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Synthetic amyloid-β oligomers impair long-term memory independently of cellular prion protein
Open accessAbstract
Inability to form new memories is an early clinical sign of Alzheimer’s disease (AD). There is ample evidence that the amyloid-β (Aβ) peptide plays a key role in the pathogenesis of this disorder. Soluble, bio-derived oligomers of Aβ are proposed as the key mediators of synaptic and cognitive dysfunction, but more tractable models of Aβ−mediated cognitive impairment are needed. Here we report that, in mice, acute intracerebroventricular injections of synthetic Aβ 1–42 oligomers impaired consolidation of the long-term recognition memory, whereas mature Aβ 1–42 fibrils and freshly dissolved peptide did not. The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody. It has been suggested that the cellular prion protein (PrP C ) mediates the impairment of synaptic plasticity induced by Aβ. We confirmed that Aβ 1–42 oligomers interact with PrP C , with nanomolar affinity. However, PrP-expressing and PrP knock-out mice were equally susceptible to this impairment. These data suggest that Aβ 1–42 oligomers are responsible for cognitive impairment in AD and that PrP C is not required.
Overview
AI snapshot
Written from the paper’s full text.
TL;DR
Acute intracerebroventricular injection of synthetic Aβ1–42 oligomers impaired consolidation of long-term object-recognition memory in mice, whereas fibrils and freshly dissolved peptide did not. Although Aβ oligomers bound cellular prion protein (PrPC) with high affinity, PrP-expressing and PrP knockout mice were equally susceptible, indicating PrPC is not required for this memory impairment.
Key findings
- Synthetic Aβ1–42 oligomers (estimated 10–50 nM) impaired long-term recognition memory; mature fibrils and freshly dissolved Aβ did not.
- The oligomer-induced deficit was reversible: memory had fully recovered 10 days after injection without further Aβ, and was completely prevented by i.c.v. pretreatment with 0.25 μg/2 μL of the anti-Aβ antibody 4G8.
- Aβ oligomers bound PrPC with high affinity (Kd ≤20 nM monomer equivalent), but Prnp 0/0 mice were as susceptible as Prnp +/+ mice to oligomer-induced memory impairment; oligomers were also toxic to both Prnp +/+ and Prnp 0/0 hippocampal neurons in vitro.
- Oligomers disrupted memory encoding/consolidation but not retrieval: injection before familiarization prevented memory, whereas injection before the test phase did not.
Methods
- Male C57BL/6 mice, 7–8 weeks old, received acute i.c.v. injections of synthetic Aβ1–42 preparations and were tested in the novel-object recognition task; Prnp 0/0 and Prnp +/+ mice were compared.
- Aβ1–42 oligomers, fibrils, and initial-state peptide were characterized by atomic force microscopy and size exclusion chromatography before behavioral testing.
- Binding to PrPC was measured by surface plasmon resonance using brain homogenates and anti-PrP antibodies; primary hippocampal neuron cultures were treated with 1–3 μM oligomers for 72 h and survival measured by MTT assay. Statistical analysis used ANOVA with post hoc tests.
Limitations
- The paper states that one limitation is the use of oligomeric Aβ preparations not proven identical to those found in AD patient brains.
- Evident from the text: object recognition memory is associated more with perirhinal cortex than hippocampus, so the behavioral model may not fully align with hippocampal LTP studies.
- Evident from the text: the study used only male C57BL/6 mice and a single behavioral task, and it does not establish the mechanism linking Aβ oligomer binding to PrPC with memory impairment.
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Claims the paper makes
20 Own result · 18 Not checked yet · 11 Own interpretation · 2 No basis given · 1 Own method
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody.”
- Also stated in: § Results · plain
“After 10 days, with no further Aβ injection, the memory deficit had fully recovered (Fig. 3A).”
plaindirect- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“However, PrP-expressing and PrP knock-out mice were equally susceptible to this impairment.”
- Also stated in: § Results · plain
“We found that Prnp 0/0 mice were as susceptible as Prnp +/+ mice to oligomer-induced memory impairment (Figs. 2B and 4A).”
plain- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Here we report that, in mice, acute intracerebroventricular injections of synthetic Aβ1–42 oligomers impaired consolidation of the long-term recognition memory, whereas mature Aβ1–42 fibrils and freshly dissolved peptide did not.”
- Also stated in: § Results · plain
“Aβ oligomer–injected mice were unable to distinguish the new object, with no significant difference in the percentage of time spent investigating the two (Fig. 2A), and a discrimination index significantly lower than vehicle-injected mice (Fig. 2B).”
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“We confirmed that Aβ1–42 oligomers interact with PrPC, with nanomolar affinity.”
- Also stated in: § Results · plain
“The binding was dose dependent, with a dissociation constant (K d) of ≤20 nM monomer equivalent (Fig. 7 B and D).”
plaincorrelational- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: passes — The paper’s conclusions depend on it.
- Based: passes — The paper gives a reason why it holds.
- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“The deficit induced by oligomers was reversible and was prevented by an anti-Aβ antibody.”
- Also stated in: § Results · plain
“An i.c.v. injection of 0.25 μg/2 μL of 4G8, 5 min before the Aβ oligomers, completely prevented the memory impairment (Fig. 3B).”
plaindirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
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- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“but found no evidence that the two events are related.”
plain- Asserted: passes — The authors put it forward as true.
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A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“An i.c.v. injection of 4G8 alone did not affect memory.”
plain- Asserted: passes — The authors put it forward as true.
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- Load-bearing: unclear — It is unclear whether the paper’s conclusions depend on it.
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A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“On the basis of SEC, we estimated the actual oligomer concentration in this sample as 10–50 nM.”
- Also stated in: § Discussion · plain
“The effect was detectable at a nanomolar concentration of Aβ oligomers (10–50 nM).”
plain- Asserted: passes — The authors put it forward as true.
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- Also stated in: § Discussion · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“A single i.c.v. injection of a nanomolar concentration of synthetic Aβ1–42 oligomers impairs memory consolidation within 24 h, suggesting that oligomers rapidly interfere with the synaptic activity necessary for the stabilization of new memories.”
plaindirect- Asserted: passes — The authors put it forward as true.
