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How many NOD like receptors in Human?

How many NOD like receptors in Human?


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This is pretty specific question maybe. Anybody have an estimate? For Toll Like Receptors there are something like 10…

http://www.jbc.org/content/276/4/2551.long

I'm only finding NOD1 and NOD2 => only 2?


This review 22 proteins in the NOD like human repetoire. It was published in 2013…

The families are broken down into 9 general groups according to their domain composition in Figure 1 from that review. Most of them are not named "NOD".


1. Zhu S, Ding S, Wang P, Wei Z, Pan W, Palm NW, et al. Nlrp9b inflammasome restricts rotavirus infection in intestinal epithelial cells. Nature. (2017) 546:667�. doi: 10.1038/nature22967

2. Kofoed EM, Vance RE. Innate immune recognition of bacterial ligands by NAIPs determines inflammasome specificity. Nature. (2011) 477:592𠄵. doi: 10.1038/nature10394

3. Zhao Y, Yang J, Shi J, Gong YN, Lu Q, Xu H, et al. The NLRC4 inflammasome receptors for bacterial flagellin and type III secretion apparatus. Nature. (2011) 477:596�. doi: 10.1038/nature10510

4. Kayagaki N, Warming S, Lamkanfi M, Vande Walle L, Louie S, Dong J, et al. Non-canonical inflammasome activation targets caspase-11. Nature. (2011) 479:117�. doi: 10.1038/nature10558

Keywords: NLRP3, inflammasome, inflammation, NOD-like receptor, infection, immunological diseases

Citation: Lupfer CR, Anand PK, Qi X and Zaki H (2020) Editorial: Role of NOD-Like Receptors in Infectious and Immunological Diseases. Front. Immunol. 11:923. doi: 10.3389/fimmu.2020.00923

Received: 11 April 2020 Accepted: 21 April 2020
Published: 19 May 2020.

Edited and reviewed by: Francesca Granucci, University of Milano-Bicocca, Italy

Copyright © 2020 Lupfer, Anand, Qi and Zaki. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.


TRAF1 Signaling in Human Health and Disease

Tumor necrosis factor receptor (TNFR) associated factor 1 (TRAF1) is a signaling adaptor first identified as part of the TNFR2 signaling complex. TRAF1 plays a key role in pro-survival signaling downstream of TNFR superfamily members such as TNFR2, LMP1, 4-1BB, and CD40. Recent studies have uncovered another role for TRAF1, independent of its role in TNFR superfamily signaling, in negatively regulating Toll-like receptor and Nod-like receptor signaling, through sequestering the linear ubiquitin assembly complex, LUBAC. TRAF1 has diverse roles in human disease. TRAF1 is overexpressed in many B cell related cancers and single nucleotide polymorphisms (SNPs) in TRAF1 have been linked to non-Hodgkin's lymphoma. Genome wide association studies have identified an association between SNPs in the 5' untranslated region of the TRAF1 gene with increased incidence and severity of rheumatoid arthritis and other rheumatic diseases. The loss of TRAF1 from chronically stimulated CD8 T cells results in desensitization of the 4-1BB signaling pathway, thereby contributing to T cell exhaustion during chronic infection. These apparently opposing roles of TRAF1 as both a positive and negative regulator of immune signaling have led to some confusion in the literature. Here we review the role of TRAF1 as a positive and negative regulator in different signaling pathways. Then we discuss the role of TRAF1 in human disease, attempting to reconcile seemingly contradictory roles based on current knowledge of TRAF1 signaling and biology. We also discuss avenues for future research to further clarify the impact of TRAF1 in human disease.

Keywords: TNFR superfamily autoimmunity cancer chronic viral infection linear ubiquitination signaling toll-like receptor.

