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All controls had wild-type MYD88 and CXCR4.
MYD88 L265P is a prevalent somatic mutation in patients with Waldenstrom macroglobulinemia, IgM monoclonal gammopathy of undetermined significance, activated B-cell-like-Diffuse Large B-Cell Lymphoma, and other non-Hodgkin lymphomas
MYD88 was validated as the target for miR-155. Its expression affected breast cancer cell apoptosis, migration, and invasion.
This study suggests that activated monocytes have an impact on brain vascular function through intercellular exosome signaling via Tlr4/MyD88.
these results suggest that MYD88L265P signaling can be enhanced by a second genetic alteration in TNFAIP3 and highlights a potential opportunity for therapeutic targeting.
Therefore, the IRAK4-MyD88 scaffolding function is essential for IL-1 signaling, but IRAK4 kinase activity can control IL-1 signal strength by modulating the association of IRAK4, MyD88, and IRAK1.
This article reviews the significance of MYD88(L265P) and CXCR4(WHIM) mutations in the diagnosis and treatment of Waldenstrom Macroglobulinemia [review]
Blocking either STAT3 or IL-10 could significantly increase the susceptibility of MYD88 L265P mutant lymphomas toward CD8(+) T cell-mediated cytotoxicity.
There is an association between increased MyD88 expression and poor survival in high-grade serous ovarian carcinoma; and demonstrates that increased MyD88 expression is also associated with advanced stage high-grade serous ovarian carcinoma.
MYD88 is highly expressed in primary central nervous system lymphoma and is associated with poor survival.
First report of MYD88(L265P) somatic mutation in IgM-associated light chain amyloidosis.
the MYD88 L265P mutation is significantly associated with the tumor sites and molecular subtypes in diffuse large B-cell lymphomas patients (meta-analysis)
Authors reveal the Toll-like receptor (TLR)-associated factor MyD88 as a target of this K63 deubiquitinase activity.
mutational frequencies in CD79B and MYD88 greatly varied with respect to tissue distribution
MYD88(L265P) mutation does not appear to be a determinant of outcome, and its presence may not be a disease-defining feature in Waldenstrom macroglobulinemia.
A summary of recent progress on elucidating the molecular and cellular processes affected by the oncogenic L265P mutation of MYD88 (review) .
the results of the present study showed significantly higher mRNA expression levels for MYD88 180days post-transplantation in the graft dysfunction group compared to well functioning graft group
the expression levels of TLR4/MyD88 were positively correlated with the metastatic potential of breast cancer cells and tumors. The expression levels of TLR4/MyD88 may be used as a biomarker to evaluate the prognosis and guide the treatment of patients with breast cancer.
AGAP2-AS1 was upregulated and transcriptionally induced by SP1 in breast cancer..ChIP assays showed that AGAP2-AS1-bound CBP increased the enrichment of H3K27ac at the promoter region of MyD88, thus resulting in the upregulation of MyD88. Gain- and loss-of-function assays confirmed that the NF-kappaB pathway was activated by MyD88 and AGAP2-AS1
Activates the NFkappaB pathway through the Tolllike receptor 4 (TLR4)/myeloid differentiation factor 88 (MyD88)/IkappaBalpha axis.
The alarmin IL-1alpha released upon ozone-induced tissue damage and inflammation is mediated by MyD88 signaling in epithelial cells.
These results suggest that urban atmospheric particulate matter less than 2.5mum in diameter (PM2.5) may exacerbate allergic inflammation in the murine lung via a TLR2/TLR4/MyD88-signaling pathway. PM2.5-bound trace microbial elements, such as lipopolysaccharide may be a strong candidate for exacerbation of murine lung eosinophilia.
Both IL1R and MyD88 signalling in CD4+ T cells promote Th17 immunity, atherosclerotic plaque growth and may regulate plaque collagen levels.
