Impaired myoblast differentiation and muscle IGF-1 receptor signaling pathway activation after N-glycosylation inhibition.
Animals
Mice
Cell Differentiation
Glycosylation
Signal Transduction
Myoblasts
/ metabolism
Endoplasmic Reticulum Chaperone BiP
/ metabolism
Tunicamycin
/ pharmacology
Receptor, IGF Type 1
/ metabolism
Muscle, Skeletal
/ metabolism
Muscle Development
/ physiology
Cell Line
Mice, Transgenic
Endoplasmic Reticulum Stress
Insulin-Like Growth Factor I
/ metabolism
PMM2
IGF1R signaling pathway
congenital disorders of glycosylation
glycosylation
muscle atrophy
myoblast differentiation
Journal
FASEB journal : official publication of the Federation of American Societies for Experimental Biology
ISSN: 1530-6860
Titre abrégé: FASEB J
Pays: United States
ID NLM: 8804484
Informations de publication
Date de publication:
15 Jul 2024
15 Jul 2024
Historique:
revised:
08
06
2024
received:
27
01
2024
accepted:
24
06
2024
medline:
4
7
2024
pubmed:
4
7
2024
entrez:
4
7
2024
Statut:
ppublish
Résumé
The role of N-glycosylation in the myogenic process remains poorly understood. Here, we evaluated the impact of N-glycosylation inhibition by Tunicamycin (TUN) or by phosphomannomutase 2 (PMM2) gene knockdown, which encodes an enzyme essential for catalyzing an early step of the N-glycosylation pathway, on C2C12 myoblast differentiation. The effect of chronic treatment with TUN on tibialis anterior (TA) and extensor digitorum longus (EDL) muscles of WT and MLC/mIgf-1 transgenic mice, which overexpress muscle Igf-1Ea mRNA isoform, was also investigated. TUN-treated and PMM2 knockdown C2C12 cells showed reduced ConA, PHA-L, and AAL lectin binding and increased ER-stress-related gene expression (Chop and Hspa5 mRNAs and s/uXbp1 ratio) compared to controls. Myogenic markers (MyoD, myogenin, and Mrf4 mRNAs and MF20 protein) and myotube formation were reduced in both TUN-treated and PMM2 knockdown C2C12 cells. Body and TA weight of WT and MLC/mIgf-1 mice were not modified by TUN treatment, while lectin binding slightly decreased in the TA muscle of WT (ConA and AAL) and MLC/mIgf-1 (ConA) mice. The ER-stress-related gene expression did not change in the TA muscle of WT and MLC/mIgf-1 mice after TUN treatment. TUN treatment decreased myogenin mRNA and increased atrogen-1 mRNA, particularly in the TA muscle of WT mice. Finally, the IGF-1 production and IGF1R signaling pathways activation were reduced due to N-glycosylation inhibition in TA and EDL muscles. Decreased IGF1R expression was found in TUN-treated C2C12 myoblasts which was associated with lower IGF-1-induced IGF1R, AKT, and ERK1/2 phosphorylation compared to CTR cells. Chronic TUN-challenge models can help to elucidate the molecular mechanisms through which diseases associated with aberrant N-glycosylation, such as Congenital Disorders of Glycosylation (CDG), affect muscle and other tissue functions.
Identifiants
pubmed: 38963344
doi: 10.1096/fj.202400213RR
doi:
Substances chimiques
Endoplasmic Reticulum Chaperone BiP
0
Tunicamycin
11089-65-9
Receptor, IGF Type 1
EC 2.7.10.1
Hspa5 protein, mouse
0
Insulin-Like Growth Factor I
67763-96-6
Igf1r protein, mouse
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e23797Subventions
Organisme : Next Generation EU PRIN 2022
ID : 202255RLB4
Organisme : Next Generation EU PRIN 2022
ID : 2022LZARA3
Organisme : University of Urbino Carlo Bo
ID : 446/2020
Organisme : AFM-Telethon
ID : 23608
Organisme : Fondazione Roma
ID : 2022/2025
Informations de copyright
© 2024 The Author(s). The FASEB Journal published by Wiley Periodicals LLC on behalf of Federation of American Societies for Experimental Biology.
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