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A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Heat-denatured antibody, unable to bind Aβ, could not antagonize the effect of Aβ oligomers.”
hedged- Asserted: passes — The authors put it forward as true.
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- It may state two separate claims as one. 14
- Probably not a substantial claim. 15
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“whereas mature Aβ1–42 fibrils and freshly dissolved peptide did not.”
- Also stated in: § Results · plain
“Neither Aβ in the initial state nor the fibrils affected memory (Fig. 2 A and B).”
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Results · plain
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“When Aβ initial state, oligomers or fibrils were assayed for their binding to PrPC, only Aβ oligomers bound PrPC specifically, and Aβ initial state and fibrils did not (Fig. 7 A and C).”
plaincorrelational- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Mice injected 2 h before familiarization were unable to remember the object previously investigated, whereas mice injected 2 h before the test phase recalled the familiar object investigated the day before (Fig. 8).”
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A result the paper reports from its own data — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Preliminary data confirmed that the captured protein is actually PrPC, as no capture was detected when flowing brain homogenate from Prnp 0/0 mice (Fig. 6).”
plain- Asserted: passes — The authors put it forward as true.
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In the paper
“PrPC binds synthetic Aβ oligomers with high affinity and plays a role in the oligomer-mediated inhibition of LTP (17).”
What the sources say
- Not checked yetcites [17] Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009;457:1128–1132. doi: 10.1038/nature07761. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“All of these processes are affected by Aβ oligomers in vitro, using primary neuronal cultures (12, 15, 36, 37).”
What the sources say
- Not checked yetcites [12] Shankar GM, et al. Natural oligomers of the Alzheimer amyloid-beta protein induce reversible synapse loss by modulating an NMDA-type glutamate receptor-dependent signaling pathway. J Neurosci. 2007;27:2866–2875. doi: 10.1523/JNEUROSCI.4970-06.2007. [DOI] [PMC free article] [PubMed] [Google Scholar] source
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- Not checked yetcites [36] Hsieh H, et al. AMPAR removal underlies Abeta-induced synaptic depression and dendritic spine loss. Neuron. 2006;52:831–843. doi: 10.1016/j.neuron.2006.10.035. [DOI] [PMC free article] [PubMed] [Google Scholar] source
- Not checked yetcites [37] Lacor PN, et al. Synaptic targeting by Alzheimer’s-related amyloid beta oligomers. J Neurosci. 2004;24:10191–10200. doi: 10.1523/JNEUROSCI.3432-04.2004. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“Several neuronal receptors have been proposed as mediating the effect of Aβ on synaptic plasticity and memory, including the α-7-nicotinic (16), glutamatergic (39–40), and insulin (14) receptors.”
What the sources say
- Not checked yetcites [16] Snyder EM, et al. Regulation of NMDA receptor trafficking by amyloid-beta. Nat Neurosci. 2005;8:1051–1058. doi: 10.1038/nn1503. [DOI] [PubMed] [Google Scholar] source
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hedgedconditional- Asserted: passes — The authors put it forward as true.
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- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“These data indicate that Aβ oligomers acutely disrupt anterograde memory storage but do not interfere with its retrieval when the information has been properly stored.”
- Also stated in: § Discussion · plain
“Aβ oligomers inhibited the encoding/consolidation of information, without affecting its retrieval if properly stored.”
plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
- Also stated in: § Discussion · plain
In the paper
“In an elegant study Lauren et al. (17) reported that PrPC mediates the Aβ oligomer-induced hippocampal synaptic plasticity impairment.”
What the sources say
- Not checked yetcites [17] Laurén J, Gimbel DA, Nygaard HB, Gilbert JW, Strittmatter SM. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-beta oligomers. Nature. 2009;457:1128–1132. doi: 10.1038/nature07761. [DOI] [PMC free article] [PubMed] [Google Scholar] source
plaindirect- Asserted: fails — The authors may not put it forward as true.
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Probably not a substantial claim. The authors may not put it forward as true. The paper’s conclusions may not depend on it.
In the paper
“Because recognition memory is dependent on the medial temporal lobe including the hippocampus (25), we examined whether oligomer-mediated memory impairment was also related to PrPC expression.”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“Unlike Aβ aggregates purified from biological sources, synthetic Aβ oligomers are chemically defined, and can be easily produced and biophysically characterized.”
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“However, some human and primate studies have shown that hippocampal lesions result in impaired object recognition (41, 42)”
What the sources say
- Not checked yetcites [41] Reed JM, Squire LR. Impaired recognition memory in patients with lesions limited to the hippocampal formation. Behav Neurosci. 1997;111:667–675. doi: 10.1037//0735-7044.111.4.667. [DOI] [PubMed] [Google Scholar]
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hedgeddirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
What the paper did — it cites no source for this, so there is none to check. The quote shows it is in the paper.
In the paper
“These preparations, and freshly dissolved Aβ1−42 (hereafter referred to as “initial state”), were characterized by atomic force microscopy (AFM) and size exclusion chromatography (SEC) before behavioral investigation.”
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Thus, although Aβ oligomers interact with PrPC with high affinity, they do not act together to induce memory derangement.”
plain- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“PrPC has been involved in neurotrophic signaling (44, 45), and in the regulation of Aβ-production (46), suggesting that PrPC and Aβ may be part of a common molecular pathway governing neuronal differentiation.”
What the sources say
- Not checked yetcites [44] Kanaani J, Prusiner SB, Diacovo J, Baekkeskov S, Legname G. Recombinant prion protein induces rapid polarization and development of synapses in embryonic rat hippocampal neurons in vitro. J Neurochem. 2005;95:1373–1386. doi: 10.1111/j.1471-4159.2005.03469.x. [DOI] [PubMed] [Google Scholar]
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plaincorrelational- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“However, some human and primate studies have shown that hippocampal lesions result in impaired object recognition (41, 42) and that, for the 24 h intertrial interval from familiarization to test phase used in our study, hippocampal activity is required (43).”
What the sources say
- Not checked yetcites [43] Hammond RS, Tull LE, Stackman RW. On the delay-dependent involvement of the hippocampus in object recognition memory. Neurobiol Learn Mem. 2004;82:26–34. doi: 10.1016/j.nlm.2004.03.005. [DOI] [PubMed] [Google Scholar] source
plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
None of the sources cited for this claim have been checked yet.
