Dual inhibition of P38 MAPK and JNK pathways preserves stemness markers and alleviates premature activation of muscle stem cells during isolation.


Journal

Stem cell research & therapy
ISSN: 1757-6512
Titre abrégé: Stem Cell Res Ther
Pays: England
ID NLM: 101527581

Informations de publication

Date de publication:
21 Jun 2024
Historique:
received: 03 04 2024
accepted: 08 06 2024
medline: 21 6 2024
pubmed: 21 6 2024
entrez: 20 6 2024
Statut: epublish

Résumé

Adult skeletal muscle contains resident muscle stem cells (MuSC) with high myogenic and engraftment potentials, making them suitable for cell therapy and regenerative medicine approaches. However, purification process of MuSC remains a major hurdle to their use in the clinic. Indeed, muscle tissue enzymatic dissociation triggers a massive activation of stress signaling pathways, among which P38 and JNK MAPK, associated with a premature loss of MuSC quiescence. While the role of these pathways in the myogenic progression of MuSC is well established, the extent to which their dissociation-induced activation affects the functionality of these cells remains unexplored. We assessed the effect of P38 and JNK MAPK induction on stemness marker expression and MuSC activation state during isolation by pharmacological approaches. MuSC functionality was evaluated by in vitro assays and in vivo transplantation experiments. We performed a comparative analysis of the transcriptome of human MuSC purified with pharmacological inhibitors of P38 and JNK MAPK (SB202190 and SP600125, respectively) versus available RNAseq resources. We monitored PAX7 protein levels in murine MuSC during muscle dissociation and demonstrated a two-step decline partly dependent on P38 and JNK MAPK activities. We showed that simultaneous inhibition of these pathways throughout the MuSC isolation process preserves the expression of stemness markers and limits their premature activation, leading to improved survival and amplification in vitro as well as increased engraftment in vivo. Through a comparative RNAseq analysis of freshly isolated human MuSC, we provide evidence that our findings in murine MuSC could be relevant to human MuSC. Based on these findings, we implemented a purification strategy, significantly improving the recovery yields of human MuSC. Our study highlights the pharmacological limitation of P38 and JNK MAPK activities as a suitable strategy to qualitatively and quantitatively ameliorate human MuSC purification process, which could be of great interest for cell-based therapies.

Sections du résumé

BACKGROUND BACKGROUND
Adult skeletal muscle contains resident muscle stem cells (MuSC) with high myogenic and engraftment potentials, making them suitable for cell therapy and regenerative medicine approaches. However, purification process of MuSC remains a major hurdle to their use in the clinic. Indeed, muscle tissue enzymatic dissociation triggers a massive activation of stress signaling pathways, among which P38 and JNK MAPK, associated with a premature loss of MuSC quiescence. While the role of these pathways in the myogenic progression of MuSC is well established, the extent to which their dissociation-induced activation affects the functionality of these cells remains unexplored.
METHODS METHODS
We assessed the effect of P38 and JNK MAPK induction on stemness marker expression and MuSC activation state during isolation by pharmacological approaches. MuSC functionality was evaluated by in vitro assays and in vivo transplantation experiments. We performed a comparative analysis of the transcriptome of human MuSC purified with pharmacological inhibitors of P38 and JNK MAPK (SB202190 and SP600125, respectively) versus available RNAseq resources.
RESULTS RESULTS
We monitored PAX7 protein levels in murine MuSC during muscle dissociation and demonstrated a two-step decline partly dependent on P38 and JNK MAPK activities. We showed that simultaneous inhibition of these pathways throughout the MuSC isolation process preserves the expression of stemness markers and limits their premature activation, leading to improved survival and amplification in vitro as well as increased engraftment in vivo. Through a comparative RNAseq analysis of freshly isolated human MuSC, we provide evidence that our findings in murine MuSC could be relevant to human MuSC. Based on these findings, we implemented a purification strategy, significantly improving the recovery yields of human MuSC.
CONCLUSION CONCLUSIONS
Our study highlights the pharmacological limitation of P38 and JNK MAPK activities as a suitable strategy to qualitatively and quantitatively ameliorate human MuSC purification process, which could be of great interest for cell-based therapies.

Identifiants

pubmed: 38902774
doi: 10.1186/s13287-024-03795-0
pii: 10.1186/s13287-024-03795-0
doi:

Substances chimiques

p38 Mitogen-Activated Protein Kinases EC 2.7.11.24
Anthracenes 0
JNK Mitogen-Activated Protein Kinases EC 2.7.11.24

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

179

Subventions

Organisme : AFM-Téléthon
ID : Translamuscle PROJECT 19507
Organisme : Agence Nationale de la Recherche
ID : ANR-22-ASTR-0034 HydrACell
Organisme : Fondation des Gueules Cassées
ID : Dossier n°59

Informations de copyright

© 2024. The Author(s).

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Auteurs

Teoman Ozturk (T)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.

Julien Mignot (J)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.

Francesca Gattazzo (F)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.

Marianne Gervais (M)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.

Frédéric Relaix (F)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.
EnvA, IMRB, 94700, Maisons-Alfort, France.
AP-HP, Hopital Mondor, Service d'histologie, 94010, Creteil, France.

Hélène Rouard (H)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France.
AP-HP, Hopital Mondor, Service d'histologie, 94010, Creteil, France.

Nathalie Didier (N)

Univ Paris Est Creteil, INSERM, EFS, IMRB, 94010, Creteil, France. nathalie.didier@inserm.fr.

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