The keystone of Alzheimer pathogenesis might be sought in Aβ physiology

Puzzo, D.; Gulisano, W.; Arancio, O.; Palmeri, A.

doi:10.1016/j.neuroscience.2015.08.039

Cited by 119Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The keystone of Alzheimer pathogenesis might be sought in Aβ physiology

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Puzzo, D., Gulisano, W., Arancio, O., Palmeri, A.·2015·Neuroscience

DOI 10.1016/j.neuroscience.2015.08.039PMC PMC4591241

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Abstract

For several years Amyloid-beta peptide (Aβ) has been considered the main pathogenetic factor of Alzheimer's disease (AD). According to the so called Amyloid Cascade Hypothesis the increase of Aβ triggers a series of events leading to synaptic dysfunction and memory loss as well as to the structural brain damage in the later stage of the disease. However, several evidences suggest that this hypothesis is not sufficient to explain AD pathogenesis, especially considering that most of the clinical trials aimed to decrease Aβ levels have been unsuccessful. Moreover, Aβ is physiologically produced in the healthy brain during neuronal activity and it is needed for synaptic plasticity and memory. Here we propose a model interpreting AD pathogenesis as an alteration of the negative feedback loop between Aβ and its physiological receptors, focusing on alpha7 nicotinic acetylcholine receptors (α7-nAchRs). According to this vision, when Aβ cannot exert its physiological function a negative feedback mechanism would induce a compensatory increase of its production leading to an abnormal accumulation that reduces α7-nAchR function, leading to synaptic dysfunction and memory loss. In this perspective, the indiscriminate Aβ removal might worsen neuronal homeostasis, causing a further impoverishment of learning and memory. Even if further studies are needed to better understand and validate these mechanisms, we believe that to deepen the role of Aβ in physiological conditions might represent the keystone to elucidate important aspects of AD pathogenesis.

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Soluble amyloid-beta exerts physiological functions including modulating synaptic function, facilitating neuronal growth, protecting the brain from infections, repairing leaks in the blood-brain barrier, and promoting recovery from injury.
“Soluble Aβ exerts a physiological function, modulating synaptic function and facilitating neuronal growth; furthermore, Aβ protects the brain from infections, repairs leaks in the blood–brain barrier, and promotes recovery from injury [57, 58].”
From Clinical trials of new drugs for Alzheimer disease (2020) · cites this paper as [57]
In “Aβ Between Pathology and Physiology” (page unavailable), the paper describes low concentrations of soluble Aβ as supporting synaptic plasticity and reports that picomolar Aβ restored neuronal viability. It does not establish that Aβ facilitates neuronal growth, protects against infections, repairs blood–brain barrier leaks, or promotes recovery from injury; its discussion of neurite outgrowth concerns APP rather than Aβ. (LLM, conf=0.87)
Experimental — accuracy not yet measured
Under healthy conditions, soluble monomeric Aβ contributes to synaptic regulation, neuronal signaling, and neuroprotection through modulation of calcium homeostasis, metal ion binding, and antimicrobial defense.
“Under healthy conditions, soluble monomeric Aβ contributes to synaptic regulation, neuronal signaling, and neuroprotection through modulation of calcium homeostasis, metal ion binding, and antimicrobial defense [41–43].”
From Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses (2026) · cites this paper as [43]
In “Aβ Between Pathology and Physiology” (page unavailable), the paper says low soluble Aβ has a physiological synaptic role, affects neurotransmitter release, and acts through mechanisms involving Ca2+ channels; it also reports that low Aβ concentrations can restore neuronal survival. It cautions that the species responsible for normal synaptic function is unknown, rather than establishing an exclusively monomeric role. The passages do not support metal-ion binding or antimicrobial defense as mechanisms of that role. (LLM, conf=0.87)
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1 retracted

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Retracted
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“Nevertheless, the specific block of endogenous Ab by antibodies impairs LTP and memory (Garcia-Osta and Alberini, 2009; Morley et al., 2010; Puzzo et al., 2011) and, more importantly, this impairment is rescued by the administration of picomolar concentrations of Ab (Puzzo et al.”
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A failure of β-amyloid physiological function due to genetic deletion of α7 nicotinic acetylcholine receptors induces an Alzheimer’s disease-like pathologyPreprint
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Authors: Puzzo, D., Gulisano, W., Arancio, O., & Palmeri, A.
Affiliations: University of Catania (IT)
Columbia University (US)
Corresponding author: Puzzo, D.
ORCID: Puzzo, D.
Gulisano, W.
Arancio, O.
Palmeri, A.
Venue: Neuroscience
Publisher: Elsevier BV
Published: 2015-10
Volume: 307
Pages: 26-36
ISSN: 0306-4522 (ISSN-L)
DOI: 10.1016/j.neuroscience.2015.08.039
PMC: PMC4591241
OpenAlex: W1149434589
Cited by: 116
References: 181
Citations by year: 2026: 2 · 2025: 5 · 2024: 5 · 2023: 8 · 2022: 7 · 2021: 14 · 2020: 7 · 2019: 15 · 2018: 11 · 2017: 17 · 2016: 23 · 2015: 2
FWCI: 2.21
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuroscience (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: Alzheimer’s Association (NIRG-07-59597, IIRG-09-134220)
National Institutes of Health (NS049442, AG034248)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease pathogenesis, amyloid-beta, amyloid hypothesis, alpha7 nicotinic acetylcholine receptor, negative feedback loop, synaptic plasticity, memory loss, synaptic dysfunction
MeSH terms: Alzheimer Disease, Animals, Humans, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor

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