An Increase in Peroxiredoxin 6 Expression Induces Neurotoxic A1 Astrocytes in the Lumbar Spinal Cord of Amyotrophic Lateral Sclerosis Mice Model.
Mice
Humans
Animals
Amyotrophic Lateral Sclerosis
/ metabolism
Astrocytes
/ metabolism
Peroxiredoxin VI
/ genetics
Neurodegenerative Diseases
/ metabolism
Mice, Transgenic
Spinal Cord
/ metabolism
Cytokines
/ metabolism
Disease Models, Animal
Neurotoxicity Syndromes
/ metabolism
RNA, Messenger
/ metabolism
Superoxide Dismutase-1
/ genetics
Superoxide Dismutase
/ metabolism
A1 astrocyte
Amyotrophic lateral sclerosis
Complement 3
Inflammatory cytokine
Peroxiredoxin 6
Journal
Neurochemical research
ISSN: 1573-6903
Titre abrégé: Neurochem Res
Pays: United States
ID NLM: 7613461
Informations de publication
Date de publication:
Dec 2023
Dec 2023
Historique:
received:
25
01
2023
accepted:
25
07
2023
revised:
30
06
2023
medline:
23
10
2023
pubmed:
9
8
2023
entrez:
9
8
2023
Statut:
ppublish
Résumé
Amyotrophic lateral sclerosis (ALS) is a severe neurodegenerative disease with selective degeneration of motor neurons. It has been reported that an increase in the levels of inflammatory cytokines and glial cells such as reactive astrocytes is closely involved in the pathological progression of ALS. Recently, the levels of neuropathic cytotoxic (A1) astrocytes among reactive astrocytes have reportedly increased in the central nervous system of ALS mice, which induce motor neuron degeneration through the production of inflammatory cytokines and secretion of neuropathic factors. Hence, elucidating the induction mechanism of A1 astrocytes in ALS is important to understand the mechanism of disease progression in ALS. In this study, we observed that the expression of peroxiredoxin 6 (PRDX6), a member of the peroxiredoxin family, was markedly upregulated in astrocytes of the lumbar spinal cord of SOD1
Identifiants
pubmed: 37556038
doi: 10.1007/s11064-023-04003-w
pii: 10.1007/s11064-023-04003-w
doi:
Substances chimiques
Peroxiredoxin VI
EC 1.11.1.15
Cytokines
0
RNA, Messenger
0
Superoxide Dismutase-1
EC 1.15.1.1
Superoxide Dismutase
EC 1.15.1.1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
3571-3584Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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