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  1. Article ; Online: Neutrophil-specific depletion of gasdermin D does not protect against murine sepsis.

    Liu, Fei / Ghimire, Laxman / Balasubramanian, Arumugam / Hsu, Alan Y / Zhang, Zhaoran / Yu, Hongbo / Ma, Fengxia / Luo, Hongbo R

    Blood

    2022  Volume 141, Issue 5, Page(s) 550–554

    MeSH term(s) Humans ; Animals ; Mice ; Neutrophils/metabolism ; Gasdermins ; Apoptosis Regulatory Proteins/metabolism ; Intracellular Signaling Peptides and Proteins ; Sepsis/prevention & control
    Chemical Substances Gasdermins ; Apoptosis Regulatory Proteins ; Intracellular Signaling Peptides and Proteins
    Language English
    Publishing date 2022-11-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.2022016931
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Gasdermin E dictates inflammatory responses by controlling the mode of neutrophil death.

    Ma, Fengxia / Ghimire, Laxman / Ren, Qian / Fan, Yuping / Chen, Tong / Balasubramanian, Arumugam / Hsu, Alan / Liu, Fei / Yu, Hongbo / Xie, Xuemei / Xu, Rong / Luo, Hongbo R

    Nature communications

    2024  Volume 15, Issue 1, Page(s) 386

    Abstract: Both lytic and apoptotic cell death remove senescent and damaged cells in living organisms. However, they elicit contrasting pro- and anti-inflammatory responses, respectively. The precise cellular mechanism that governs the choice between these two ... ...

    Abstract Both lytic and apoptotic cell death remove senescent and damaged cells in living organisms. However, they elicit contrasting pro- and anti-inflammatory responses, respectively. The precise cellular mechanism that governs the choice between these two modes of death remains incompletely understood. Here we identify Gasdermin E (GSDME) as a master switch for neutrophil lytic pyroptotic death. The tightly regulated GSDME cleavage and activation in aging neutrophils are mediated by proteinase-3 and caspase-3, leading to pyroptosis. GSDME deficiency does not alter neutrophil overall survival rate; instead, it specifically precludes pyroptosis and skews neutrophil death towards apoptosis, thereby attenuating inflammatory responses due to augmented efferocytosis of apoptotic neutrophils by macrophages. In a clinically relevant acid-aspiration-induced lung injury model, neutrophil-specific deletion of GSDME reduces pulmonary inflammation, facilitates inflammation resolution, and alleviates lung injury. Thus, by controlling the mode of neutrophil death, GSDME dictates host inflammatory outcomes, providing a potential therapeutic target for infectious and inflammatory diseases.
    MeSH term(s) Humans ; Gasdermins ; Lung Injury ; Neutrophils ; Apoptosis ; Pyroptosis
    Chemical Substances Gasdermins
    Language English
    Publishing date 2024-01-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-44669-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Gasdermin E dictates inflammatory responses by controlling the mode of neutrophil death

    Fengxia Ma / Laxman Ghimire / Qian Ren / Yuping Fan / Tong Chen / Arumugam Balasubramanian / Alan Hsu / Fei Liu / Hongbo Yu / Xuemei Xie / Rong Xu / Hongbo R. Luo

    Nature Communications, Vol 15, Iss 1, Pp 1-

    2024  Volume 18

    Abstract: Abstract Both lytic and apoptotic cell death remove senescent and damaged cells in living organisms. However, they elicit contrasting pro- and anti-inflammatory responses, respectively. The precise cellular mechanism that governs the choice between these ...

    Abstract Abstract Both lytic and apoptotic cell death remove senescent and damaged cells in living organisms. However, they elicit contrasting pro- and anti-inflammatory responses, respectively. The precise cellular mechanism that governs the choice between these two modes of death remains incompletely understood. Here we identify Gasdermin E (GSDME) as a master switch for neutrophil lytic pyroptotic death. The tightly regulated GSDME cleavage and activation in aging neutrophils are mediated by proteinase-3 and caspase-3, leading to pyroptosis. GSDME deficiency does not alter neutrophil overall survival rate; instead, it specifically precludes pyroptosis and skews neutrophil death towards apoptosis, thereby attenuating inflammatory responses due to augmented efferocytosis of apoptotic neutrophils by macrophages. In a clinically relevant acid-aspiration-induced lung injury model, neutrophil-specific deletion of GSDME reduces pulmonary inflammation, facilitates inflammation resolution, and alleviates lung injury. Thus, by controlling the mode of neutrophil death, GSDME dictates host inflammatory outcomes, providing a potential therapeutic target for infectious and inflammatory diseases.
    Keywords Science ; Q
    Subject code 610
    Language English
    Publishing date 2024-01-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: The palmitoylation of gasdermin D directs its membrane translocation and pore formation during pyroptosis.

