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Article ; Online: Harnessing Pyroptosis for Cancer Immunotherapy.

Bourne, Christopher M / Taabazuing, Cornelius Y

2024 Volume 13, Issue 4

Abstract: Cancer immunotherapy is a novel pillar of cancer treatment that harnesses the immune system to fight tumors and generally results in robust antitumor immunity. Although immunotherapy has achieved remarkable clinical success for some patients, many ... ...

Abstract	Cancer immunotherapy is a novel pillar of cancer treatment that harnesses the immune system to fight tumors and generally results in robust antitumor immunity. Although immunotherapy has achieved remarkable clinical success for some patients, many patients do not respond, underscoring the need to develop new strategies to promote antitumor immunity. Pyroptosis is an immunostimulatory type of regulated cell death that activates the innate immune system. A hallmark of pyroptosis is the release of intracellular contents such as cytokines, alarmins, and chemokines that can stimulate adaptive immune activation. Recent studies suggest that pyroptosis promotes antitumor immunity. Here, we review the mechanisms by which pyroptosis can be induced and highlight new strategies to induce pyroptosis in cancer cells for antitumor defense. We discuss how pyroptosis modulates the tumor microenvironment to stimulate adaptive immunity and promote antitumor immunity. We also suggest research areas to focus on for continued development of pyroptosis as an anticancer treatment. Pyroptosis-based anticancer therapies offer a promising new avenue for treating immunologically 'cold' tumors.
MeSH term(s)	Humans ; Pyroptosis ; Immunotherapy ; Immunization ; Adaptive Immunity ; Neoplasms/therapy ; Tumor Microenvironment
Language	English
Publishing date	2024-02-16
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2661518-6
ISSN	2073-4409 ; 2073-4409
ISSN (online)	2073-4409
ISSN	2073-4409
DOI	10.3390/cells13040346
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Article ; Online: Dynamic Domain Links Substrate Binding and Catalysis in the Factor-Inhibiting-HIF-1.

Martin, Cristina B / Taabazuing, Cornelius Y / Knapp, Michael J

Biochemistry

2023 Volume 62, Issue 16, Page(s) 2442–2449

Abstract: The interplay between active-site chemistry and functionally relevant enzyme motions can provide useful insights into selective enzyme modulation. Modulation of the hypoxia-sensing function of factor-inhibiting-HIF-1 (FIH) enzyme is a potential ... ...

Abstract	The interplay between active-site chemistry and functionally relevant enzyme motions can provide useful insights into selective enzyme modulation. Modulation of the hypoxia-sensing function of factor-inhibiting-HIF-1 (FIH) enzyme is a potential therapeutic strategy in disease states such as ischemia and cancer. The hypoxia-sensing function of FIH relies in major part on the tight coupling of the first half of the catalytic mechanism which involves O
Language	English
Publishing date	2023-08-01
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.3c00231
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Article ; Online: The NLRP1 and CARD8 inflammasomes.

Taabazuing, Cornelius Y / Griswold, Andrew R / Bachovchin, Daniel A

Immunological reviews

2020 Volume 297, Issue 1, Page(s) 13–25

Abstract: Inflammasomes are multiprotein complexes that activate inflammatory cytokines and induce pyroptosis in response to intracellular danger-associated signals. NLRP1 and CARD8 are related germline-encoded pattern recognition receptors that form inflammasomes, ...