In the paper
“Memory processing requires NMDA receptor activation and intracellular signaling leading to AMPA receptor trafficking, synthesis of new proteins, and formation of dendritic spines (34, 35).”
What the sources say
- Not checked yetcites [34] Collingridge GL, Isaac JT, Wang YT. Receptor trafficking and synaptic plasticity. Nat Rev Neurosci. 2004;5:952–962. doi: 10.1038/nrn1556. [DOI] [PubMed] [Google Scholar]
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plaindirect- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
In the paper
“The novel-object recognition task is simple and reproducible, it measures recognition memory, which is heavily impaired in AD, and relies on spontaneous animal behavior without the need for stressor elements such as food or water deprivation, electric foot-shock, or aversive environments like water (25).”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plain- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“Proof that Aβ oligomers are the active amyloid-β species was the lack of effect of either the freshly solubilized Aβ (initial state) or fibrils.”
boosteddirect- Asserted: passes — The authors put it forward as true.
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- Load-bearing: passes — The paper’s conclusions depend on it.
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It may state two separate claims as one.
In the paper
“The novel-object recognition task is simple and reproducible, it measures recognition memory, which is heavily impaired in AD, and relies on spontaneous animal behavior without the need for stressor elements such as food or water deprivation, electric foot-shock, or aversive environments like water (25).”
What the sources say
- Not checked yetcites [25] Squire LR, Wixted JT, Clark RE. Recognition memory and the medial temporal lobe: A new perspective. Nat Rev Neurosci. 2007;8:872–883. doi: 10.1038/nrn2154. [DOI] [PMC free article] [PubMed] [Google Scholar]
plaincorrelational- Asserted: passes — The authors put it forward as true.
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Probably not a substantial claim. The paper’s conclusions may not depend on it. It may state two separate claims as one.
None of the sources cited for this claim have been checked yet.
In the paper
“At variance with the native peptide, the depsi-peptide is highly soluble and it has a much lower propensity to aggregate, thus preventing the spontaneous formation of seeds in the solution (49, 50).”
What the sources say
- Not checked yetcites [49] Taniguchi A, et al. “Click peptide”: pH-triggered in situ production and aggregation of monomer Abeta1-42. ChemBioChem. 2009;10:710–715. doi: 10.1002/cbic.200800765. [DOI] [PubMed] [Google Scholar]
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plaindirect- Asserted: passes — The authors put it forward as true.
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It may state two separate claims as one.
A conclusion the paper draws from its own results — it cites no other source for it, so there is none to check. The quote shows it is in the paper.
In the paper
“One limitation of this study worth to be mentioned may be the use of oligomeric Aβ preparations which haven’t been proven to be identical to those found in the brain of AD patients.”
hedged- Asserted: passes — The authors put it forward as true.
- Checkable: passes — It can be checked against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. The paper’s conclusions may not depend on it.
The paper states this without a source or data behind it here, so there is nothing to check it against. The quote shows it is in the paper.
In the paper
“The novel-object recognition task is simple and reproducible”
plain- Asserted: passes — The authors put it forward as true.
- Checkable: fails — It may be too vague to check against evidence.
- Load-bearing: fails — The paper’s conclusions may not depend on it.
- Based: passes — The paper gives a reason why it holds.
Probably not a substantial claim. It may be too vague to check against evidence. The paper’s conclusions may not depend on it. It may state two separate claims as one.
The paper relies on this without support.
Synthetic Aβ1–42 oligomers injected intracerebroventricularly in mice reproduce the relevant actions of endogenous Aβ oligomers in Alzheimer’s disease.
“These data suggest that Aβ1–42 oligomers are responsible for cognitive impairment in AD and that PrPC is not required.”
“Soluble, bio-derived oligomers of Aβ are proposed as the key mediators of synaptic and cognitive dysfunction, but more tractable models of Aβ−mediated cognitive impairment are needed.”
The paper relies on this without support.
There is no consensus as to which brain-derived oligomeric species mediate cognitive deficits in AD.
“since there remains no consensus as to which brain-derived oligomeric species mediate cognitive deficits in AD”
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“Atomic Force Microscopy (AFM) was used to verify the actual and correct formation of the Aβ1-42 fibrils ([36]) [68,69].”
From PCSK9 affects astrocyte cholesterol metabolism and reduces neuron cholesterol supplying in vitro: potential implications in Alzheimer’s disease (2022) · cites this paper as [69]
In the citing paper
“other studies have shown that PrP-expressing and PrP-knockout mice are equally susceptible to long-term memory impairment induced by Aβ oligomers (Balducci et al., 2010; Calella et al., 2010)”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Balducci et al., 2010
Citations
Cites
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769
RetractedMemory - A century of consolidation
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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Mice devoid of PrP are resistant to scrapie
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Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
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Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 5×
“Almeida CG, et al. (2005) Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses.”
InfluentialCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Cited by
Sorted by citations
Items 101–200 of 468
Repression of phagocytosis by human CD33 is not conserved with mouse CD33
Bhattacherjee, A., Rodrigues, E., Jung, J., Luzentales-Simpson, M., Enterina, J. R., Galleguillos, D., Laurent, C. D. S., Nakhaei‐Nejad, M., Fuchsberger, F. F., Streith, L., et al. (2019) · Communications Biology · doi:10.1038/s42003-019-0698-6 · Cited by 101
Synaptic Cell Adhesion Molecules in Alzheimer’s Disease
Leshchyns’ka, I., & Sytnyk, V. (2016) · Neural Plasticity · doi:10.1155/2016/6427537 · Cited by 93
“However, memory impairment induced by injection of Aβ oligomers is not reduced in PrPc knockoutmice [77], ablation or overexpression of PrPc has no effect on the impairment of hippocampal synaptic plasticity in a transgenic model of AD [78], and synaptic depression, reduction in spine density, or blockade of LTP is in…”
BackgroundShrivastava, A. N., Aperia, A. C., Melki, R., & Triller, A. (2017) · Neuron · doi:10.1016/j.neuron.2017.05.026 · Cited by 96
Röthlisberger, P., Gasse, C., & Hollenstein, M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18112430 · Cited by 97
Ugalde, C. L., Finkelstein, D. I., Lawson, V. A., & Hill, A. F. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13772 · Cited by 92
“It has been reported PrP knockout mice are resistant to toxicity elicited by Ab oligomers (Lauren et al. 2009), however, follow-up studies have been unable to observe such a striking effect (Balducci et al. 2010; Calella et al. 2010; Kessels et al. 2010; Cisse et al. 2011).”
