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  1. Article ; Online: Protocol for a semi-quantitative approach to identify protein S-palmitoylation in cultured cells by acyl biotin exchange assay.

    Leishman, Stuart / Aljadeed, Najd M / Anand, Paras K

    STAR protocols

    2024  Volume 5, Issue 2, Page(s) 103054

    Abstract: Palmitoylation is a post-translational lipid modification in which palmitic acid is conjugated predominantly to cysteine residues of target proteins, allowing them to tether to cell membranes. Here, we describe a protocol to perform a stepwise acyl ... ...

    Abstract Palmitoylation is a post-translational lipid modification in which palmitic acid is conjugated predominantly to cysteine residues of target proteins, allowing them to tether to cell membranes. Here, we describe a protocol to perform a stepwise acyl biotin exchange assay to identify protein S-palmitoylation. We describe steps for initial blocking of free thiols in protein lysates, subsequent replacement of thioester-linked palmitate groups with a biotin tag for affinity enrichment, and identification of palmitoylated proteins by SDS-PAGE. For complete details on the use and execution of this protocol, please refer to Leishman et al.
    Language English
    Publishing date 2024-05-04
    Publishing country United States
    Document type Journal Article
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2024.103054
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Lipids, inflammasomes, metabolism, and disease.

    Anand, Paras K

    Immunological reviews

    2020  Volume 297, Issue 1, Page(s) 108–122

    Abstract: Inflammasomes are multi-protein complexes that regulate the cleavage of cysteine protease caspase-1, secretion of inflammatory cytokines, and induction of inflammatory cell death, pyroptosis. Several members of the nod-like receptor family assemble ... ...

    Abstract Inflammasomes are multi-protein complexes that regulate the cleavage of cysteine protease caspase-1, secretion of inflammatory cytokines, and induction of inflammatory cell death, pyroptosis. Several members of the nod-like receptor family assemble inflammasome in response to specific ligands. An exception to this is the NLRP3 inflammasome which is activated by structurally diverse entities. Recent studies have suggested that NLRP3 might be a sensor of cellular homeostasis, and any perturbation in distinct metabolic pathways results in the activation of this inflammasome. Lipid metabolism is exceedingly important in maintaining cellular homeostasis, and it is recognized that cells and tissues undergo extensive lipid remodeling during activation and disease. Some lipids are involved in instigating chronic inflammatory diseases, and new studies have highlighted critical upstream roles for lipids, particularly cholesterol, in regulating inflammasome activation implying key functions for inflammasomes in diseases with defective lipid metabolism. The focus of this review is to highlight how lipids regulate inflammasome activation and how this leads to the progression of inflammatory diseases. The key roles of cholesterol metabolism in the activation of inflammasomes have been comprehensively discussed. Besides, the roles of oxysterols, fatty acids, phospholipids, and lipid second messengers are also summarized in the context of inflammasomes. The overriding theme is that lipid metabolism has numerous but complex functions in inflammasome activation. A detailed understanding of this area will help us develop therapeutic interventions for diseases where dysregulated lipid metabolism is the underlying cause.
    MeSH term(s) Caspase 1 ; Cholesterol ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Pyroptosis
    Chemical Substances Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Cholesterol (97C5T2UQ7J) ; Caspase 1 (EC 3.4.22.36)
    Language English
    Publishing date 2020-06-20
    Publishing country England
    Document type Journal Article ; 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.12891
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  3. Article ; Online: Adapt(ed) to repair - T

    Lukens, John R / Anand, Paras K

    Nature immunology

    2020  Volume 21, Issue 6, Page(s) 597–599

    MeSH term(s) Humans ; Infections ; Th1 Cells ; Th2 Cells ; Urinary Bladder
    Keywords covid19
    Language English
    Publishing date 2020-05-18
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2016987-5
    ISSN 1529-2916 ; 1529-2908
    ISSN (online) 1529-2916
    ISSN 1529-2908
    DOI 10.1038/s41590-020-0689-2
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  4. Article ; Online: The NLRP3 inflammasome: regulation by metabolic signals.