Abstract	Inflammasomes are multiprotein complexes that activate inflammatory cytokines and induce pyroptosis in response to intracellular danger-associated signals. NLRP1 and CARD8 are related germline-encoded pattern recognition receptors that form inflammasomes, but their activation mechanisms and biological purposes have not yet been fully established. Both NLRP1 and CARD8 undergo post-translational autoproteolysis to generate two non-covalently associated polypeptide chains. NLRP1 and CARD8 activators induce the proteasome-mediated destruction of the N-terminal fragment, liberating the C-terminal fragment to form an inflammasome. Here, we review the danger-associated stimuli that have been reported to activate NLRP1 and/or CARD8, including anthrax lethal toxin, Toxoplasma gondii, Shigella flexneri and the small molecule DPP8/9 inhibitor Val-boroPro, focusing on recent mechanistic insights and highlighting unresolved questions. In addition, we discuss the recently identified disease-associated mutations in NLRP1 and CARD8, the potential role that DPP9's protein structure plays in inflammasome regulation, and the emerging link between NLRP1 and metabolism. Finally, we summarize all of this latest research and consider the possible biological purposes of these enigmatic inflammasomes.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Apoptosis Regulatory Proteins/metabolism ; CARD Signaling Adaptor Proteins/metabolism ; Humans ; Inflammasomes/metabolism ; NLR Proteins ; Neoplasm Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Apoptosis Regulatory Proteins ; CARD Signaling Adaptor Proteins ; CARD8 protein, human ; Inflammasomes ; NLR Proteins ; NLRP1 protein, human ; Neoplasm Proteins
Language	English
Publishing date	2020-06-19
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	391796-4
ISSN	1600-065X ; 0105-2896
ISSN (online)	1600-065X
ISSN	0105-2896
DOI	10.1111/imr.12884
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Article ; Online: A practical guide to graduate school interviewing for historically excluded individuals.

Ransey, Elizabeth / Brookens, Shawna / Beasley, Heather K / Marshall, Andrea / Marlin, Bianca J / Rodriguez-Aliaga, Piere / Headley, Colwyn Ansel / Wanjalla, Celestine / Vazquez, Arnaldo Diaz / Murray, Sandra / Damo, Steven / Taabazuing, Cornelius Y / Hinton, Antentor

American journal of physiology. Heart and circulatory physiology

2023 Volume 324, Issue 6, Page(s) H786–H790

Language	English
Publishing date	2023-04-07
Publishing country	United States
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	603838-4
ISSN	1522-1539 ; 0363-6135
ISSN (online)	1522-1539
ISSN	0363-6135
DOI	10.1152/ajpheart.00123.2023
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Article: The tetrapeptide sequence of IL-1β regulates its recruitment and activation by inflammatory caspases.

Exconde, Patrick M / Hernandez-Chavez, Claudia / Bray, Mark B / Lopez, Jan L / Srivastava, Tamanna / Egan, Marisa S / Zhang, Jenna / Shin, Sunny / Discher, Bohdana M / Taabazuing, Cornelius Y

bioRxiv : the preprint server for biology

2023

Abstract: The mammalian innate immune system uses germline-encoded cytosolic pattern-recognition receptors (PRRs) to detect intracellular danger signals. At least six of these PRRs are known to form multiprotein complexes called inflammasomes which activate ... ...

Abstract	The mammalian innate immune system uses germline-encoded cytosolic pattern-recognition receptors (PRRs) to detect intracellular danger signals. At least six of these PRRs are known to form multiprotein complexes called inflammasomes which activate cysteine proteases known as caspases. Canonical inflammasomes recruit and activate caspase-1 (CASP1), which in turn cleaves and activates inflammatory cytokines such as IL-1β and IL-18, as well as the pore forming protein, gasdermin D (GSDMD), to induce pyroptotic cell death. In contrast, non-canonical inflammasomes, caspases-4/-5 (CASP4/5) in humans and caspase-11 (CASP11) in mice, are activated by intracellular LPS to cleave GSDMD, but their role in direct processing of inflammatory cytokines has not been established. Here we show that active CASP4/5 directly cleave IL-18 to generate the active species. Surprisingly, we also discovered that CASP4/5/11 cleave IL-1β at D27 to generate a 27 kDa fragment that is predicted to be inactive and cannot signal to the IL-1 receptor. Mechanistically, we discovered that the sequence identity of the P4-P1 tetrapeptide sequence adjacent to the caspase cleavage site (D116) regulates the recruitment and processing of IL-1β by inflammatory caspases to generate the bioactive species. Thus, we have identified new substrates of the non-canonical inflammasomes and reveal key mechanistic details regulating inflammation.
Language	English
Publishing date	2023-02-16
Publishing country	United States
Document type	Preprint
DOI	10.1101/2023.02.16.528859
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Article ; Online: The tetrapeptide sequence of IL-18 and IL-1β regulates their recruitment and activation by inflammatory caspases.