BackgroundSharma, S., Verma, S., Kapoor, M., Saini, A., & Nehru, B. (2016) · Neurological Research · doi:10.1080/01616412.2016.1209337 · Cited by 92
Cellular prion protein as a receptor for amyloid-β oligomers in Alzheimer's disease
Salazar, S. V., & Strittmatter, S. M. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.09.062 · Cited by 94
Peripheral inflammation exacerbates α‐synuclein toxicity and neuropathology in Parkinson's models
Vitola, P. L., Balducci, C., Baroni, M., Artioli, L., Santamaria, G., Castiglioni, M., Cerovic, M., Colombo, L., Caldinelli, L., Pollegioni, L., et al. (2020) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12644 · Cited by 89
Self-citationTherapeutic potential of mGluR5 targeting in Alzheimer's disease
Kumar, A., Dhull, D. K., & Mishra, P. S. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00215 · Cited by 93
“However, a successive study ruled out the PrPC mediated oligomer induced memory impairment and cytotoxicity (Balducci et al., 2010).”
BackgroundThe sheddase ADAM10 is a potent modulator of prion disease
Altmeppen, H. C., Prox, J., Krasemann, S., Puig, B., Kruszewski, K., Dohler, F., Bernreuther, C., Hoxha, A., Linsenmeier, L., Sikorska, B., et al. (2015) · eLife · doi:10.7554/elife.04260 · Cited by 89
Amyloid-β-induced Synapse Damage Is Mediated via Cross-linkage of Cellular Prion Proteins
Bate, C., & Williams, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248724 · Cited by 93
The missing link in the amyloid cascade of Alzheimer’s disease – Metal ions
Tiiman, A., Palumaa, P., & Tõugu, V. (2013) · Neurochemistry International · doi:10.1016/j.neuint.2013.01.023 · Cited by 92
“Different biochemically distinct oligomeric species have been identified and shown to be toxic both in vitro and in vivo (Ahmed et al., 2010; Balducci et al., 2010; Cizas et al., 2010; Freir et al., 2011; Walsh et al., 2002).”
The Prion Protein Ligand, Stress-Inducible Phosphoprotein 1, Regulates Amyloid-β Oligomer Toxicity
Ostapchenko, V. G., Beraldo, F. H., Mohammad, A. H., Xie, Y., Hirata, P. H. F., Magalhães, A. C., Lamour, G., Li, H., Maciejewski, A., Belrose, J. C., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3214-13.2013 · Cited by 87
“…were analyzed using a simple bimolecular binding model with GraphPad Software Prism linear (for initial binding rates), exponential decay (for off-kinetics), and “one-site binding” (to determine RUmax and KD from the Langmuir equation for the STI1–PrP complex) regressions (Balducci et al., 2010).”
MethodResultInfluentialHaas, L. T., Kostylev, M. A., & Strittmatter, S. M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.584342 · Cited by 91
Soluble Prion Protein Inhibits Amyloid-β (Aβ) Fibrillization and Toxicity
Nieznański, K., Choi, J.-K., Chen, S., Surewicz, K. A., & Surewicz, W. K. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c112.400614 · Cited by 90
“Previous studies have shown that the prion protein binds with high affinity to relatively large (2–6 nm in diameter) toxic oligomers of A 1–42, but not to the monomeric form of the peptide (11, 19, 21).”
BackgroundPathogenesis of Abeta Oligomers in Synaptic Failure
Sivanesan, S., Tan, A., & Rajadas, J. (2013) · Current Alzheimer Research · doi:10.2174/1567205011310030011 · Cited by 85
“Acute intracerebroventricular injections of A oligomers impair long-term recognition memory [82, 83].”
BackgroundBrody, A. H., & Strittmatter, S. M. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.09.007 · Cited by 89
“…longer periods of high-concentration Aβo incubation, appear to be independent of PrPC, suggesting that these phenotypes may be mediated by alternative Aβo receptors or possibly distinct species of oligomeric Aβ (Balducci et al., 2010; Calella et al., 2010; Cisse et al., 2011; Kessels et al., 2010).”
BackgroundPrion Protein as a Toxic Acceptor of Amyloid-β Oligomers
Purro, S. A., Nicoll, A. J., & Collinge, J. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.11.020 · Cited by 81
EphA4 Activation of c-Abl Mediates Synaptic Loss and LTP Blockade Caused by Amyloid-β Oligomers
M. Vargas, L., Leal, N., Estrada, L. D., González, A., Serrano, F., Araya, K., Gysling, K., Inestrosa, N. C., Pasquale, E. B., & Alvarez, A. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092309 · Cited by 85
Diverse functions of the prion protein – Does proteolytic processing hold the key?
Linsenmeier, L., Altmeppen, H. C., Wetzel, S., Mohammadi, B., Säftig, P., & Glatzel, M. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.06.022 · Cited by 83
Pitt, J. E., Wilcox, K. C., Tortelli, V., Diniz, L. P., Oliveira, M. S., Dobbins, C., Yu, X., Nandamuri, S., Gomes, F. C. A., DiNunno, N., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0416 · Cited by 87
“…al., 2006) and AD neuropathology, including tau hyperphosphorylation and synapse dysfunction and deterioration (De Felice et al., 2007, 2008; Lacor et al., 2007; Ma et al., 2009; Balducci et al., 2010; Nimmrich et al., 2010; Tomiyama et al., 2010; Sebollela et al., 2012; Figueiredo et al., 2013).”