    Balasubramanian, Arumugam / Hsu, Alan Y / Ghimire, Laxman / Tahir, Muhammad / Devant, Pascal / Fontana, Pietro / Du, Gang / Liu, Xing / Fabin, Dang / Kambara, Hiroto / Xie, Xuemei / Liu, Fei / Hasegawa, Tomoya / Xu, Rong / Yu, Hongbo / Chen, Mei / Kolakowski, Steven / Trauger, Sunia / Larsen, Martin Røssel /
    Wei, Wenyi / Wu, Hao / Kagan, Jonathan C / Lieberman, Judy / Luo, Hongbo R

    Science immunology

    2024  Volume 9, Issue 94, Page(s) eadn1452

    Abstract: Plasma membrane perforation elicited by caspase cleavage of the gasdermin D (GSDMD) N-terminal domain (GSDMD-NT) triggers pyroptosis. The mechanisms underlying GSDMD membrane translocation and pore formation are not fully understood. Here, using a ... ...

    Abstract Plasma membrane perforation elicited by caspase cleavage of the gasdermin D (GSDMD) N-terminal domain (GSDMD-NT) triggers pyroptosis. The mechanisms underlying GSDMD membrane translocation and pore formation are not fully understood. Here, using a proteomic approach, we identified fatty acid synthase (FASN) as a GSDMD-binding partner. S-palmitoylation of GSDMD at Cys
    MeSH term(s) Animals ; Humans ; Mice ; Gasdermins ; Lipoylation ; Proteomics ; Pyroptosis
    Chemical Substances Gasdermins ; GSDMD protein, human ; Gsdmd protein, mouse
    Language English
    Publishing date 2024-04-12
    Publishing country United States
    Document type Journal Article
    ISSN 2470-9468
    ISSN (online) 2470-9468
    DOI 10.1126/sciimmunol.adn1452
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Palmitoylation of gasdermin D directs its membrane translocation and pore formation in pyroptosis.

    Balasubramanian, Arumugam / Ghimire, Laxman / Hsu, Alan Y / Kambara, Hiroto / Liu, Xing / Hasegawa, Tomoya / Xu, Rong / Tahir, Muhammad / Yu, Hongbo / Lieberman, Judy / Luo, Hongbo R

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Gasdermin D (GSDMD)-mediated macrophage pyroptosis plays a critical role in inflammation and host defense. Plasma membrane perforation elicited by caspase-cleaved GSDMD N-terminal domain (GSDMD-NT) triggers membrane rupture and subsequent pyroptotic cell ...

    Abstract Gasdermin D (GSDMD)-mediated macrophage pyroptosis plays a critical role in inflammation and host defense. Plasma membrane perforation elicited by caspase-cleaved GSDMD N-terminal domain (GSDMD-NT) triggers membrane rupture and subsequent pyroptotic cell death, resulting in release of pro-inflammatory IL-1β and IL-18. However, the biological processes leading to its membrane translocation and pore formation are not fully understood. Here, using a proteomics approach, we identified fatty acid synthase (FASN) as a GSDMD-binding partner and demonstrated that post-translational palmitoylation of GSDMD at Cys191/Cys192 (human/mouse) led to membrane translocation of GSDMD-NT but not full-length GSDMD. GSDMD lipidation, mediated by palmitoyl acyltransferases ZDHHC5/9 and facilitated by LPS-induced reactive oxygen species (ROS), was essential for GSDMD pore-forming activity and pyroptosis. Inhibition of GSDMD palmitoylation with palmitate analog 2-bromopalmitate or a cell permeable GSDMD-specific competing peptide suppressed pyroptosis and IL-1β release in macrophages, mitigated organ damage, and extended the survival of septic mice. Collectively, we establish GSDMD-NT palmitoylation as a key regulatory mechanism controlling GSDMD membrane localization and activation, providing a novel target for modulating immune activity in infectious and inflammatory diseases.
    One sentence summary: LPS-induced palmitoylation at Cys191/Cys192 is required for GSDMD membrane translocation and its pore-forming activity in macrophages.
    Language English
    Publishing date 2023-02-21
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.02.21.529402
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: A dual regulator of neutrophil recruitment.