Exconde, Patrick M / Hernandez-Chavez, Claudia / Bourne, Christopher M / Richards, Rachel M / Bray, Mark B / Lopez, Jan L / Srivastava, Tamanna / Egan, Marisa S / Zhang, Jenna / Yoo, William / Shin, Sunny / Discher, Bohdana M / Taabazuing, Cornelius Y

Cell reports

2023 Volume 42, Issue 12, Page(s) 113581

Abstract: Inflammasomes are multiprotein signaling complexes that activate the innate immune system. Canonical inflammasomes recruit and activate caspase-1, which then cleaves and activates IL-1β and IL-18, as well as gasdermin D (GSDMD) to induce pyroptosis. In ... ...

Abstract	Inflammasomes are multiprotein signaling complexes that activate the innate immune system. Canonical inflammasomes recruit and activate caspase-1, which then cleaves and activates IL-1β and IL-18, as well as gasdermin D (GSDMD) to induce pyroptosis. In contrast, non-canonical inflammasomes, caspases-4/-5 (CASP4/5) in humans and caspase-11 (CASP11) in mice, are known to cleave GSDMD, but their role in direct processing of other substrates besides GSDMD has remained unknown. Here, we show that CASP4/5 but not CASP11 can directly cleave and activate IL-18. However, CASP4/5/11 can all cleave IL-1β to generate a 27-kDa fragment that deactivates IL-1β signaling. Mechanistically, we demonstrate that the sequence identity of the tetrapeptide sequence adjacent to the caspase cleavage site regulates IL-18 and IL-1β recruitment and activation. Altogether, we have identified new substrates of the non-canonical inflammasomes and reveal key mechanistic details regulating inflammation that may aid in developing new therapeutics for immune-related disorders.
MeSH term(s)	Caspases/genetics ; Caspases/immunology ; Interleukin-18/chemistry ; Interleukin-18/genetics ; Interleukin-18/immunology ; Interleukin-1beta/chemistry ; Interleukin-1beta/genetics ; Interleukin-1beta/immunology ; RAW 264.7 Cells ; HEK293 Cells ; HeLa Cells ; THP-1 Cells ; Humans ; Inflammasomes/immunology ; Signal Transduction/genetics ; Proteolysis ; Protein Binding ; Protein Multimerization ; Salmonella Infections/enzymology ; Salmonella Infections/immunology
Chemical Substances	Caspases (EC 3.4.22.-) ; Interleukin-18 ; Interleukin-1beta ; Inflammasomes
Language	English
Publishing date	2023-12-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2649101-1
ISSN	2211-1247 ; 2211-1247
ISSN (online)	2211-1247
ISSN	2211-1247
DOI	10.1016/j.celrep.2023.113581
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Article ; Online: Pyroptosis and Apoptosis Pathways Engage in Bidirectional Crosstalk in Monocytes and Macrophages.

Taabazuing, Cornelius Y / Okondo, Marian C / Bachovchin, Daniel A

Cell chemical biology

2017 Volume 24, Issue 4, Page(s) 507–514.e4

Abstract: Pyroptosis is a lytic form of programmed cell death mediated by the inflammatory caspase-1, -4, and -5. We recently discovered that small-molecule inhibitors of the serine peptidases DPP8 and DPP9 (DPP8/9) induce pro-caspase-1-dependent pyroptosis in ... ...