Figures

TRAF1 and TRAF 2 proteins…

TRAF1 and TRAF 2 proteins in TNFRI signaling. (A) Schematic of TRAF1 and…

Role of TRAF1 and linear ubiquitination downstream of LMP1 and TLR4. (A) TRAF1…


The Nod-like receptor (NLR) family: a tale of similarities and differences

Innate immunity represents an important system with a variety of vital processes at the core of many diseases. In recent years, the central role of the Nod-like receptor (NLR) protein family became increasingly appreciated in innate immune responses. NLRs are classified as part of the signal transduction ATPases with numerous domains (STAND) clade within the AAA+ ATPase family. They typically feature an N-terminal effector domain, a central nucleotide-binding domain (NACHT) and a C-terminal ligand-binding region that is composed of several leucine-rich repeats (LRRs). NLRs are believed to initiate or regulate host defense pathways through formation of signaling platforms that subsequently trigger the activation of inflammatory caspases and NF-kB. Despite their fundamental role in orchestrating key pathways in innate immunity, their mode of action in molecular terms remains largely unknown. Here we present the first comprehensive sequence and structure modeling analysis of NLR proteins, revealing that NLRs possess a domain architecture similar to the apoptotic initiator protein Apaf-1. Apaf-1 performs its cellular function by the formation of a heptameric platform, dubbed apoptosome, ultimately triggering the controlled demise of the affected cell. The mechanism of apoptosome formation by Apaf-1 potentially offers insight into the activation mechanisms of NLR proteins. Multiple sequence alignment analysis and homology modeling revealed Apaf-1-like structural features in most members of the NLR family, suggesting a similar biochemical behaviour in catalytic activity and oligomerization. Evolutionary tree comparisons substantiate the conservation of characteristic functional regions within the NLR family and are in good agreement with domain distributions found in distinct NLRs. Importantly, the analysis of LRR domains reveals surprisingly low conservation levels among putative ligand-binding motifs. The same is true for the effector domains exhibiting distinct interfaces ensuring specific interactions with downstream target proteins. All together these factors suggest specific biological functions for individual NLRs.

Conflict of interest statement

Competing Interests: The authors have declared that no competing interests exist.

Figures

Figure 1. Multiple sequence alignment of NLR…

Figure 1. Multiple sequence alignment of NLR NACHT-WH-SH domains and the Apaf-1 NACHT-WH-SH domain.

A Apaf-1 structure and domain…

A Apaf-1 structure and domain organization. Apaf-1ΔWD40 (PDB id: 1z6t) is shown in…

Figure 3. Model of the NOD2 nucleotide-binding…

Figure 3. Model of the NOD2 nucleotide-binding site with an ADP molecule and conserved sequence…

A NLR oligomerization interface: Apaf-1…

A NLR oligomerization interface: Apaf-1 oligomer modeled on the basis of the NtrC1…

A Multiple sequence alignment of…

A Multiple sequence alignment of NLR and Apaf-1 CARD domains. Acidic key residues…

A Homology model of NOD2 LRR domain based on the ribonuclease inhibitor (pdb…


Genetic Alterations of TRAF Proteins in Human Cancers

The tumor necrosis factor receptor (TNF-R)-associated factor (TRAF) family of cytoplasmic adaptor proteins regulate the signal transduction pathways of a variety of receptors, including the TNF-R superfamily, Toll-like receptors (TLRs), NOD-like receptors (NLRs), RIG-I-like receptors (RLRs), and cytokine receptors. TRAF-dependent signaling pathways participate in a diverse array of important cellular processes, including the survival, proliferation, differentiation, and activation of different cell types. Many of these TRAF-dependent signaling pathways have been implicated in cancer pathogenesis. Here we analyze the current evidence of genetic alterations of TRAF molecules available from The Cancer Genome Atlas (TCGA) and the Catalog of Somatic Mutations in Cancer (COSMIC) as well as the published literature, including copy number variations and mutation landscape of TRAFs in various human cancers. Such analyses reveal that both gain- and loss-of-function genetic alterations of different TRAF proteins are commonly present in a number of human cancers. These include pancreatic cancer, meningioma, breast cancer, prostate cancer, lung cancer, liver cancer, head and neck cancer, stomach cancer, colon cancer, bladder cancer, uterine cancer, melanoma, sarcoma, and B cell malignancies, among others. Furthermore, we summarize the key in vivo and in vitro evidence that demonstrates the causal roles of genetic alterations of TRAF proteins in tumorigenesis within different cell types and organs. Taken together, the information presented in this review provides a rationale for the development of therapeutic strategies to manipulate TRAF proteins or TRAF-dependent signaling pathways in different human cancers by precision medicine.