BackgroundProteotoxicity and Neurodegenerative Diseases
Ruz, C., Alcantud, J. L., Montero, F. V., Durán, R., & Bandrés‐Ciga, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165646 · Cited by 84
Thal, D. R., & Tomé, S. O. (2022) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2022.10.006 · Cited by 92
Canovi, M., Markoutsa, E., Lazar, A. N., Pampalakis, G., Clemente, C., Re, F., Sesana, S., Masserini, M., Salmona, M., Duyckaerts, C. J., et al. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.04.020 · Cited by 84
Self-citationA Rationally Designed Humanized Antibody Selective for Amyloid Beta Oligomers in Alzheimer’s Disease
Gibbs, E., Silverman, J. M., Zhao, B., Peng, X., Wang, J., Wellington, C. L., Mackenzie, I. R., Plotkin, S. S., Kaplan, J. M., & Cashman, N. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-46306-5 · Cited by 83
Doxycycline counteracts neuroinflammation restoring memory in Alzheimer's disease mouse models
Balducci, C., Santamaria, G., Vitola, P. L., Brandi, E., Grandi, F., Viscomi, A. R., Beeg, M., Gobbi, M., Salmona, M., Ottonello, S., et al. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.06.002 · Cited by 83
Self-citationTylek, K., Trojan, E., Regulska, M., Lacivita, E., Leopoldo, M., & Basta‐Kaim, A. (2021) · Pharmacological Reports · doi:10.1007/s43440-021-00271-x · Cited by 83
Proteolytic processing of the prion protein in health and disease.
Altmeppen, H. C., Puig, B., Dohler, F., Thurm, D., Falker‐Gieske, C., Krasemann, S., & Glatzel, M. (2012) · Europe PMC (PubMed Central) · Cited by 93
Amyloid-β42 Interacts Mainly with Insoluble Prion Protein in the Alzheimer Brain
Zou, W., Xiao, X., Yuan, J., Puoti, G., Fujioka, H., Wang, X., Richardson, S. L., Zhou, X., Zou, R. S., Li, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199356 · Cited by 81
APP transgenic mice: their use and limitations
Balducci, C., & Forloni, G. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8141-7 · Cited by 79
“APP23Tg and Tg2576 mice have been helpful for identifying changes in N-methyl-D-aspartate (NMDA) receptor traffic or altered response to the MK-801 antag- onist (Snyder et al. 2005; Balducci et al. 2010b).”
InfluentialSelf-citationLi, M. C., Xu, C., Ren, J., Wang, E., & Qu, X. (2013) · Chemical Communications · doi:10.1039/c3cc46772d · Cited by 81
Chung, H., Park, K., Jang, H. J., Kohl, M. M., & Kwag, J. (2020) · Brain Structure and Function · doi:10.1007/s00429-020-02044-3 · Cited by 85
Doxycycline for Alzheimer’s Disease: Fighting β-Amyloid Oligomers and Neuroinflammation
Balducci, C., & Forloni, G. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00738 · Cited by 74
“From transgenic mouse models of AD, it emerged that the onset of synaptic and cognitive dysfunction preceded plaque deposition (Holcomb et al., 1998; Hsia et al., 1999; Mucke et al., 2000; Balducci et al., 2010b).”
BackgroundResultInfluentialSelf-citationKasza, Á., Penke, B., Frank, Z., Bozsó, Z., Szegedi, V., Hunya, Á. G., Németh, K., Kozma, G., & Fülöp, L. (2017) · Molecules · doi:10.3390/molecules22112007 · Cited by 78
Neurotoxic Mutants of the Prion Protein Induce Spontaneous Ionic Currents in Cultured Cells
Solomon, I. H., Huettner, J. E., & Harris, D. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.134619 · Cited by 73
Involvement of Cellular Prion Protein in α-Synuclein Transport in Neurons
Urrea, L., Segura-Feliu, M., Masuda‐Suzukake, M., Hervera, A., Pedraz, L., García‐Aznar, J. M., Vila, M., Samitier, J., Torrents, E., Ferrer, I., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0451-4 · Cited by 78
Yi, J. H., Baek, S. J., Heo, S., Park, H. J., Kwon, H., Lee, S., Jung, J.-W., Park, S. J., Kim, B. C., Lee, Y. C., et al. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.10.028 · Cited by 76
“Synthetic Ab transiently impaired hippocampus-dependent memory (Balducci et al., 2010).”
Caetano, F. A., Beraldo, F. H., Hajj, G. N. M., Guimaraes, A. L., Jürgensen, S., Wasilewska-Sampaio, A. P., Hirata, P. H. F., Souza, I., Machado, C. F., Wong, D. Y.-L., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07225.x · Cited by 74
“In spite of this, it is well established that Ab binds to PrPC (Lauren et al. 2009; Balducci et al. 2010; Calella et al. 2010; Chen et al. 2010).”
BackgroundResultAlpha-synuclein oligomers impair memory through glial cell activation and via Toll-like receptor 2
Vitola, P. L., Balducci, C., Cerovic, M., Santamaria, G., Brandi, E., Grandi, F., Caldinelli, L., Colombo, L., Morgese, M. G., Trabace, L., et al. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.02.012 · Cited by 74
Self-citationInhibiting BACE1 to reverse synaptic dysfunctions in Alzheimer’s disease
Yan, R., Fan, Q., Zhou, J., & Vassar, R. J. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.025 · Cited by 71
“…to replicate the role of PrP in Aβ-induced synaptic depression, reduction in spine density, or blockade of LTP, regardless of whether PrP was overexpressed or ablated (Balducci et al., 2010; Calella et al., 2010; Kessels et al., 2010), arguing against a critical role of PrP as a coupling receptor.”
Hamilton, A., Zamponi, G. W., & Ferguson, S. S. G. (2015) · Molecular Brain · doi:10.1186/s13041-015-0107-0 · Cited by 72
“Oligomeric forms of Aβ42 also bind to PrP to alter synaptic plasticity and recent work clearly supports the concept that PrP is required for Aβ42 oligomer-mediated neuronal toxicity [25,59-65].”
BackgroundMore, J., Galusso, N., Veloso, P., Montecinos, L., Finkelstein, J. P., Sánchez, G., Bull, R., Valdés, J. L., Hidalgo, C., & Paula-Lima, A. C. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00399 · Cited by 71
SIRPα polymorphisms, but not the prion protein, control phagocytosis of apoptotic cells
Nuvolone, M., Kana, V., Hütter, G., Sakata, D., Mortin-Toth, S. M., Russo, G., Danska, J. S., & Aguzzi, A. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20131274 · Cited by 70
“…or inhibit autophagy (Oh et al., 2008, 2012; Korom et al., 2013) and to be indispensable or dispensable to mediate A toxicity (Laurén et al., 2009; Balducci et al., 2010; Calella et al., 2010; Gimbel et al., 2010; Kessels et al., 2010; Cissé et al., 2011; Larson et al., 2012; Um et al., 2012).”
