Evidence map›Paper›PMID 29665128›Full record

ArticleBrain pathology (Zurich, Switzerland)2019

A role for astrocyte-derived amyloid β peptides in the degeneration of neurons in an animal model of temporal lobe epilepsy.

A Kodam, D Ourdev, M Maulik, J Hariharakrishnan, M Banerjee, Y Wang, S Kar

Open access · greenAbstract read
In one paragraph

Article in Brain pathology (Zurich, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 27 citations in OpenAlex.

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  14. Annexin A1-derived peptide AcJournal of neuroinflammation · 2019
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

A KodamDepartment of Psychiatry, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
D OurdevDepartment of Psychiatry, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
M MaulikCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
J HariharakrishnanCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
M BanerjeeCentre for Prions and Protein Folding Diseases, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
Y WangDepartment of Psychiatry, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.
S KarDepartment of Psychiatry, University of Alberta, Edmonton, Alberta, Canada, T6G 2M8.ORCID 0000-0003-0167-3808
University of Alberta · CA

Funding

CIHR
6 · The paper itself

Abstract

Kainic acid, an analogue of the excitatory neurotransmitter glutamate, can trigger seizures and neurotoxicity in the hippocampus and other limbic structures in a manner that mirrors the neuropathology of human temporal lobe epilepsy (TLE). However, the underlying mechanisms associated with the neurotoxicity remain unclear. Since amyloid-β (Aβ) peptides, which are critical in the development of Alzheimer's disease, can mediate toxicity by activating glutamatergic NMDA receptors, it is likely that the enhanced glutamatergic transmission that renders hippocampal neurons vulnerable to kainic acid treatment may involve Aβ peptides. Thus, we seek to establish what role Aβ plays in kainic acid-induced toxicity using in vivo and in vitro paradigms. Our results show that systemic injection of kainic acid to adult rats triggers seizures, gliosis and loss of hippocampal neurons, along with increased levels/processing of amyloid precursor protein (APP), resulting in the enhanced production of Aβ-related peptides. The changes in APP levels/processing were evident primarily in activated astrocytes, implying a role for astrocytic Aβ in kainic acid-induced toxicity. Accordingly, we showed that treating rat primary cultured astrocytes with kainic acid can lead to increased Aβ production/secretion without any compromise in cell viability. Additionally, we revealed that kainic acid reduces neuronal viability more in neuronal/astrocyte co-cultures than in pure neuronal culture, and this is attenuated by precluding Aβ production. Collectively, these results indicate that increased production/secretion of Aβ-related peptides from activated astrocytes can contribute to neurotoxicity in kainic acid-treated rats. Since kainic acid administration can lead to neuropathological changes resembling TLE, it is likely that APP/Aβ peptides derived from astrocytes may have a role in TLE pathogenesis.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesAnimalsAstrocytesBrainCells, CulturedDisease Models, AnimalEpilepsy, Temporal LobeHippocampusHumansKainic AcidMaleNeurodegenerative DiseasesNeuronsAmyloid beta-PeptidesAmyloid beta-Protein PrecursorAmyloid Precursor Protein SecretasesKainic AcidPeptide FragmentsReceptors, N-Methyl-D-Aspartateamyloid precursor proteinepilepsyneurodegenerationreactive astrocytesβ-amyloid peptideβ-secretaseγ-secretase

Identifiers

PMID29665128
PMCPMC8028321
OpenAlexW2802082294

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.