Abstract	Pyroptosis is a lytic form of programmed cell death mediated by the inflammatory caspase-1, -4, and -5. We recently discovered that small-molecule inhibitors of the serine peptidases DPP8 and DPP9 (DPP8/9) induce pro-caspase-1-dependent pyroptosis in monocytes and macrophages. Notably, DPP8/9 inhibitors, unlike microbial agents, absolutely require caspase-1 to induce cell death. Therefore, DPP8/9 inhibitors are useful probes to study caspase-1 in cells. Here, we show that, in the absence of the pyroptosis-mediating substrate gasdermin D (GSDMD), caspase-1 activates caspase-3 and -7 and induces apoptosis, demonstrating that GSDMD is the only caspase-1 substrate that induces pyroptosis. Conversely, we found that, during apoptosis, caspase-3/-7 specifically block pyroptosis by cleaving GSDMD at a distinct site from the inflammatory caspases that inactivates the protein. Overall, this work reveals bidirectional crosstalk between apoptosis and pyroptosis in monocytes and macrophages, further illuminating the complex interplay between cell death pathways in the innate immune system.
Language	English
Publishing date	2017-04-20
Publishing country	United States
Document type	Journal Article
ISSN	2451-9456
ISSN (online)	2451-9456
DOI	10.1016/j.chembiol.2017.03.009
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Article ; Online: A ubiquitin-independent proteasome pathway controls activation of the CARD8 inflammasome.

Hsiao, Jeffrey C / Neugroschl, Atara R / Chui, Ashley J / Taabazuing, Cornelius Y / Griswold, Andrew R / Wang, Qinghui / Huang, Hsin-Che / Orth-He, Elizabeth L / Ball, Daniel P / Hiotis, Giorgos / Bachovchin, Daniel A

The Journal of biological chemistry

2022 Volume 298, Issue 7, Page(s) 102032

Abstract: CARD8 is a pattern-recognition receptor that forms a caspase-1-activating inflammasome. CARD8 undergoes constitutive autoproteolysis, generating an N-terminal (NT) fragment with a disordered region and a ZU5 domain and a C-terminal (CT) fragment with UPA ...

Abstract	CARD8 is a pattern-recognition receptor that forms a caspase-1-activating inflammasome. CARD8 undergoes constitutive autoproteolysis, generating an N-terminal (NT) fragment with a disordered region and a ZU5 domain and a C-terminal (CT) fragment with UPA and CARD domains. Dipeptidyl peptidase 8 and dipeptidyl peptidase 9 inhibitors, including Val-boroPro, accelerate the degradation of the NT fragment via a poorly characterized proteasome-mediated pathway, thereby releasing the inflammatory CT fragment from autoinhibition. Here, we show that the core 20S proteasome, which degrades disordered and misfolded proteins independent of ubiquitin modification, controls activation of the CARD8 inflammasome. In unstressed cells, we discovered that the 20S proteasome degrades just the NT disordered region, leaving behind the folded ZU5, UPA, and CARD domains to act as an inhibitor of inflammasome assembly. However, in Val-boroPro-stressed cells, we show the 20S proteasome degrades the entire NT fragment, perhaps due to ZU5 domain unfolding, freeing the CT fragment from autoinhibition. Taken together, these results show that the susceptibility of the CARD8 NT domain to 20S proteasome-mediated degradation controls inflammasome activation.
MeSH term(s)	CARD Signaling Adaptor Proteins/metabolism ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/antagonists & inhibitors ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases/metabolism ; Humans ; Inflammasomes/metabolism ; Neoplasm Proteins/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Ubiquitins/metabolism
Chemical Substances	CARD Signaling Adaptor Proteins ; CARD8 protein, human ; Inflammasomes ; Neoplasm Proteins ; Ubiquitins ; Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (EC 3.4.14.-) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
Language	English
Publishing date	2022-05-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2022.102032
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Article ; Online: The tetrapeptide sequence of IL-18 and IL-1β regulates their recruitment and activation by inflammatory caspases

Patrick M. Exconde / Claudia Hernandez-Chavez / Christopher M. Bourne / Rachel M. Richards / Mark B. Bray / Jan L. Lopez / Tamanna Srivastava / Marisa S. Egan / Jenna Zhang / William Yoo / Sunny Shin / Bohdana M. Discher / Cornelius Y. Taabazuing

Cell Reports, Vol 42, Iss 12, Pp 113581- (2023)

2023

Abstract: Summary: Inflammasomes are multiprotein signaling complexes that activate the innate immune system. Canonical inflammasomes recruit and activate caspase-1, which then cleaves and activates IL-1β and IL-18, as well as gasdermin D (GSDMD) to induce ... ...

