Calpain-1 weakens the nuclear envelope and promotes the release of neutrophil extracellular traps.
Calpain-1
Nesprin-1
Neutrophil extracellular traps (NETs)
Nuclear envelope break down
Journal
Cell communication and signaling : CCS
ISSN: 1478-811X
Titre abrégé: Cell Commun Signal
Pays: England
ID NLM: 101170464
Informations de publication
Date de publication:
09 Sep 2024
09 Sep 2024
Historique:
received:
09
02
2024
accepted:
09
08
2024
medline:
10
9
2024
pubmed:
10
9
2024
entrez:
9
9
2024
Statut:
epublish
Résumé
The inducers of neutrophil extracellular trap (NET) formation are heterogeneous and consequently, there is no specific pathway or signature molecule indispensable for NET formation. But certain events such as histone modification, chromatin decondensation, nuclear envelope breakdown, and NET release are ubiquitous. During NET formation, neutrophils drastically rearrange their cytoplasmic, granular and nuclear content. Yet, the exact mechanism for decoding each step during NET formation still remains elusive. Here, we investigated the mechanism of nuclear envelope breakdown during NET formation. Immunofluorescence microscopic evaluation revealed a gradual disintegration of outer nuclear membrane protein nesprin-1 and alterations in nuclear morphology during NET formation. MALDI-TOF analysis of NETs that had been generated by various inducers detected the accumulation of nesprin-1 fragments. This suggests that nesprin-1 degradation occurs before NET release. In the presence of a calpain-1, inhibitor nesprin-1 degradation was decreased in calcium driven NET formation. Microscopic evaluation confirmed that the disintegration of the lamin B receptor (LBR) and the collapse of the actin cytoskeleton occurs in early and later phases of NET release, respectively. We conclude that the calpain-1 degrades nesprin-1, orchestrates the weakening of the nuclear membrane, contributes to LBR disintegration, and promoting DNA release and finally, NETs formation.
Identifiants
pubmed: 39252008
doi: 10.1186/s12964-024-01785-6
pii: 10.1186/s12964-024-01785-6
doi:
Substances chimiques
Calpain
EC 3.4.22.-
Lamin B Receptor
0
Nerve Tissue Proteins
0
SYNE1 protein, human
0
Nuclear Proteins
0
Receptors, Cytoplasmic and Nuclear
0
CAPN1 protein, human
EC 3.4.22.52
Calcium
SY7Q814VUP
Cytoskeletal Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
435Informations de copyright
© 2024. The Author(s).
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