MyD88-loaded EVs were detected in the bone marrow aspirates of WM patients thus establishing the physiological role of EVs for MyD88(L265P) transmission and shaping of the proinflammatory microenvironment. Results establish the mechanism of transmission of signaling complexes via EVs to propagate inflammation as a new mechanism of intercellular communication.
Deficiency in MyD88 was associated with decreased BDNF expression. Furthermore, the authors identified a valid kappaB-binding site in the BDNF promoter, consistent with activation of NF-kappaB induced by inflammation.
Analysis of NF-kappaB activation caused by transient expression of proteins involved in the MyD88-dependent pathway in TLR signaling revealed that AKT1 suppressed signaling that occurs between activation of IKKbeta and that of NF-kappaB.
MyD88(-/-) NOD mice had increased numbers of CD11c(+) CD207(-) CD103(+) DCs and activated T effector cells in the skin-draining lymph nodes in a model of contact sensitivity.
the functional activity of TLR2, cluster of differentiation 14 (CD14), and myeloid differentiation primary response gene 88 (MyD88) molecules in the recognition of C. albicans by gingival fibroblast, was investigated.
Study demonstrated the protective effects of miR-203 on mice with IRI after TKA through inhibiting TLR signaling pathway by negatively regulating MYD88.
we found that satellite cell-specific deletion of MyD88 leads to aberrant activation of Notch and Wnt signaling in skeletal muscle of mdx mice. Collectively, our results demonstrate that MyD88-mediated signaling in satellite cells is essential for the regeneration of injured myofibers in dystrophic muscle of mdx mice.
our results indicate that IRAK4 has a critical scaffold function in myddosome formation and that its kinase activity is dispensable for myddosome assembly and activation of the NF-kappaB and MAPK pathways but is essential for MyD88-dependent production of inflammatory cytokines. Our findings suggest that the scaffold function of IRAK4 may be an attractive target for treating inflammatory and autoimmune diseases.
Mice lacking TLR signaling, MyD88-/-, were protected from experimental dry eye-induced ocular surface damage and inflammatory mediator expression, warranting further investigation into TLR inhibition as a potential therapeutic for dry eye disease.
Our findings demonstrate that alkali burn promotes the TLR4-MyD88-caspase-8 axis to cause imbalanced NLRP3/NLRP6, and DS exacerbates ocular surface damage via magnifying this imbalance.
Ablation of inflammsome components reduces SOCS1 induction, and relieves its inhibition on MyD88-IRF7-dependent-IFN-I signaling, leading to high levels of IFN-alpha/beta production and host survival.
Experiments with homozygous knockouts of Irakm (encoding a suppressor of MyD88 inactivation) and Trif in competitive bone marrow transplants revealed that MyD88 is required for High Fat Diet expansion of granulocyte macrophage progenitors and that Trif is required for pregranulocyte macrophage progenitor expansion.
cell-intrinsic and cell-extrinsic MyD88 signaling controls gene expression in conventional dendritic cells and orchestrates immune responses to inhaled allergens
Findings confirm that signalling through MyD88 is the primary driver for Lipopolysaccharide-dependent NF-kappaB translocation to the nucleus. The pattern of NF-kappaB dynamics in TRIF-deficient cells does not, however, directly reflect the kinetics of TNFalpha promoter activation, supporting the concept that TRIF-dependent signalling plays an important role in the transcription of this cytokine.
Study shows the identification two novel variants of MyD88 gene in mouse. The novel transcript and protein isoform MYD88N1 was expressed in several tissues while the MyD88N2 variant was found only in the brain. The existence of different transcription factors binding sites observed after promoter analysis indicates their role in the critical control of gene expression at different developmental stages.
by promoting the initial antigen-specific B cell proliferation and differentiation, B cell-intrinsic MyD88 signaling enhanced both T-independent and T-dependent antibody responses elicited by Bacterial phage Qbeta-derived virus-like particle. This finding will provide additional insight into the role of Toll-Like Receptor signaling in antiviral immunity, autoimmune diseases, and vaccine design.