Keywords: MAPK NF-κB TRAFs cancer oncogenes tumor suppressor genes.

Figures

Landscape of genetic alterations of…

Landscape of genetic alterations of the TRAF family in human cancers. (A) Representative…

Overview of recurrent mutations of…

Overview of recurrent mutations of the TRAF family in human cancers. Recurrent mutations…

Map of recurrent TRAF mutations…

Map of recurrent TRAF mutations of human cancers on the TRAF proteins. The…

Combined genetic alterations of the…

Combined genetic alterations of the TRAF family in human cancers. Representative results of…

Causal roles and signaling mechanisms…

Causal roles and signaling mechanisms of TRAF proteins in skin carcinogenesis. Evidence of…

Complex protective and pathogenic roles…

Complex protective and pathogenic roles as well as signaling mechanisms of TRAF proteins…


Innate immune receptors in platelets and platelet-leukocyte interactions

Laboratory of Immunology, Infectious Diseases and Obesity, Department of Parasitology, Microbiology and Immunology, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Eugenio Damaceno Hottz, Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Brazil.

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunology, Infectious Diseases and Obesity, Department of Parasitology, Microbiology and Immunology, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Juiz de Fora, Brazil

Eugenio Damaceno Hottz, Laboratory of Immunothrombosis, Department of Biochemistry, Institute of Biological Sciences, Federal University of Juiz de Fora, Brazil.

Abstract

Platelets are chief cells in hemostasis. Apart from their hemostatic roles, platelets are major inflammatory effector cells that can influence both innate and adaptive immune responses. Activated platelets have thromboinflammatory functions linking hemostatic and immune responses in several physiological and pathological conditions. Among many ways in which platelets exert these functions, platelet expression of pattern recognition receptors (PRRs), including TLR, Nod-like receptor, and C-type lectin receptor families, plays major roles in sensing and responding to pathogen-associated or damage-associated molecular patterns (PAMPs and DAMPs, respectively). In this review, an increasing body of evidence is compiled showing the participation of platelet innate immune receptors, including PRRs, in infectious diseases, sterile inflammation, and cancer. How platelet recognition of endogenous DAMPs participates in sterile inflammatory diseases and thrombosis is discussed. In addition, platelet recognition of both PAMPs and DAMPs initiates platelet-mediated inflammation and vascular thrombosis in infectious diseases, including viral, bacterial, and parasite infections. The study also focuses on the involvement of innate immune receptors in platelet activation during cancer, and their contribution to tumor microenvironment development and metastasis. Finally, how innate immune receptors participate in platelet communication with leukocytes, modulating leukocyte-mediated inflammation and immune functions, is highlighted. These cell communication processes, including platelet-induced release of neutrophil extracellular traps, platelet Ag presentation to T-cells and platelet modulation of monocyte cytokine secretion are discussed in the context of infectious and sterile diseases of major concern in human health, including cardiovascular diseases, dengue, HIV infection, sepsis, and cancer.