BackgroundCellular prion protein and NMDA receptor modulation: protecting against excitotoxicity
Black, S. A. G., Stys, P. K., Zamponi, G. W., & Tsutsui, S. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00045 · Cited by 68
“…of Aβ peptides that occur in AD, although the requirement of PrPC for Aβ-induced toxicity has been controversial, with some investigators finding that PrPC was not required for the pathological effects of Aβ (Balducci et al., 2010; Calella et al., 2010; Kessels et al., 2010; Cisse et al., 2011).”
BackgroundAmyloid and Alzheimer's Disease: Inside and Out
Tam, J. H. K., & Pasternak, S. (2012) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100013408 · Cited by 64
Béland, M., & Roucou, X. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07613.x · Cited by 65
Sinomenine inhibits microglial activation by Aβ and confers neuroprotection
Shukla, S. M., & Sharma, S. K. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-117 · Cited by 66
“[3-6]].”
Sivilia, S., Lorenzini, L., Giuliani, A., Gusciglio, M., Fernández, M., Baldassarro, V. A., Mangano, C., Ferraro, L., Pietrini, V., Baroc, M. F., et al. (2013) · BMC Neuroscience · doi:10.1186/1471-2202-14-44 · Cited by 65
“This test, which is based on spontaneous animal behavior and does not require any exogenously applied stress, is widely used for memory evaluation in mouse models of AD [37-39].”
BackgroundKaiser, D., Acharya, M., Leighton, P. L. A., Wang, H., Daude, N., Wohlgemuth, S. L., Shi, B., & Allison, W. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051305 · Cited by 63
“published [5] translation blocking morpholino designed to specifically bind the 59 UTR of zebrafish prp1 mRNA (59 TGA GCA GAG AGT GCT GCG GGA GAG A 39).”
BackgroundPyrroloquinoxaline hydrazones as fluorescent probes for amyloid fibrils
Gemma, S., Colombo, L., Forloni, G., Savini, L., Fracasso, C., Caccia, S., Salmona, M., Brindisi, M., Joshi, B. P., Tripaldi, P., et al. (2011) · Organic & Biomolecular Chemistry · doi:10.1039/c1ob05288h · Cited by 63
Self-citationNicole, O., Hadžibegović, S., Gajda, J., Bontempi, B., Bem, T., & Meyrand, P. (2016) · Scientific Reports · doi:10.1038/srep22728 · Cited by 61
Zhang, Y., Zhao, Y., Zhang, L., Yu, W., Wang, Y., & Chang, W. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00339 · Cited by 58
“For example, Balducci et al. (2010) demonstrated that Aβ oligomers induced in vivo memory impairment and bound PrPC with high affinity but found that PrPC is not responsible for the recognition impairment in AD induced by Aβ.”
BackgroundCentral and peripheral circadian clocks and their role in Alzheimer's disease
Chauhan, R., Chen, K.-F., Kent, B. A., & Crowther, D. C. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.030627 · Cited by 58
“Activating this mediator of innate immunity, which classically responds to bacteria-derived lipopolysaccharide, likely enhances the proinflammatory environment in the brain in AD (Balducci et al., 2010; Huang et al., 2017).”
BackgroundNovel targets in Alzheimer’s disease: A special focus on microglia
Balducci, C., & Forloni, G. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.017 · Cited by 62
Self-citationWang, X., Xu, W. R., Chen, H., Li, W., Li, W., & Zhu, G. (2020) · Brain Research · doi:10.1016/j.brainres.2020.147041 · Cited by 61
The Peculiar Role of the A2V Mutation in Amyloid-β (Aβ) 1–42 Molecular Assembly
Messa, M., Colombo, L., Favero, E. D., Cantú, L., Stoilova, T., Cagnotto, A., Rossi, A., Morbin, M., Fede, G. D., Tagliavini, F., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576256 · Cited by 59
“4, and incubated for 24 h at 4 or 22 °C to obtain oligomer-rich preparations (36, 37).”
BackgroundSelf-citationGuzmán, B. C., Chaffey, T. E., Palpagama, T. H., Waters, S., Boix, J., Tate, W. P., Peppercorn, K., Dragunow, M., Waldvogel, H. J., Faull, R. L. M., et al. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.552073 · Cited by 63
“Much evidence has shown that spatial memory impairment is caused by Aβ deposition and the subsequent synaptic dysfunction, among other Aβ-mediated effects, in the hippocampal area (Balducci et al., 2010).”
BackgroundBalducci, C., Mehdawy, B., Mare, L., Giuliani, A., Lorenzini, L., Sivilia, S., Giardino, L., Calzà, L., Lanzillotta, A., Sarnico, I., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101839 · Cited by 58
Self-citationStravalaci, M., Bastone, A., Beeg, M., Cagnotto, A., Colombo, L., Fede, G. D., Tagliavini, F., Cantú, L., Favero, E. D., Mazzanti, M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334979 · Cited by 60
“Consistently, we previously found that 4G8 also antagonizes the memory impairment induced by intracerebroventricular injection of synthetic A 1–42 oligomers in mice (22).”
BackgroundMethodSelf-citationAntibody-based therapy in Alzheimer's disease
Pul, R., Dodel, R. C., & Stangel, M. (2011) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.2011.552884 · Cited by 59
Coskuner‐Weber, O., & Uversky, V. N. (2017) · Intrinsically Disordered Proteins · doi:10.1080/21690707.2017.1377813 · Cited by 57
Vitola, P. L., Beeg, M., Balducci, C., Santamaria, G., Restelli, E., Colombo, L., Caldinelli, L., Pollegioni, L., Gobbi, M., Chiesa, R., et al. (2018) · Brain · doi:10.1093/brain/awy318 · Cited by 56
“Furthermore, at molecular level, we verified the existence of a direct binding between -synO and PrPC by surface plas- mon resonance (SPR), using the same approach described for the investigation of AbO-PrPC interaction (Balducci et al., 2010).”