    Luo, Hongbo R

    Blood

    2014  Volume 123, Issue 13, Page(s) 1983–1985

    Abstract: In this issue of Blood, Boespflug et al report that activating transcription factor 3 (ATF3), a member of the ATF/cyclic AMP response element-binding (ATF/CREB) family of transcription factors, plays a crucial role in regulating neutrophil recruitment ... ...

    Abstract In this issue of Blood, Boespflug et al report that activating transcription factor 3 (ATF3), a member of the ATF/cyclic AMP response element-binding (ATF/CREB) family of transcription factors, plays a crucial role in regulating neutrophil recruitment during lung inflammation.
    MeSH term(s) Activating Transcription Factor 3/physiology ; Animals ; Immune System Diseases/genetics ; Leukocyte Disorders/genetics
    Chemical Substances Activating Transcription Factor 3 ; Atf3 protein, mouse
    Language English
    Publishing date 2014-03-26
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2014-02-554774
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  7. Article ; Online: αDβ2 as a novel target of experimental polymicrobial sepsis.

    Koutsogiannaki, Sophia / Hou, Lifei / Okuno, Toshiaki / Shibamura-Fujiogi, Miho / Luo, Hongbo R / Yuki, Koichi

    Frontiers in immunology

    2022  Volume 13, Page(s) 1059996

    Abstract: Since sepsis was defined three decades ago, it has been a target of intensive study. However, there is no specific sepsis treatment available, with its high mortality and morbidity. αDβ2 (CD11d/CD18) is one of the four β2 integrin members. Its role in ... ...

    Abstract Since sepsis was defined three decades ago, it has been a target of intensive study. However, there is no specific sepsis treatment available, with its high mortality and morbidity. αDβ2 (CD11d/CD18) is one of the four β2 integrin members. Its role in sepsis has been limitedly studied. Using an experimental polymicrobial sepsis model, we found that the deficiency of αDβ2 was associated with less lung injury and better outcome, which was in sharp contrast to other β2 integrin member αLβ2 (CD11a/CD18), and αMβ2 (CD11b/CD18). This phenotype was supported by a reduction of bacterial loads in αDβ2 knockout mice. Further analysis showed that the deficiency of αDβ2 led to a reduction of neutrophil cell death as well as an increase in neutrophil phagocytosis in both murine and human systems. Our data showed a unique role of αDβ2 among the β2 integrin members, which would serve as a potential target to improve the outcome of sepsis.
    MeSH term(s) Humans ; Animals ; Mice ; CD18 Antigens/genetics ; Sepsis ; Neutrophils ; Macrophage-1 Antigen ; Lung Injury ; Lymphocyte Function-Associated Antigen-1 ; Mice, Knockout
    Chemical Substances CD18 Antigens ; Macrophage-1 Antigen ; Lymphocyte Function-Associated Antigen-1
    Language English
    Publishing date 2022-11-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2022.1059996
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  8. Article ; Online: Neutrophil Lifespan Extension with CLON-G and an In Vitro Spontaneous Death Assay.

    Fan, Yuping / Teng, Yan / Liu, Fu Tong / Ma, Fengxia / Hsu, Alan Y / Feng, Sizhou / Luo, Hongbo R

    Journal of visualized experiments : JoVE

    2023  , Issue 195

    Abstract: The average lifespan of a neutrophil is less than 24 h, which limits basic research on neutrophils and the application of neutrophil studies. Our previous research indicated that multiple pathways could mediate the spontaneous death of neutrophils. A ... ...

