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Patients with primary breast and primary female genital tract diffuse large B cell lymphoma have a high frequency of MYD88 mutations.
Mutation in the MYD88 gene is associated with lymphoplasmacytic lymphoma and chronic lymphocytic leukemia.
the polymorphisms in TLR-MyD88-NF-kappaB (show NFKB1 Proteins) signaling pathway confer genetic susceptibility to Type 2 diabetes mellitus and diabetic nephropathy.
Here the authors show that MAL TIR domains spontaneously and reversibly form filaments in vitro. They also form cofilaments with TLR4 (show TLR4 Proteins) TIR domains and induce formation of MyD88 assemblies.
data show that in pericytes, MyD88 and IRAK4 (show IRAK4 Proteins) are key regulators of 2 major injury responses: inflammatory and fibrogenic.
Data indicate that 64 patients (57.1%) carried the myeloid differentiation factor 88 protein (MYD88) L265P mutation and 14 patients (12.5%) carried the chemokine (C-X-C motif) receptor 4 (CXCR4) WHIM (show CXCR4 Proteins)-like mutation.
HCK (show HCK Proteins) represents a novel target for therapeutic development in MYD88-mutated Waldenstrom macroglobulinemia and activated-B cell diffuse large B-cell lymphoma, and possibly other diseases driven by mutated MYD88.
We found an that enhanced expression of the TLR4 (show TLR4 Proteins)-MyD88-NF-kB pathway occurs in GDM placentae, which positively correlates with heightened local IR in placentae and higher maternal hyperglycemia. The TLR4 (show TLR4 Proteins)/MyD88/NF-kB pathway may play a potential role in the development of IR in placentae of GDM.
We found that over-expression of CRNDE in astrocytes increased the expression of key factors in the toll (show TLR4 Proteins)-like receptor signaling pathway, especially toll-like receptor-3 (show TLR3 Proteins)-mediated MyD88-independent pathway.We speculated that CRNDE might trigger inflammation to regulate tumorigenesis and tumor development through the toll (show TLR4 Proteins)-like receptor pathway
Data suggest that, in monocytes and macrophages, the interleukin-1B- (IL1B (show IL1B Proteins))-stimulated trans-autophosphorylation of IRAK4 (interleukin-1 receptor-associated kinase 4 (show IRAK4 Proteins)) is initiated by MYD88-induced dimerization of IRAK4 (show IRAK4 Proteins). In contrast, IRAK1 (interleukin-1 receptor-associated kinase 1 (show IRAK1 Proteins)) is inactive in unstimulated monocytes/macrophages and is converted to an active protein kinase (show CDK7 Proteins) in response to IL1B (show IL1B Proteins).
MyD88 signaling in lysozyme (show LYZ Proteins) M and CD11c (show ITGAX Proteins)-expressing myeloid cells, as well as in pulmonary epithelial cells, is critical to restore inflammatory cytokine and antimicrobial peptide (show cAMP Proteins) production, leading to efficient neutrophil recruitment and enhanced bacterial clearance.
These results suggest that S. Typhimurium promotes its systemic growth and dissemination through MyD88 signaling pathways in mesenchymal cells.
data are significant in uncovering a latent, but potent, negative-regulatory role for Myd88 and Fcer1g (show FCER1G Proteins) in the late stages of B cell responses; such roles could limit acute responses; however, they could be particularly significant in chronic responses, such as autoimmunity and chronic infection
both Myd88(-/-) mouse strains developed some degree of epidermal thickening during the initial stages of IMQ-induced psoriasis, even in the absence of hematopoietic cell activation and infiltration into the skin, suggesting a contribution of MyD88-independent mechanisms in skin-resident stromal cells.
The data suggest that MyD88 signaling in dendritic cells (DC) and intestinal epithelial cells (IEC) is both essential and sufficient to induce a full spectrum of host responses upon intestinal infection with Citrobacter rodentium.
Downregulation of adaptor protein MyD88 compromises the angiogenic potential of B16 murine melanoma\
These data show that the normal distribution of surface glycosylation requires IL-1R, but not MyD88, and is not sufficient to prevent bacterial binding.
TLR4 (show TLR4 Proteins) agonist MPLA potently induced MyD88-dependent signaling. Neutrophil recruitment after multiple injections of MPLA was reliant on MyD88-dependent signaling. MPLA treatment induced expansion of myeloid progenitors in bone marrow and upregulation of CD11b (show ITGAM Proteins) and shedding of L-selectin (show SELL Proteins) by neutrophils, all of which were attenuated in MyD88-deficient mice.
Autophagy contributes to macrophage resistance to Leishmania major. Data, including data from studies in knockout mice, suggest a key resistance mechanism involves endosomal signaling via Tlr3 (show TLR3 Proteins)/7/9 in macrophages; macrophages deficient for Tlr3 (show TLR3 Proteins)/7/9, Unc93b1, or MyD88 fail to undergo L. major-induced autophagy. (TLR = Toll (show TLR4 Proteins)-like receptor; Unc93b1 = unc-93 homolog B1; MyD88 = myeloid differentiation primary response gene 88)
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 (show TIRAP Proteins) and that both proteins function as sorting adaptors to recruit downstream signaling adaptors to activated receptors
DmMyD88 encodes an essential component of the Toll (show TLR4 Proteins) 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 (show IRAK1 Proteins).
These results suggest that porcine circovirus 2 induces IL-8 (show IL8 Proteins) secretion via the TLR2/MyD88/NF-kappaB (show NFKB1 Proteins) 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.
Fish IRF6 (show IRF6 Proteins) is distinguished from the homolog of mammals by being a positive regulator of IFN transcription and phosphorylated by MyD88 and TBK1 (show TBK1 Proteins), suggesting that differences in the IRF6 (show IRF6 Proteins) 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 (show IRF1 Proteins) 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 (show IRF6 Proteins) signaling from TLR-4 (show TLR4 Proteins) to downstream effector molecules involved in NF-kappaB (show NFKB1 Proteins) activation
MyD88 interacts with interferon (show IFNA Proteins) regulatory factor (IRF) 3 (show IRF3 Proteins) and IRF7 (show IRF7 Proteins) 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
, interleukin-1 receptor-associated kinase-like 2
, interleukin-1 receptor-associated kinase 2
, 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