Caspase-7 mediates caspase-1-induced apoptosis independently of Bid.
Animals
Apoptosis
/ physiology
BH3 Interacting Domain Death Agonist Protein
/ metabolism
Caspase 1
/ metabolism
Caspase 3
/ metabolism
Caspase 7
/ metabolism
Cell Line
Immunity, Innate
Inflammasomes
/ metabolism
Intracellular Signaling Peptides and Proteins
/ metabolism
Metabolic Networks and Pathways
Mice
Mice, Inbred C57BL
Phosphate-Binding Proteins
/ metabolism
Pyroptosis
/ physiology
apoptosis
caspase-1
caspase-7
inflammasome
pyroptosis
Journal
Microbiology and immunology
ISSN: 1348-0421
Titre abrégé: Microbiol Immunol
Pays: Australia
ID NLM: 7703966
Informations de publication
Date de publication:
Feb 2020
Feb 2020
Historique:
received:
09
09
2019
revised:
16
10
2019
accepted:
01
11
2019
pubmed:
7
11
2019
medline:
15
5
2020
entrez:
6
11
2019
Statut:
ppublish
Résumé
Inflammasomes are innate immune mechanisms that activate caspase-1 in response to a variety of stimuli, including Salmonella infection. Active caspase-1 has a potential to induce two different types of cell death, depending on the expression of the pyroptosis mediator gasdermin D (GSDMD); following caspase-1 activation, GSDMD-sufficient and GSDMD-null/low cells undergo pyroptosis and apoptosis, respectively. Although Bid, a caspase-1 substrate, plays a critical role in caspase-1 induction of apoptosis in GSDMD-null/low cells, an additional mechanism that mediates this cell death independently of Bid has also been suggested. This study investigated the Bid-independent pathway of caspase-1-induced apoptosis. Caspase-1 has been reported to process caspase-6 and caspase-7. Silencing of caspase-7, but not caspase-6, significantly reduced the activation of caspase-3 induced by caspase-1, which was activated by chemical dimerization, in GSDMD/Bid-deficient cells. CRISPR/Cas9-mediated depletion of caspase-7 had the same effect on the caspase-3 activation. Moreover, in the absence of GSDMD and Bid, caspase-7 depletion reduced apoptosis induced by caspase-1 activation. Caspase-7 was activated following caspase-1 activation independently of caspase-3, suggesting that caspase-7 acts downstream of caspase-1 and upstream of caspase-3. Salmonella induced the activation of caspase-3 in GSDMD-deficient macrophages, which relied partly on Bid and largely on caspase-1. The caspase-3 activation and apoptotic morphological changes seen in Salmonella-infected GSDMD/Bid-deficient macrophages were attenuated by caspase-7 knockdown. These results suggest that in addition to Bid, caspase-7 can also mediate caspase-1-induced apoptosis and provide mechanistic insights into inflammasome-associated cell death that is one major effector mechanism of inflammasomes.
Identifiants
pubmed: 31687791
doi: 10.1111/1348-0421.12756
doi:
Substances chimiques
BH3 Interacting Domain Death Agonist Protein
0
Gsdmd protein, mouse
0
Inflammasomes
0
Intracellular Signaling Peptides and Proteins
0
Phosphate-Binding Proteins
0
Caspase 3
EC 3.4.22.-
Caspase 7
EC 3.4.22.-
Caspase 1
EC 3.4.22.36
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
143-152Subventions
Organisme : Japan Society for the Promotion of Science
ID : 18K07106
Organisme : Japan Society for the Promotion of Science
ID : 26110002
Organisme : Institute for Frontier Science Initiative
Informations de copyright
© 2019 The Societies and John Wiley & Sons Australia, Ltd.
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