BackgroundMethodInfluentialSelf-citationBrambilla, D., Verpillot, R., Taverna, M., Kimpe, L. D., Droumaguet, B. L., Nicolas, J., Canovi, M., Gobbi, M., Mantegazza, F., Salmona, M., et al. (2010) · Analytical Chemistry · doi:10.1021/ac102045x · Cited by 59
Self-citationCui, Y., Ma, S., Zhang, C., et al. (2017) · Behavioural Brain Research · doi:10.1016/j.bbr.2017.09.011 · Cited by 56
Terrone, G., Pauletti, A., Salamone, A., Rizzi, M., Villa, B. R., Porcu, L., Sheehan, M. J., Guilmette, E. R., Butler, C. R., Piro, J. R., et al. (2017) · Epilepsia · doi:10.1111/epi.13950 · Cited by 54
Vandendriessche, C., Balusu, S., Cauwenberghe, C. V., Brkić, M., Pauwels, M. J., Plehiers, N., Bruggeman, A., Dujardin, P., Imschoot, G. V., Wonterghem, E. V., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01245-z · Cited by 58
Peters, C., Espinoza, M. P., Gallegos, S., Opazo, C., & Aguayo, L. G. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.11.019 · Cited by 56
Amin, L., & Harris, D. A. (2021) · Nature Communications · doi:10.1038/s41467-021-23507-z · Cited by 59
The Molecular Assembly of Amyloid Aβ Controls Its Neurotoxicity and Binding to Cellular Proteins
Manzoni, C., Colombo, L., Bigini, P., Diana, V., Cagnotto, A., Messa, M., Lupi, M., Bonetto, V., Pignataro, M., Airoldi, C., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024909 · Cited by 55
“However, this result is still quite controversial [15] because more than one single and specific protein seem to be involved in triggering of Ab dependent neuronal alterations.”
BackgroundSelf-citationInhibition of group-I metabotropic glutamate receptors protects against prion toxicity
Goniotaki, D., Lakkaraju, A. K., Shrivastava, A. N., Bakirci, P., Sorce, S., Senatore, A., Marpakwar, R., Hornemann, S., Gasparini, F., Triller, A., et al. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006733 · Cited by 52
Amyloid beta receptors responsible for neurotoxicity and cellular defects in Alzheimer’s disease
Kam, T., Gwon, Y., & Jung, Y. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1706-0 · Cited by 59
“Further, cognitive impairment is not ameliorated in Ab-injected mice lacking PrP [61].”
BackgroundAmyloid Oligomer Neurotoxicity, Calcium Dysregulation, and Lipid Rafts
Malchiodi‐Albedi, F., Paradisi, S., Matteucci, A., Frank, C., & Diociaiuti, M. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/906964 · Cited by 55
Dinamarca, M. C., Weinstein, D. B., Monasterio, O., & Inestrosa, N. C. (2011) · Biochemistry · doi:10.1021/bi201246t · Cited by 53
Salazar, S. V., Gallardo, C., Kaufman, A. C., Herber, C. S., Haas, L. T., Robinson, S., Manson, J. C., Lee, M. K., & Strittmatter, S. M. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0722-17.2017 · Cited by 55
Ding, M., Ding, S., Du, D., Wang, X., Hu, X., Guan, P., Lyu, Z., & Lin, Y. (2023) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2023.117087 · Cited by 56
Roles of endoproteolytic α‐cleavage and shedding of the prion protein in neurodegeneration
Altmeppen, H. C., Prox, J., Puig, B., Dohler, F., Falker‐Gieske, C., Krasemann, S., & Glatzel, M. (2013) · FEBS Journal · doi:10.1111/febs.12196 · Cited by 56
Mechanisms of prion-induced neurodegeneration
Saá, P., Harris, D. A., & Červen̆áková, L. (2016) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2016.8 · Cited by 52
Cellular Prion Protein as a Therapeutic Target in Alzheimer's Disease
Laurén, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130950 · Cited by 55
“administration of A oligomers, despite that fact that the same research group had earlier reported that this toxic effect of A oligomers was not mediated by PrPC [9].”
BackgroundMethodResultInfluentialLiu, L., Xia, N., Jiang, M., Huang, N., Guo, S., Li, S., & Zhang, S. (2015) · Journal of Electroanalytical Chemistry · doi:10.1016/j.jelechem.2015.06.017 · Cited by 52
Scott-McKean, J. J., Surewicz, K. A., Choi, J.-K., Ruffin, V. A., Salameh, A., Nieznański, K., Costa, A. C. S., & Surewicz, W. K. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.03.001 · Cited by 49
“…cell-surface PrP C (Dohler et al., 2014; Freir et al., 2011; Lauren et al., 2009; Nicoll et al., 2013; AC C EP TE D M AN U SC R IP T Zou et al., 2011) and soluble, GPI-free recombinant human prion protein (Balducci et al., 2010; Chen et al., 2010; Fluharty et al., 2013; Nieznanski et al., 2014).”
Sáez-Orellana, F., Godoy, P. A., Bastidas, C. Y., Silva-Grecchi, T., Guzmán, L., Aguayo, L. G., & Fuentealba, J. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2015.04.005 · Cited by 50
“…by us and others, this selectivity could be explained according to recent findings suggesting that Prion Proteins (PrPc) might be acting as receptors for oligomers in the plasmamembrane, with a nanomolar affinity between PrPc and amyloid oligomers (Lauren et al., 2009; Balducci et al., 2010).”
Ganzinger, K. A., Narayan, P. S., Qamar, S., Weimann, L., Ranasinghe, R. T., Aguzzi, A., Dobson, C. M., McColl, J. T., George‐Hyslop, P. S., & Klenerman, D. (2014) · ChemBioChem · doi:10.1002/cbic.201402377 · Cited by 50
Kam, T., Park, H., Gwon, Y., Song, S., Kim, S.-H., Moon, S. W., Jo, D., & Jung, Y. (2016) · eLife · doi:10.7554/elife.18691 · Cited by 47
Sharma, S., Nehru, B., & Saini, A. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.011 · Cited by 48
“…correlated soluble Ab 42 oligomers with the progression of AD and cognitive decline (Zussy et al., 2013; Wang et al., 2016; Ferreira et al., 2015; Balducci et al., 2010, 2016) and are also considered to be the keymediators of synaptic and cognitive dysfunction (Ahmed et al., 2010; Benilova et…”
BackgroundMemantine prevents memory consolidation failure induced by soluble beta amyloid in rats
Tucci, P., Mhillaj, E., Morgese, M. G., Colaianna, M., Zotti, M., Schiavone, S., Cicerale, M., Trezza, V., Campolongo, P., Cuomo, V., et al. (2014) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2014.00332 · Cited by 49
“The NOR2 test was performed according to Balducci et al. (2010).”
