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Myocarditis
Published in Mary N. Sheppard, Practical Cardiovascular Pathology, 2022
IL (interleukin)-1 is a pivotal proinflammatory cytokine amplifying the innate immune response. Upstream of IL-1 is the inflammasome, a cytosolic molecular structure composed of an adaptor protein, procaspase-1, and a sensor molecule. The best-characterized inflammasome has a sensor molecule called NLRP3 (nucleotide-binding domain and leucine-rich repeat pyrin domain containing-3). Biological treatments that block the IL-1 pathway, including the IL-Ra (IL-1 receptor antagonist) anakinra, the fully human IgG1 anti–IL-1β monoclonal antibody, canakinumab, and colchicine are potential candidates to treat myocarditis.
SARS-CoV-2 Morphology, Genomic Organisation and Lifecycle
Published in Srijan Goswami, Chiranjeeb Dey, COVID-19 and SARS-CoV-2, 2022
Srijan Goswami, Ushmita Gupta Bakshi
Envelope proteins or E-proteins are the smallest of all major structural proteins present on SARS-CoV-2. The major functions of the envelope protein are as follows:First, it helps in the assembly and release of viruses from host cells.Second, during the process of viral replication, it is largely located at the regions of intracellular trafficking, for example, near the endoplasmic reticulum and Golgi apparatus.It functions as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport and plays a role in the induction of apoptosis (UniProtKB – P59637, n.d.).It is known to activate the host NLR family pyrin domain containing 3 (NLRP3) inflammasome, leading to interleukin-1 beta (IL-1β) overproduction.
(Poly)phenols in Exercise Performance and Recovery
Published in James N. Cobley, Gareth W. Davison, Oxidative Eustress in Exercise Physiology, 2022
Many (poly)phenols have been shown to attenuate inflammation. Part of their anti-inflammatory effects is mediated by interfering with key pro-inflammatory signalling cascades (Kobayashi et al., 2016). The mechanisms for such effects are still being unravelled but could involve activation of Nrf2 (Kobayashi et al., 2016; Zhang and Tsao, 2016). Indeed, by activating Nrf2 many (poly)phenols have been shown to inhibit the NLR family pyrin domain containing 3 (NLPR3) inflammasome that governs pro-inflammatory signalling following stress (Zhang and Tsao, 2016). Disrupting this pathway decreases nuclear factor kappa-light-chain-enhancer of activated B cells (NF-κB) expression and subsequent pro-inflammatory signalling, which might limit damage to skeletal muscle tissue and accelerate regeneration following exercise (Pizza et al., 2005). Nonetheless, these mechanisms are yet to be validated in humans, and some have questioned whether dampening the inflammatory response could delay rather than accelerate muscle regeneration (Lundberg and Howatson, 2018).
Platelet-derived microparticles stimulated by anti-β2GPI/β2GPI complexes induce pyroptosis of endothelial cells in antiphospholipid syndrome
Published in Platelets, 2023
Longjiang Di, Caijun Zha, Yanhong Liu
Pyroptosis has been increasingly referred to in the context of disease development mechanisms. Pyroptosis, also known as cellular inflammatory necrosis, is different from other forms of cell death such as apoptosis [19]. Pyroptosis is cell death via NLR family pyrin domain containing 3 (NLRP3) inflammasome activation, which manifests as swelling, lysis and perforation of cell membranes [20]. Specifically, activation of inflammasomes induces the cleavage of gasdermin D (GSDMD), which releases the N-terminal structural domain (GSDMD-N) and causes perforation of the cell membrane [21]. Inflammatory factors such as interleukin (IL)-1β and IL-18 can be released after pyroptosis [22]. NLRP3 inflammatory vesicles generate GSDMD, pro-IL-1β and pro-IL-18 by activating nuclear factor (NF)-κB, and induce GSDMD cleavage, IL-1β and IL-18 maturation by activating Caspase-1, leading to pyroptosis [23,24]. During inflammation, IC can induce increased NLRP3 in platelets. Recent studies have found that increased Caspase-1 protein expression in MPs directly activates endothelial cell pyroptosis [25]. However, the relationship between IC-PMPs and endothelial cell pyroptosis remains unclear.
Microtubule affinity regulating kinase 4 promoted activation of the NLRP3 inflammasome-mediated pyroptosis in periodontitis
Published in Journal of Oral Microbiology, 2022
Lulu Wang, Wenchen Pu, Chun Wang, Lang Lei, Houxuan Li
Host immune cells are equipped with ample pattern recognition receptors on the cell membrane and in the cytosol to detect the invasion of the microbe and their products. The NLR family pyrin domain containing 3 (NLRP3) inflammasome is one important sensor of bacterial invasion in the cytosol of immune cells. After ligation with its ligand, NLRP3 recruits its adaptor, apoptosis-associated speck-like protein (ASC), to form the NLRP3-ASC complex, which sequentially cleaves pro-caspase-1 into mature caspase-1, and caspase-1 contributes to the maturation of the inflammatory cytokines interleukin-1β (IL-1β) as well as IL-18; moreover, the assembly of the NLRP3-ASC-caspase 1 complex may further cleave the Gasdermin family protein, leading to cell membrane pore formation, leakage of cellular contents and eventual occurrence of cell death, a type of regulated cell death called pyroptosis [2]. Therefore, the NLRP3 inflammasome acts as a critical sensor in the innate immune program, tightly regulating inflammatory responses and cell death [3]. The NLRP3 inflammasome plays a crucial role in the pathogenesis and development of periodontal disease [4–7]. The suppression of the NLRP3 inflammasome enables alleviation of periodontitis in a mouse model [8]; meanwhile, NLRP3 knockout reduces periodontal bone loss during P. gingivalis infection in mice [1].
Prebiotic oligofructose protects against high-fat diet-induced obesity by changing the gut microbiota, intestinal mucus production, glycosylation and secretion
Published in Gut Microbes, 2022
Paola Paone, Francesco Suriano, Ching Jian, Katri Korpela, Nathalie M. Delzenne, Matthias Van Hul, Anne Salonen, Patrice D. Cani
After being synthesized and glycosylated in the goblet cells, Muc2 is packed inside the secretory vesicles that are then excreted by exocytosis, forming the protective mucus layer. Among the proteins involved in this process, we found a significant increase in expression of the bactericidal protein resistin-like beta (Retnlb), in the jejunum and ileum and an increase in the autophagic protein Atg5 in the cecum and colon and Atg7 only in the colon. We also measured the expression of the NOD‐like receptor family pyrin domain containing 6 (Nlrp6), which promote autophagy-dependent mucus secretion from goblet cells,37,38 and we found a significant increase in the cecum (Figure 5a-d). Finally, Fc gamma-binding protein (Fcgbp), involved in the stabilization of the Muc2 mucin networks of the inner firm mucus layer,39,40 was not different between the groups (Figure 5e). All the data from the mRNA expression described in the colon are schematized in Figure 6.