The DNA Damage Response (DDR)

It is vital for every cell to protect the integrity of all the encoded information it hosts and enable the accurate transfer of genetic material during cell division. Given that all human cells are exposed to a multitude of genotoxic insults, endogenous and exogenous (Jackson and Bartek, 2009), a highly conserved and advanced DNA recognition and repair network, against a variety of DNA lesions is in operation. The DDR is a complex network of molecular mechanisms, which identifies the genetic damage and induces biochemical pathways which cause cell cycle arrest (so-called control points, checkpoints), promotes repair of lesions in the genetic material, or, alternatively, proceeds to the activation of anti-tumor barriers, apoptosis and senescence (Halazonetis et al., 2008 Gorgoulis and Halazonetis, 2010 Evangelou et al., 2013 Velimezi et al., 2013).

Among all types of genetic damage, the double-stranded breaks (DSBs) constitute the greatest threat to the cell. The presence of DSBs results in the DDR activation having as a key effector the tumour-suppressor protein p53 (Rodier et al., 2007). DSBs can be induced by various stimuli such as ionizing radiation, activated oncogenes, or defective telomeres and are very harmful, even fatal, for the cell. Early activation of DDR in human precancerous lesions highlights the importance of this network in preventing cancer progression (Gorgoulis et al., 2005 Bartkova et al., 2006 Halazonetis et al., 2008 Gorgoulis and Halazonetis, 2010). However, continuous activation of DDR constitutes a sustained “pressure” eventually leading to the mutation of the TP53 gene and loss of the anti-tumor barriers elicited by DDR, providing an explanation for the extremely high rate of TP53 mutations in sporadic solid tumors and initiation of DDR in advanced cancers (Halazonetis et al., 2008 Negrini et al., 2010).


NLRs as Double Agents

As discussed in the last section, NLRP12 and NLRP6 have roles in inhibiting inflammation by modulating NF-㮫 activation (77�, 83). In addition, both of these NLRs are reported to regulate inflammasome activation (84�). As discussed in the introduction, NLRC2 is able to respond to both MDP and viral RNA and activates distinct pathways including NF-㮫, autophagy, or antiviral signaling (Table ​ (Table1). 1 ). All of these pathways are important for inflammation and immunity. However, NLRs are also implicated in numerous non-inflammatory roles. NLRC1 and NLRC2 have been shown to regulate the differentiation of human umbilical cord blood-derived mesenchymal stem cells (MSC). Although NLRC1 and NLRC2 had no effect on MSC proliferation, they enhanced their differentiation into chondrocytes and osteocytes and inhibited adipocyte formation in vitro (95). The ability of NLRC1 and NLRC2 to regulate MSC differentiation was associated with increased ERK1/2 MAPK signaling a known function of these NLRs (Table ​ (Table1). 1 ). The ability of NLRs to affect MSC may play an important part of wound healing and the resolution of inflammation. In fact, NLRP3 was found to play an important function in tissue repair in the lung during influenza A virus infection, although this was likely due to impaired recruitment of macrophages or other cells necessary for wound repair and healing (43).

Table 1

Functionally distinct roles of NLRs in biology.

NLRDual rolesReference
NLRP12 a NF-㮫 inhibition, caspase-1 activationWilliams et al. (76), Arthur et al. (81), Ye et al. (79), Jeru et al. (87), Jeru et al. (88), Zaki et al. (77), Allen et al. (78), Vladimer et al. (86), Chattoraj et al. (80)
NLRP6 a NF-㮫 inhibition, caspase-1 activationChen et al. (84), Elinav et al. (85), Anand et al. (83)
NLRC2 b NF-㮫 and MAPK activation, type-I IFN production, autophagy, MSC differentiationBertin et al. (20), Girardin et al. (21), Park et al. (22), Dugan et al. (23), Sabbah et al. (24), Kim et al. (95), Lupfer et al. (25)
NLRP2 c Embryonic development, caspase-1 activationBruey et al. (96), Fontalba et al. (97), Meyer et al. (99), Peng et al. (101), Huang et al. (100), Minkiewicz et al. (98)
NLRP7 c Embryonic development, caspase-1 activationMurdoch et al. (103), Messaed et al. (104), Khare et al. (102), Huang et al. (100), Ulker et al. (105)