    Abstract The average lifespan of a neutrophil is less than 24 h, which limits basic research on neutrophils and the application of neutrophil studies. Our previous research indicated that multiple pathways could mediate the spontaneous death of neutrophils. A cocktail was developed by simultaneously targeting these pathways, caspases-lysosomal membrane permeabilization-oxidant-necroptosis inhibition plus granulocyte colony-stimulating factor (CLON-G), which prolonged the neutrophil lifespan to greater than 5 days without significantly compromising the neutrophil function. Concurrently, a reliable and stable protocol for assessing and evaluating neutrophil death was also developed. In this work, we show that CLON-G can prolong the neutrophil lifespan in vitro to more than 5 days, and we exhibit the lengthening of the neutrophil lifespan with FACS and confocal fluorescence microscopy. This report introduces procedures for the preparation of CLON-G and showcases an in vitro spontaneous death assay of neutrophils, which can be used for the study of neutrophils and for subsequently interrogating neutrophil death, thus providing a reliable resource for the neutrophil community.
    MeSH term(s) Neutrophils/metabolism ; Granulocyte-Macrophage Colony-Stimulating Factor/metabolism ; Longevity ; Granulocyte Colony-Stimulating Factor/metabolism ; Granulocyte Colony-Stimulating Factor/pharmacology ; Caspases/metabolism
    Chemical Substances Granulocyte-Macrophage Colony-Stimulating Factor (83869-56-1) ; Granulocyte Colony-Stimulating Factor (143011-72-7) ; Caspases (EC 3.4.22.-)
    Language English
    Publishing date 2023-05-12
    Publishing country United States
    Document type Journal Article ; Video-Audio Media ; Research Support, Non-U.S. Gov't
    ZDB-ID 2259946-0
    ISSN 1940-087X ; 1940-087X
    ISSN (online) 1940-087X
    ISSN 1940-087X
    DOI 10.3791/65132
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: ROS-dependent S-palmitoylation activates cleaved and intact gasdermin D.

    Du, Gang / Healy, Liam B / David, Liron / Walker, Caitlin / El-Baba, Tarick J / Lutomski, Corinne A / Goh, Byoungsook / Gu, Bowen / Pi, Xiong / Devant, Pascal / Fontana, Pietro / Dong, Ying / Ma, Xiyu / Miao, Rui / Balasubramanian, Arumugam / Puthenveetil, Robbins / Banerjee, Anirban / Luo, Hongbo R / Kagan, Jonathan C /
    Oh, Sungwhan F / Robinson, Carol V / Lieberman, Judy / Wu, Hao

    Nature

    2024  

    Abstract: Gasdermin D (GSDMD) is the common effector for cytokine secretion and pyroptosis downstream of inflammasome activation and was previously shown to form large transmembrane pores upon cleavage by inflammatory caspases to generate the GSDMD N-terminal ... ...

    Abstract Gasdermin D (GSDMD) is the common effector for cytokine secretion and pyroptosis downstream of inflammasome activation and was previously shown to form large transmembrane pores upon cleavage by inflammatory caspases to generate the GSDMD N-terminal domain (GSDMD-NT)
    Language English
    Publishing date 2024-04-10
    Publishing country England
    Document type Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/s41586-024-07373-5
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  10. Article ; Online: NLRP3 is essential for neutrophil polarization and chemotaxis in response to leukotriene B4 gradient.

    Van Bruggen, Stijn / Jarrot, Pierre-André / Thomas, Eline / Sheehy, Casey E / Silva, Camila M S / Hsu, Alan Y / Cunin, Pierre / Nigrovic, Peter A / Gomes, Edgar R / Luo, Hongbo R / Waterman, Clare M / Wagner, Denisa D

    Proceedings of the National Academy of Sciences of the United States of America

    2023  Volume 120, Issue 35, Page(s) e2303814120

    Abstract: Neutrophil recruitment to sites of infection and inflammation is an essential process in the early innate immune response. Upon activation, a subset of neutrophils rapidly assembles the multiprotein complex known as the NLRP3 inflammasome. The NLRP3 ... ...

    Abstract Neutrophil recruitment to sites of infection and inflammation is an essential process in the early innate immune response. Upon activation, a subset of neutrophils rapidly assembles the multiprotein complex known as the NLRP3 inflammasome. The NLRP3 inflammasome forms at the microtubule organizing center, which promotes the formation of interleukin (IL)-1β and IL-18, essential cytokines in the immune response. We recently showed that mice deficient in NLRP3 (NLRP3
    MeSH term(s) Animals ; Mice ; Chemotaxis ; Inflammasomes ; Leukotriene B4/metabolism ; Neutrophils ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism
    Chemical Substances Inflammasomes ; Leukotriene B4 (1HGW4DR56D) ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nlrp3 protein, mouse
    Language English
    Publishing date 2023-08-21
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.2303814120
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