Physiopathological changes of ferritin mRNA density and distribution in hippocampal astrocytes in the mouse brain.


Journal

Journal of neurochemistry
ISSN: 1471-4159
Titre abrégé: J Neurochem
Pays: England
ID NLM: 2985190R

Informations de publication

Date de publication:
03 2023
Historique:
revised: 30 11 2022
received: 18 07 2022
accepted: 05 12 2022
medline: 30 3 2023
pubmed: 24 12 2022
entrez: 23 12 2022
Statut: ppublish

Résumé

Astrocytes are thought to play a crucial role in brain iron homeostasis. How they accomplish this regulation in vivo is unclear. In a recent transcriptomic analysis, we showed that polysomal Ftl1 and Fth1 mRNAs, encoding the ferritin light (Ftl) and heavy (Fth) chains that assemble into ferritin, a critical complex for iron storage and reduction, are enriched in perisynaptic astrocytic processes as compared to astrocytic soma. These data suggested that ferritin translation plays a specific role at the perisynaptic astrocytic interface and is tighly regulated by local translation. Here, we used our recently described AstroDot 3D in situ methodology to study the density and localization of ferritin mRNAs in astrocytes in the hippocampus in three different contexts in which local or systemic iron overload has been documented: aging, the hepcidin knock-out mouse model of hemochromatosis and the APP/PS1dE9 mouse model of Alzheimer's disease (AD). Our results showed that in wild type mice, Fth1 mRNA density was higher than Ftl1 and that both mRNAs were mostly distributed in astrocyte fine processes. Aging and absence of hepcidin caused an increased Fth1/Ftl1 ratio in astrocytes and in the case of aging, led to a redistribution of Fth1 mRNAs in astrocytic fine processes. In contrast, in AD mice, we observed a lower Fth1/Ftl1 ratio. Fth1 mRNAs became more somatic and Ftl1 mRNAs redistributed in large processes of astrocytes proximal to Amyloid beta (Aß) deposits. Hence, we propose that regulation of ferritin mRNA density and distribution in astrocytes contribute to iron homeostasis in physiology and pathophysiology.

Identifiants

pubmed: 36562685
doi: 10.1111/jnc.15747
doi:

Substances chimiques

Ferritins 9007-73-2
Hepcidins 0
Amyloid beta-Peptides 0
RNA, Messenger 0
Iron E1UOL152H7

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

847-857

Informations de copyright

© 2022 The Authors. Journal of Neurochemistry published by John Wiley & Sons Ltd on behalf of International Society for Neurochemistry.

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Auteurs

Romain Tortuyaux (R)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.
Intensive Care Unit, CHU Lille, Lille, France.

Katia Avila-Gutierrez (K)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.

Marc Oudart (M)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.

Noémie Mazaré (N)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.

Philippe Mailly (P)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.

Jean-Christophe Deschemin (JC)

CNRS, INSERM, Institut Cochin, Université Paris Cité, Paris, France.

Sophie Vaulont (S)

CNRS, INSERM, Institut Cochin, Université Paris Cité, Paris, France.

Carole Escartin (C)

Université Paris-Saclay, CEA, CNRS, MIRCen, Laboratoire des Maladies Neurodégénératives, Fontenay-aux-Roses, France.

Martine Cohen-Salmon (M)

Center for Interdisciplinary Research in Biology (CIRB), Collège de France, CNRS, INSERM, Université PSL, Paris, France.

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