The NLRs listed in this table have been implicated in multiple functional roles. However, the mechanisms by which they perform these distinct roles have not been elucidated. a It is unclear how NLRP6 and NLRP12 function under some inflammatory conditions as inhibitors of NF-㮫 but under other conditions can serve as inflammasome activators. b NLRC2 responds to a variety of PAMPs including MDP and viral RNA, but the downstream signaling pathways triggered by NLRC2 are distinct for specific PAMPs suggesting alterative activation mechanisms. c Finally, NLRP2 and NLRP7 may serve as inflammasome regulators, but whether their functions in embryonic development are tied to inflammasome activation or are separate functions is unclear.

The role of NLRs in tissue repair or MSC differentiation may be a logical progression following inflammation but several additional NLRs have been reported to regulate seemingly disparate functions. NLRP2 is reported to inhibit NF-㮫 activation (96, 97) and to enhance caspase-1 activation (96). In addition, siRNA mediated knockdown of NLRP2 in primary human astrocytes was recently reported to impair inflammasome activation (98). How NLRP2 affects inflammasome activation is not entirely clear, as knockdown of NLRP2 resulted in decreased caspase-1 expression as well. Furthermore, the stimulus used for NLRP2 activation was the NLRP3 activator extracellular ATP (98). These findings might indicate that NLRP2 regulates the expression of key NLRP3 inflammasome components as opposed to a novel NLRP2 specific inflammasome. In addition to the role for NLRP2 in inflammasome activation and inhibition of NF-㮫 signaling, NLRP2 has a definite role in embryonic development (Table ​ (Table1). 1 ). A truncation mutation of NLRP2 was found in association with Beckwith–Wiedemann Syndrome (BWS) (99). The NLRP2 mutation resulted in developmental defects that stemmed from altered DNA methylation and gene expression initially present in the maternal oocyte (maternal imprinting) and perpetuated in the fertilized embryo and developing fetus (99). Another study found some association between NLRP2 and recurrent miscarriages (100). Finally, siRNA knockdown of NLRP2 in murine oocytes or embryos leads to nearly complete developmental arrest (101).

Other NLRs have also been proposed to regulate inflammasome activation and development. NLRP7 regulates inflammasome activation in response to acylated lipopeptides like FSL-1 or triacylated Pam3CSK4 (102). In addition, NLRP7 is associated with recurrent miscarriages and recurrent hydatidiform molar pregnancies (100, 103�). The above findings definitely support roles for NLRP2 and NLRP7 in inflammation and development. Interestingly, NLRP7 is not present in the mouse genome and appears to have arisen from a gene duplication event from NLRP2 (103). Therefore, it is not surprising that these two NLRs possess similar functions, but how they regulate both inflammasome activation and development is currently unknown (Table ​ (Table1). 1 ). Indeed, the role of NLRs in development is severely understudied, and many biochemical and cell specific studies on the function of these NLRs are needed to understand their differential roles. One possibility is that inflammasome activation is the mechanism by which NLRP2 and NLRP7 regulate embryonic development. The role of IL-1β in oocyte maturation and development has been appreciated for over a decade and has been reviewed previously (106, 107). Intrafollicular injection of IL-1β in horses induces ovulation but also inhibits embryo development (108), which is similar to the developmental arrest seen with NLRP2 and NLRP7 mutations. Furthermore, treatment of rabbit ovaries in vitro with IL-1β also arrests developing embryos (109). However, a lack of IL-1β signaling does not significantly affect fertility and embryo viability as IL-1 receptor deficient mice reproduce normally (110). Therefore, increased levels of IL-1β in patients with NLRP2 and NLRP7 mutations may be the cause of developmental arrest. However, much additional research on the roles of NLRP2 and NLRP7 needs to be performed before any conclusions can be reached regarding their functions in development.


