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The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Differential Requirement for Caspase-1 Autoproteolysis in Pathogen-Induced Cell Death and Cytokine Processing

Open access
Broz, Petr, von Moltke, Jakob, Jones, Jonathan W., Vance, Russell E., Monack, Denise M.·2010·Cell Host & Microbe

Abstract

Summary Activation of the cysteine protease Caspase-1 is a key event in the innate immune response to infections. Synthesized as a pro-protein, Caspase-1 undergoes autoproteolysis within multi-protein complexes called inflammasomes. Activated Caspase-1 is required for proteolytic processing and release of the cytokines interleukin-1β and interleukin-18, and can also cause rapid macrophage cell death. We show that macrophage cell death and cytokine maturation in response to infection with diverse bacterial pathogens can be separated genetically and that two distinct inflammasome complexes mediate these events. Inflammasomes containing the signaling adaptor Asc form a single large ‘focus’ in which Caspase-1 undergoes autoproteolysis and processes IL-1β/IL-18. In contrast, Asc-independent inflammasomes activate Caspase-1 without autoproteolysis and do not form any large structures in the cytosol. Caspase-1 mutants unable to undergo autoproteolysis promoted rapid cell death, but processed IL-1β/18 inefficiently. Our results suggest the formation of spatially and functionally distinct inflammasomes complexes in response to bacterial pathogens.

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Metadata

Authors
Broz, P., von Moltke, J., Jones, J. W., Vance, R. E., & Monack, D. M.
Venue
Cell Host & Microbe
Publisher
Elsevier BV
Published
2010-12
Volume
8
Issue
6
Pages
471-483
ISSN
1931-3128 (ISSN-L)
OpenAlex
W2118800225
Cited by
622
References
9
FWCI
13.94
Type
journal article
Language
en
Open access
bronze

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Broz, P., von Moltke, J., Jones, J. W., Vance, R. E., & Monack, D. M. (2010). Differential Requirement for Caspase-1 Autoproteolysis in Pathogen-Induced Cell Death and Cytokine Processing. Cell Host & Microbe. https://doi.org/10.1016/j.chom.2010.11.007

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