MethodInfluentialA Mutant Prion Protein Sensitizes Neurons to Glutamate-Induced Excitotoxicity
Biasini, E., Unterberger, U., Solomon, I. H., Massignan, T., Senatore, A., Bian, H.-J., Voigtländer, T., Bowman, F. P., Bonetto, V., Chiesa, R., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3406-12.2013 · Cited by 48
“Recently, PrP C has also been shown to mediate the toxicity of other pathological protein aggregates, including oligomers of the amyloid (A ) peptide, which are associated with Alzheimer’s disease (Laurén et al., 2009; Balducci et al., 2010; Chen et al., 2010; Resenberger et al., 2011).”
BackgroundSelf-citationRuotolo, R., Minato, I., Vitola, P. L., Artioli, L., Curti, C., Franceschi, V., Brindani, N., Amidani, D., Colombo, L., Salmona, M., et al. (2020) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900890 · Cited by 55
Self-citationSidiropoulou, G. A., Metaxas, A., & Kourti, M. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1217730 · Cited by 54
Li, M. C., Guan, Y., Chen, Z., Gao, N., Ren, J., Dong, K., & Qu, X. (2016) · Nano Research · doi:10.1007/s12274-016-1127-5 · Cited by 45
Xing, Y., Feng, X., Zhang, L., Hou, J., Han, G., & Chen, Z. (2017) · International Journal of Nanomedicine · doi:10.2147/ijn.s132776 · Cited by 46
Béland, M., Bédard, M., Tremblay, G., Lavigne, P., & Roucou, X. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.02.001 · Cited by 44
Nitrosylation of GAPDH augments pathological tau acetylation upon exposure to amyloid-β
Sen, T., Saha, P., & Sen, N. (2018) · Science Signaling · doi:10.1126/scisignal.aao6765 · Cited by 47
Impaired Spatial Reorientation in the 3xTg-AD Mouse Model of Alzheimer’s Disease
Stimmell, A. C., Baglietto‐Vargas, D., Moseley, S. C., Lapointe, V., Thompson, L. M., LaFerla, F. M., McNaughton, B. L., & Wilber, A. A. (2019) · Scientific Reports · doi:10.1038/s41598-018-37151-z · Cited by 42
Presenilin mouse and zebrafish models for dementia: Focus on neurogenesis
van Tijn, P., Kamphuis, W., Marlatt, M. W., Hol, E. M., & Lucassen, P. J. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.10.008 · Cited by 43
“A physiological role for Ab42 in mediating synaptic plasticity has been suggested (Balducci et al., 2010; Shankar et al., 2008), and the cellular prion protein can act as an Ab-oligomer receptor (Lauren et al., 2009).”
BackgroundNguyen, H. L., Linh, H. Q., Krupa, P., Penna, G. L., & Li, M. S. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.2c01769 · Cited by 41
Risse, E., Nicoll, A. J., Taylor, W. A., Wright, D., Badoni, M., Yang, X., Farrow, M. A., & Collinge, J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.637124 · Cited by 43
Papotti, B., Adorni, M. P., Marchi, C., Zimetti, F., Ronda, N., Panighel, G., Lupo, M. G., Vilella, A., Giuliani, D., Ferri, N., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012192 · Cited by 41
Gasperini, L., & Legname, G. (2014) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2014.00044 · Cited by 45
“…Aβ and PrP exists, but the use of different in vitro or transgenic models has yielded contrasting results (Schwarze-Eicker et al., 2005; Lauren et al., 2009; Balducci et al., 2010; Calella et al., 2010; Chung et al., 2010; Kessels et al., 2010; Morales et al., 2010; Ordonez-Gutierrez et al., 2013).”
ResultCellular prion protein targets amyloid-β fibril ends via its C-terminal domain to prevent elongation
Bove‐Fenderson, E., Urano, R., Straub, J. E., & Harris, D. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.789990 · Cited by 42
Goswami, P., Afjal, M. A., Akhter, J., Mangla, A., Khan, J., Parvez, S., & Raisuddin, S. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.09.022 · Cited by 39
Metadata
- Authors
- Balducci, C., Beeg, M., Stravalaci, M., Bastone, A., Sclip, A., Biasini, E., Tapella, L., Colombo, L., Manzoni, C., Borsello, T., Chiesa, R., Gobbi, M., Salmona, M., & Forloni, G.
- Affiliations
- Mario Negri Institute for Pharmacological Research (IT)
- Dulbecco Telethon Institute (IT)
- ORCID
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2010-01-19
- Volume
- 107
- Issue
- 5
- Pages
- 2295-2300
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC2836680
- OpenAlex
- W2002280328
- Semantic Scholar
- 63625a2fc958c65a2cb276db617f403efa9be515
- Cited by
- 466
- References
- 57
- Citations by year
- 2026: 3 · 2025: 8 · 2024: 14 · 2023: 19 · 2022: 20 · 2021: 24 · 2020: 31 · 2019: 25 · 2018: 32 · 2017: 40 · 2016: 31 · 2015: 35 · 2014: 27 · 2013: 47 · 2012: 36
- FWCI
- 33.78
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Iris (University of Trento) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › 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
- amyloid-beta oligomers, amyloid-beta 42, Alzheimer's disease, long-term memory, memory consolidation, recognition memory, cellular prion protein, anti-amyloid antibodies, cognitive impairment, intracerebroventricular administration, amyloid fibrils
- MeSH terms
- Prion Proteins, Alzheimer Disease, Animals, Cognition Disorders, Humans, Injections, Intraventricular, Male, Memory, Mice, Inbred C57BL, Neuronal Plasticity, Peptide Fragments, Prions, Protein Binding, Amyloid beta-Peptides, Mice, Knockout, PrPC Proteins, Surface Plasmon Resonance, Mice
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