    Olona, Antoni / Leishman, Stuart / Anand, Paras K

    Trends in immunology

    2022  Volume 43, Issue 12, Page(s) 978–989

    Abstract: Macrophages undergo profound metabolic reprogramming upon sensing infectious and sterile stimuli. This metabolic shift supports and regulates essential innate immune functions, including activation of the NLRP3 inflammasome. Within distinct metabolic ... ...

    Abstract Macrophages undergo profound metabolic reprogramming upon sensing infectious and sterile stimuli. This metabolic shift supports and regulates essential innate immune functions, including activation of the NLRP3 inflammasome. Within distinct metabolic networks, key enzymes play pivotal roles to control flux restraining detrimental inflammasome signaling. However, depending on the metabolic cues, specific enzymes and metabolites result in inflammasome activation outcomes which contrast other metabolic steps in the pathway. We posit that understanding which metabolic steps commit to discrete inflammasome fates will broaden our understanding of metabolic checkpoints to maintain homeostasis and offer better therapeutic options in human disease.
    MeSH term(s) Humans ; Inflammasomes/metabolism ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Macrophages ; Signal Transduction ; Metabolic Networks and Pathways
    Chemical Substances Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein
    Language English
    Publishing date 2022-11-09
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2036831-8
    ISSN 1471-4981 ; 1471-4906
    ISSN (online) 1471-4981
    ISSN 1471-4906
    DOI 10.1016/j.it.2022.10.003
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  5. Article ; Online: Right place, right time

    Claire Hamilton / Paras K. Anand

    F1000Research, Vol

    localisation and assembly of the NLRP3 inflammasome [version 1; peer review: 3 approved]

    2019  Volume 8

    Abstract: The NLRP3 inflammasome is a multimeric protein complex that cleaves caspase-1 and the pro-inflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. Dysregulated NLRP3 inflammasome signalling is linked to several chronic inflammatory and autoimmune ... ...

    Abstract The NLRP3 inflammasome is a multimeric protein complex that cleaves caspase-1 and the pro-inflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. Dysregulated NLRP3 inflammasome signalling is linked to several chronic inflammatory and autoimmune conditions; thus, understanding the activation mechanisms of the NLRP3 inflammasome is essential. Studies over the past few years have implicated vital roles for distinct intracellular organelles in both the localisation and assembly of the NLRP3 inflammasome. However, conflicting reports exist. Prior to its activation, NLRP3 has been shown to be resident in the endoplasmic reticulum (ER) and cytosol, although, upon activation, the NLRP3 inflammasome has been shown to assemble in the cytosol, mitochondria, and mitochondria-associated ER membranes by different reports. Finally, very recent work has suggested that NLRP3 may be localised on or adjacent to the Golgi apparatus and that release of mediators from this organelle may contribute to inflammasome assembly. Therefore, NLRP3 may be strategically placed on or in close proximity to these subcellular compartments to both sense danger signals originating from these organelles and use the compartment as a scaffold to assemble the complex. Understanding where and when NLRP3 inflammasome assembly occurs may help identify potential targets for treatment of NLRP3-related disorders.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2019-05-01T00:00:00Z
    Publisher F1000 Research Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Right place, right time: localisation and assembly of the NLRP3 inflammasome.

    Hamilton, Claire / Anand, Paras K

    F1000Research

    2019  Volume 8

    Abstract: The NLRP3 inflammasome is a multimeric protein complex that cleaves caspase-1 and the pro-inflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. Dysregulated NLRP3 inflammasome signalling is linked to several chronic inflammatory and autoimmune ... ...