Abstract	Summary: Inflammasomes are multiprotein signaling complexes that activate the innate immune system. Canonical inflammasomes recruit and activate caspase-1, which then cleaves and activates IL-1β and IL-18, as well as gasdermin D (GSDMD) to induce pyroptosis. In contrast, non-canonical inflammasomes, caspases-4/-5 (CASP4/5) in humans and caspase-11 (CASP11) in mice, are known to cleave GSDMD, but their role in direct processing of other substrates besides GSDMD has remained unknown. Here, we show that CASP4/5 but not CASP11 can directly cleave and activate IL-18. However, CASP4/5/11 can all cleave IL-1β to generate a 27-kDa fragment that deactivates IL-1β signaling. Mechanistically, we demonstrate that the sequence identity of the tetrapeptide sequence adjacent to the caspase cleavage site regulates IL-18 and IL-1β recruitment and activation. Altogether, we have identified new substrates of the non-canonical inflammasomes and reveal key mechanistic details regulating inflammation that may aid in developing new therapeutics for immune-related disorders.
Keywords	CP: Immunology ; Biology (General) ; QH301-705.5
Language	English
Publishing date	2023-12-01T00:00:00Z
Publisher	Elsevier
Document type	Article ; Online
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Article ; Online: Increased Turnover at Limiting O2 Concentrations by the Thr(387) → Ala Variant of HIF-Prolyl Hydroxylase PHD2.

Pektas, Serap / Taabazuing, Cornelius Y / Knapp, Michael J

Biochemistry

2015 Volume 54, Issue 18, Page(s) 2851–2857

Abstract: PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1α. Identifying the active site contacts that determine the ... ...

Abstract	PHD2 is a 2-oxoglutarate, non-heme Fe(2+)-dependent oxygenase that senses O2 levels in human cells by hydroxylating two prolyl residues in the oxygen-dependent degradation domain (ODD) of HIF1α. Identifying the active site contacts that determine the rate of reaction at limiting O2 concentrations is crucial for understanding how this enzyme senses pO2 and may suggest methods for chemically altering hypoxia responses. A hydrogen bonding network extends from the Fe(II) cofactor through ordered waters to the Thr(387) residue in the second coordination sphere. Here we tested the impact of the side chain of Thr(387) on the reactivity of PHD2 toward O2 through a combination of point mutagenesis, steady state kinetic experiments and {FeNO}(7) EPR spectroscopy. The steady state kinetic parameters for Thr(387) → Asn were very similar to those of wild-type (WT) PHD2, but kcat and kcat/KM(O2) for Thr(387) → Ala were increased by roughly 15-fold. X-Band electron paramagnetic resonance spectroscopy of the {FeNO}(7) centers of the (Fe+NO+2OG) enzyme forms showed the presence of a more rhombic line shape in Thr(387) → Ala than in WT PHD2, indicating an altered conformation for bound gas in this variant. Here we show that the side chain of residue Thr(387) plays a significant role in determining the rate of turnover by PHD2 at low O2 concentrations.
MeSH term(s)	Alanine/genetics ; Electron Spin Resonance Spectroscopy ; Humans ; Hypoxia-Inducible Factor-Proline Dioxygenases/chemistry ; Hypoxia-Inducible Factor-Proline Dioxygenases/genetics ; Kinetics ; Oxygen/chemistry ; Point Mutation ; Recombinant Fusion Proteins/chemistry ; Threonine/genetics
Chemical Substances	Recombinant Fusion Proteins ; Threonine (2ZD004190S) ; EGLN1 protein, human (EC 1.14.11.2) ; Hypoxia-Inducible Factor-Proline Dioxygenases (EC 1.14.11.29) ; Alanine (OF5P57N2ZX) ; Oxygen (S88TT14065)
Language	English
Publishing date	2015-05-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi501540c
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