Inflammation and inflammasome

Inflammation

Inflammation is a nonspecific mechanism generated by the host in response to an infectious, physical, or chemical injury with recruitment of peripheral blood leukocytes and plasma proteins to the site of injury or tissue damage. In this process, there is an increase in both blood flow and vascular permeability, mainly in the vascular endothelial at the local level. Vascular permeability is a consequence of the endothelial cell retraction to allow the transmigration of leukocytes and the ingress of plasmatic proteins such as complement, coagulation factors, and antibodies, etc. (118).

After an injury, there is tissue damage with the release of components by epithelial or endothelial cells as well as by cells present in that tissue such as mast cells or ILCs. These substances include histamine, leukotrienes, extracellular matrix components, and pro-inflammatory cytokines and chemokines, all of which have the ability to induce chemotaxis and cell adhesion molecule (CAM) expression in both endothelium and leucocytes. These CAMs include selectins, integrins, immunoglobuline-like superfamily molecules and cadherins. Expression of these CAMs allows interaction between leukocytes and endothelium and the subsequent leukocyte transmigration at the site of the injury. In the latter process, cells are guided by chemoattractant stimuli (Figure 3). The cell migration process is complex and depends on cell type as well as on the differentiation and activation state of the cells (118). As was mentioned, the first cells recruited at the site of the injury are neutrophils. They are also the most abundant during the first hours or days of the inflammation process followed by mononuclear cells. If the inflammatory reaction cannot be resolved, this process may become chronic with other implications for the host.

Figure 3

Recruiting phagocytes into the inflammation site and phagocytosis. Phagocyte recruitment involves several phases including: i) marginalization, which decrease leukocyte traffic with a subsequent endothelium approach ii)adhesion, a process that depends (more. )

During the inflammation process, there is another important event known as phagocytosis. Phagocytosis is considered one of the most important processes during the innate immune response. Once phagocytes arrive at the infectious site, they ingest microbial pathogens in vacuoles called phagosomes. Here, after activation, these microorganisms are destroyed and then presented to lymphocytes via MHC. The microbicidal mechanisms included are, therefore, oxygen-dependent and -independent as described previously (5,119).

The phagocytic process is mediated by the cytoskeleton of the phagocytic cells as well as by endocytic and signaling receptors (96). These receptors, mainly PRRs present on cell surfaces, bind microbial PAMPs, and this interaction usually generates an intracellular signal which, in turn, allows the synthesis and release of proinflammatory cytokines and other effector molecules (3).

Proinflammatory cytokines play an important role during the inflammation process, and they participate in the interactions of the cells involved in not only the innate immune response but also the establishment of acquired immunity. Proinflammatory cytokines participate during the activation and effector phases of the innate immune response. These cytokines include TNF-α, IL-1, and type I IFNs. Nonetheless, other cytokines are also important during the establishment of the innate immune response (Table 3). Functions and characteristics of these cytokines are extensively described in Chapter 9.

Table 3

Cytokines of innate immunity.

Inflammasome

Inflammasome is a complex of proteins consisting of caspase-1, ASC (a CARD-containing adaptor), and NLRs. Once these are activated, they cleave the pro-IL-1β and pro-IL-18 with subsequent maturation and secretion of these cytokines. Inflammasome activation is required for many inflammatory processes. In addition to the initial recognition of PAMPs or DAMPS by TLRs or CLRs, recognition by intracytoplasmic NLRs is necessary. Inflammasome may be also activated by ROS, lysosomal damage, and cytosolic K+ efflux at the intracellular level (110,117). Several members of the NLR family are involved in the assembly of inflammasome. These molecules include NLRP3, NLRP1, NLRP6, and IPAF (NLRC4). Moreover, the AIM2 protein, a non-NLR that is identified as a PYHIN (pyrin and HIN domain-containing protein) family member, is also involved in the inflammasome activation (117).


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Comments:

  1. Mezigal

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  2. JoJozahn

    romance



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