    Abstract The NLRP3 inflammasome is a multimeric protein complex that cleaves caspase-1 and the pro-inflammatory cytokines interleukin 1 beta (IL-1β) and IL-18. Dysregulated NLRP3 inflammasome signalling is linked to several chronic inflammatory and autoimmune conditions; thus, understanding the activation mechanisms of the NLRP3 inflammasome is essential. Studies over the past few years have implicated vital roles for distinct intracellular organelles in both the localisation and assembly of the NLRP3 inflammasome. However, conflicting reports exist. Prior to its activation, NLRP3 has been shown to be resident in the endoplasmic reticulum (ER) and cytosol, although, upon activation, the NLRP3 inflammasome has been shown to assemble in the cytosol, mitochondria, and mitochondria-associated ER membranes by different reports. Finally, very recent work has suggested that NLRP3 may be localised on or adjacent to the Golgi apparatus and that release of mediators from this organelle may contribute to inflammasome assembly. Therefore, NLRP3 may be strategically placed on or in close proximity to these subcellular compartments to both sense danger signals originating from these organelles and use the compartment as a scaffold to assemble the complex. Understanding where and when NLRP3 inflammasome assembly occurs may help identify potential targets for treatment of NLRP3-related disorders.
    MeSH term(s) Caspase 1 ; Inflammasomes/physiology ; Mitochondria ; NLR Family, Pyrin Domain-Containing 3 Protein/physiology ; Protein Multimerization ; Signal Transduction
    Chemical Substances Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Caspase 1 (EC 3.4.22.36)
    Language English
    Publishing date 2019-05-17
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2699932-8
    ISSN 2046-1402 ; 2046-1402
    ISSN (online) 2046-1402
    ISSN 2046-1402
    DOI 10.12688/f1000research.18557.1
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  7. Article ; Online: Editorial: Role of NOD-Like Receptors in Infectious and Immunological Diseases.

    Lupfer, Christopher R / Anand, Paras K / Qi, Xiaopeng / Zaki, Hasan

    Frontiers in immunology

    2020  Volume 11, Page(s) 923

    MeSH term(s) Humans ; Immune System Diseases/immunology ; Immunity, Innate ; Infections/immunology ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein/immunology ; NLR Proteins/classification ; NLR Proteins/immunology
    Chemical Substances Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; NLR Proteins
    Language English
    Publishing date 2020-05-19
    Publishing country Switzerland
    Document type Editorial ; Introductory Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2020.00923
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  8. Article ; Online: NLRP3 Inflammasome Priming and Activation Are Regulated by a Phosphatidylinositol-Dependent Mechanism.

    Hamilton, Claire / Olona, Antoni / Leishman, Stuart / MacDonald-Ramsahai, Kelly / Cockcroft, Shamshad / Larrouy-Maumus, Gerald / Anand, Paras K

    ImmunoHorizons

    2022  Volume 6, Issue 8, Page(s) 642–659

    Abstract: Imbalance in lipid homeostasis is associated with discrepancies in immune signaling and is tightly linked to metabolic disorders. The diverse ways in which lipids impact immune signaling, however, remain ambiguous. The phospholipid phosphatidylinositol ( ... ...

    Abstract Imbalance in lipid homeostasis is associated with discrepancies in immune signaling and is tightly linked to metabolic disorders. The diverse ways in which lipids impact immune signaling, however, remain ambiguous. The phospholipid phosphatidylinositol (PI), which is implicated in numerous immune disorders, is chiefly defined by its phosphorylation status. By contrast, the significance of the two fatty acid chains attached to the PI remains unknown. In this study, by using a mass spectrometry-based assay, we demonstrate a role for PI acyl group chains in regulating both the priming and activation steps of the NOD-like receptor family pyrin domain-containing 3 (NLRP3) inflammasome in mouse macrophages. In response to NLRP3 stimuli, cells deficient in ABC transporter ATP Binding Cassette Subfamily B Member 1 (ABCB1), which effluxes lipid derivatives, revealed defective inflammasome activation. Mechanistically,
    MeSH term(s) Adaptor Proteins, Signal Transducing ; Animals ; Inflammasomes/metabolism ; Macrophages ; Mice ; NLR Family, Pyrin Domain-Containing 3 Protein/metabolism ; Phosphatidylinositols/metabolism ; Signal Transduction
    Chemical Substances Adaptor Proteins, Signal Transducing ; Inflammasomes ; NLR Family, Pyrin Domain-Containing 3 Protein ; Nlrp3 protein, mouse ; Phosphatidylinositols
    Language English
    Publishing date 2022-08-29
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2573-7732
    ISSN (online) 2573-7732
    DOI 10.4049/immunohorizons.2200058
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  9. Article ; Online: Integrating Inflammasome Signaling in Sexually Transmitted Infections.