This study demonstrates that the synergistic effect between TLR4 and TLR3 in macrophages is an important determinant in acute lung injury and, more importantly, that TLR3 up-regulation is dependent on TLR4-MyD88-NF-kappaB signaling.
a novel function of MyD88 in the regulation of metabolism that appears to be independent of its known roles in immunity and development.
propose that dMyD88 is the functional homolog of TIRAP and that both proteins function as sorting adaptors to recruit downstream signaling adaptors to activated receptors
DmMyD88 encodes an essential component of the Toll pathway in dorsoventral pattern formation.
We show that there is a direct interaction between Kra and Tube presumably mediated by the death domains present in both proteins.
both the heterodimeric and heterotrimeric complexes form kidney-shaped structures and that Tube is bivalent and has separate high affinity binding sites for dMyD88 and Pelle.
These results suggest that porcine circovirus 2 induces IL-8 secretion via the TLR2/MyD88/NF-kappaB signalling pathway.
At 30 days after autotransplantation of a pig kidney, mRNA expression increases for MyD88.
These results suggest that an MyD88-dependent signaling pathway is present in newborn as well as in adult swine and that it is involved in the innate immune system of these animals.
suppressed at the mRNA level by intestinal microbial colonization
microbiota-induced, Myd88-dependent signaling inhibits host Notch signaling in the intestinal epithelium, thereby promoting secretory cell fate determination
Fish IRF6 is distinguished from the homolog of mammals by being a positive regulator of IFN transcription and phosphorylated by MyD88 and TBK1, suggesting that differences in the IRF6 regulation pattern exist between lower and higher vertebrates.
DrIRF1 works in concert with MyD88 to activate zebrafish IFNvarphi3 but not IFNvarphi1. These results provide insights into the evolving function of IRF1 as a positive IFN regulator.
MyD88 signaling has an important protective role during early pathogenesis.
MyD88-dependent signaling is involved in the innate immune response of the developing zebrafish embryo, a model for the study of vertebrate innate immunity.
L. rhamnosus GR-1 ameliorates the E. coli-induced disruption of cellular ultrastructure, subsequently reducing the percentage of bovine endometrial epithelial cells apoptosis and limiting inflammatory responses, partly via attenuation of MyD88-dependent and MyD88-independent pathway activation
Modulated cytokine expression in Bovine viral diarrhea virus type 2 infected macrophages was associated with decreased MyD88 expression.
The study demonstrates that in cattle, animals heterozygous at the MyD88 A625C polymorphic marker have a 5-fold reduced risk for active pulmonary tuberculosis.
MyD88 plays a functional role in transducing LPS signaling from TLR-4 to downstream effector molecules involved in NF-kappaB activation
MyD88 interacts with interferon regulatory factor (IRF) 3 and IRF7 in Atlantic salmon (Salmo salar)
the salmon MyD88 was cloned and its expression was analysed.
This gene encodes a cytosolic adapter protein that plays a central role in the innate and adaptive immune response. This protein functions as an essential signal transducer in the interleukin-1 and Toll-like receptor signaling pathways. These pathways regulate that activation of numerous proinflammatory genes. The encoded protein consists of an N-terminal death domain and a C-terminal Toll-interleukin1 receptor domain. Patients with defects in this gene have an increased susceptibility to pyogenic bacterial infections. Alternate splicing results in multiple transcript variants.
myeloid differentiation primary response gene (88)
, myeloid differentiation primary response protein MyD88
, myeloid differentiation primary response protein MyD88-B
, Toll/IL-1 receptor binding protein MyD88-B
, myeloid differentiation primary response gene 88
, myeloid differentiation primary response factor 88
, myeloid differentiation factor 88
, myeloid differentiation primary response protein 88
, myeloid differentiation response protein 88