous Amyloid-formed CaFunction (Oxford, England) · 2023Article
- An Unbalanced Synaptic Transmission: Cause or Consequence of the Amyloid Oligomers Neurotoxicity?International journal of molecular sciences · 2021Review
- Amyloids: The History of Toxicity and Functionality.Biology · 2021Review
- Neurometals in the Pathogenesis of Prion Diseases.International journal of molecular sciences · 2021Review
- Progress toward Alzheimer's disease treatment: Leveraging the Achilles' heel of Aβ oligomers?Protein science : a publication of the Protein Society · 2020Review
- Amyloids: Regulators of Metal Homeostasis in the Synapse.Molecules (Basel, Switzerland) · 2020Review
- On the Role of Platelet-Generated Amyloid Beta Peptides in Certain Amyloidosis Health Complications.Frontiers in immunology · 2020Review
- Accumulation of Amyloid Beta (Aβ) Peptide on Blood Vessel Walls in the Damaged Brain after Transient Middle Cerebral Artery Occlusion.Biomolecules · 2019Article
- Platelet-generated amyloid beta peptides in Alzheimer's disease and glaucoma.Histology and histopathology · 2019Review
- Hypoxia induces HT-22 neuronal cell death via Orai1/CDK5 pathway-mediated Tau hyperphosphorylation.American journal of translational research · 2019Article
- Amyloid Beta Peptide Is Released during Thrombosis in the Skin.International journal of molecular sciences · 2018Article
- Modulation of Alzheimer's amyloid β peptide oligomerization and toxicity by extracellular Hsp70.Cell stress & chaperones · 2018Article
- Zinc, Carnosine, and Neurodegenerative Diseases.Nutrients · 2018Review
- Metal Ion Effects on Aβ and Tau Aggregation.International journal of molecular sciences · 2018Review
- Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Interface focus · 2017Review
- Ion Channel Formation by Amyloid-β42 Oligomers but Not Amyloid-β40 in Cellular Membranes.The Journal of biological chemistry · 2017Article
- Platelets are responsible for the accumulation of β-amyloid in blood clots inside and around blood vessels in mouse brain after thrombosis.Brain research bulletin · 2017Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have previously shown that the 40-residue peptide termed amyloid beta-protein (A beta P[1-40]) in solution forms cation-selective channels across artificial phospholipid bilayer membranes. To determine whether A beta P[1-40] also forms channels across natural membranes, we used electrically silent excised membrane patches from a cell line derived from hypothalamic gonadotrophin-releasing hormone GnRH neurons. We found that exposing either the internal or the external side of excised membrane patches to A beta P[1-40] leads to the spontaneous formation of cation-selective channels. With Cs+ as the main cation in both the external as well as the internal saline, the amplitude of the A beta P[1-40] channel currents was found to follow the Cs+ gradient and to exhibit spontaneous conductance changes over a wide range (50-500 pS). We also found that free zinc (Zn2+), reported to bind to amyloid beta-protein in solution, can block the flow of Cs+ through the A beta P[1-40] channel. Because the Zn2+ chelator o-phenanthroline can reverse this blockade, we conclude that the underlying mechanism involves a direct interaction between the transition element Zn2+ and sites in the A beta P[1-40] channel pore. These properties of the A beta P[1-40] channel are rather similar to those observed in the artificial bilayer system. We also show here, by immunocytochemical confocal microscopy, that amyloid beta-protein molecules form deposits closely associated with the plasma membrane of a substantial fraction of the GnRH neurons. Taken together, these results suggest that the interactions between amyloid beta-protein and neuronal membranes also occur in vivo, lending further support to the idea that A beta P[1-40] channel formation might be a mechanism of amyloid beta-protein neurotoxicity.
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