    Lupfer, Christopher / Anand, Paras K

    Trends in immunology

    2016  Volume 37, Issue 10, Page(s) 703–714

    Abstract: Inflammasomes are cytosolic multiprotein platforms with pivotal roles in infectious diseases. Activation of inflammasomes results in proinflammatory cytokine signaling and pyroptosis. Sexually transmitted infections (STIs) are a major health problem ... ...

    Abstract Inflammasomes are cytosolic multiprotein platforms with pivotal roles in infectious diseases. Activation of inflammasomes results in proinflammatory cytokine signaling and pyroptosis. Sexually transmitted infections (STIs) are a major health problem worldwide, yet few studies have probed the impact of inflammasome signaling during these infections. Due to the dearth of appropriate infection models, our current understanding of inflammasomes in STIs is mostly drawn from results obtained in vitro, from distant infection sites, or from related microbial strains that are not sexually transmitted. Understanding how inflammasomes influence the outcome of STIs may lead to the development of novel and effective strategies to control disease and prevent transmission. Here we discuss and highlight the recent progress in this field.
    MeSH term(s) Animals ; Apoptosis ; Cytokines/metabolism ; Disease Models, Animal ; Humans ; Infection Control ; Inflammasomes/metabolism ; Inflammation Mediators/metabolism ; Sexually Transmitted Diseases/immunology ; Sexually Transmitted Diseases/transmission ; Signal Transduction
    Chemical Substances Cytokines ; Inflammasomes ; Inflammation Mediators
    Language English
    Publishing date 2016-08-31
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2036831-8
    ISSN 1471-4981 ; 1471-4906
    ISSN (online) 1471-4981
    ISSN 1471-4906
    DOI 10.1016/j.it.2016.08.004
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  10. Article ; Online: Exosomal membrane molecules are potent immune response modulators.

    Anand, Paras K

    Communicative & integrative biology

    2010  Volume 3, Issue 5, Page(s) 405–408

    Abstract: Exosomes are endosome-derived vesicles (40-100 nm) formed during the formation of multi-vesicular bodies (MVBs). Occasionally, the MVBs fuse with the plasma membrane releasing their intra-luminal vesicles into the extracellular media, which are then ... ...

    Abstract Exosomes are endosome-derived vesicles (40-100 nm) formed during the formation of multi-vesicular bodies (MVBs). Occasionally, the MVBs fuse with the plasma membrane releasing their intra-luminal vesicles into the extracellular media, which are then known as exosomes. Different cell types such as B-cells, dendritic cells, platelets, reticulocytes and macrophages can release exosomes and current research in this area is more focused towards exosomes released by antigen-presenting cells. Exosomes have recently been shown to be immunomodulatory and the mechanism of immune response initiation by them is beginning to emerge. Besides molecules present inside the lumen of exosomes, it has been suggested that certain exosomal membrane molecules can interact with their surface receptors on the target cells thereby inducing an immunomodulatory response. In this review, Hsp70 and galectin-5, two immunogenic molecules present on exosomal membrane, are discussed in detail for initiating this response.
    Language English
    Publishing date 2010-10-21
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2451097-X
    ISSN 1942-0889 ; 1942-0889
    ISSN (online) 1942-0889
    ISSN 1942-0889
    DOI 10.4161/cib.3.5.12474
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