Evidence map›Paper›PMID 38916724›Full record

ArticleBrain structure & function2024

Bnip3 expression is strongly associated with reelin-positive entorhinal cortex layer II neurons.

Stig W Omholt, Raissa Lejneva, Maria Jose Lagartos Donate, Domenica Caponio, Evandro Fei Fang, Asgeir Kobro-Flatmoen

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Article in Brain structure & function, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

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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

4 citing papers in PubMed.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors.

Stig W OmholtDepartment of Circulation and Medical Imaging, Norwegian University of Science and Technology (NTNU), 7491, Trondheim, Norway.
Raissa LejnevaKavli Institute for Systems Neuroscience, Norwegian University of Science and Technology (NTNU), 7491, Trondheim, Norway.
Maria Jose Lagartos DonateDepartment of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, 1478, Lørenskog, Norway.
Domenica CaponioDepartment of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, 1478, Lørenskog, Norway.
Evandro Fei FangDepartment of Clinical Molecular Biology, University of Oslo and Akershus University Hospital, 1478, Lørenskog, Norway.
Asgeir Kobro-FlatmoenKavli Institute for Systems Neuroscience, Norwegian University of Science and Technology (NTNU), 7491, Trondheim, Norway. asgeir.kobro-flatmoen@ntnu.no.

Funding

Civitan Norges Forskningsfond 281931Cure Alzheimer's Fund 282952Czech Republic-Norway KAPPA programme TO01000215Molecule AG/VITADAO 282942National Natural Science Foundation of China 81971327NordForsk Foundation 119986
6 · The paper itself

Abstract

In layer II of the entorhinal cortex, the principal neurons that project to the dentate gyrus and the CA3/2 hippocampal fields markedly express the large glycoprotein reelin (Re + ECLII neurons). In rodents, neurons located at the dorsal extreme of the EC, which border the rhinal fissure, express the highest levels, and the expression gradually decreases at levels successively further away from the rhinal fissure. Here, we test two predictions deducible from the hypothesis that reelin expression is strongly correlated with neuronal metabolic rate. Since the mitochondrial turnover rate serves as a proxy for energy expenditure, the mitophagy rate arguably also qualifies as such. Because messenger RNA of the canonical promitophagic BCL2 and adenovirus E1B 19-kDa-interacting protein 3 (Bnip3) is known to be highly expressed in the EC, we predicted that Bnip3 would be upregulated in Re + ECLII neurons, and that the degree of upregulation would strongly correlate with the expression level of reelin in these neurons. We confirm both predictions, supporting that the energy requirement of Re + ECLII neurons is generally high and that there is a systematic increase in metabolic rate as one moves successively closer to the rhinal fissure. Intriguingly, the systematic variation in energy requirement of the neurons that manifest the observed reelin gradient appears to be consonant with the level of spatial and temporal detail by which they encode information about the external environment.

Indexed as

Cell Adhesion Molecules, NeuronalEntorhinal CortexExtracellular Matrix ProteinsMembrane ProteinsNerve Tissue ProteinsNeuronsReelin ProteinSerine EndopeptidasesAnimalsMaleMiceMitochondrial ProteinsRatsRNA, MessengerBNip3 protein, mouseBNIP3 protein, ratCell Adhesion Molecules, NeuronalExtracellular Matrix ProteinsMembrane ProteinsMitochondrial ProteinsNerve Tissue ProteinsReelin ProteinReln protein, mouseReln protein, ratRNA, MessengerSerine EndopeptidasesMitophagyNeuroanatomical markersNeurometabolismSynaptic modulation

Identifiers

PMID38916724
PMCPMC11374853

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