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DNA was extracted from CD138+ or CD19+CD138+ sorted cells isolated from the bone marrows of IgM amyloidosis patients. The study reports of MYD88 L265P somatic mutation in IgM-associated light-chain amyloidosis patients.
BTK (show BTK Proteins)-inhibitor ibrutinib and FK866 resulted in a significant and synergistic anti-Waldenstrom macroglobulinemia cell death, regardless of MYD88 and CXCR4 (show CXCR4 Proteins) mutational status.
Study found evidence of alterations in the expression of the initial elements of the TLR4 (show TLR4 Proteins) signalling pathway (TLR4 (show TLR4 Proteins), MyD88 and NF-kappaB (show NFKB1 Proteins)) in the PFC (show CFP Proteins) of patients with schizophrenia. These alterations seem to depend on the presence/absence of antipsychotic treatment at death. Moreover, a polymorphism within the MyD88 gene was significantly associated with schizophrenia risk.
The present study demonstrates that MYD-88 L265P mutation may represent the only sensitive marker for the differentiation of CBL (show CBL Proteins)-MZ from probable WM.
Aqueous fluid from the second patient with intraocular B-cell lymphoma demonstrated a less common mutation in the MYD88 gene associated with B-cell lymphoma.
Studies indicate that ibrutinib is active in patients with Waldenstrom macroglobulinemia (WM) and is affected by MYD88 and CXCR4 (show CXCR4 Proteins) mutation status.
Moreover, anchoring of MyD88 to the cell membrane augments signaling supporting the importance of membrane localization in MyD88-mediated signaling.
MyD88 cysteine residues functionally modulate MyD88-dependent NF-kappaB (show NFKB1 Proteins) activation, suggesting a link between MyD88 thiol oxidation state and immune signaling.
the expression of certain TAM (show CCNA1 Proteins) components was reduced as a result of prolonged degradation of MYD88 by Porphyromonas gingivalis infection.
MYD88 expression in subcutaneous adipose tissue of obese subjects could be associated with the development of components of Metabolic syndrome.
Immobilization stress-induced anorexia is mediated independent of MyD88.
TLR4 (show TLR4 Proteins)-MyD88 expression on B1a cells is critical for their IgM (show CD40LG Proteins)-dependent atheroprotection that not only reduced lesion apoptotic cells and necrotic cores, but also decreased CD4 (show CD4 Proteins) and CD8 (show CD8A Proteins) T-cell infiltrates and augmented TGF-beta1 (show TGFB1 Proteins) expression accompanied by reduced lesion inflammatory cytokines TNF-alpha (show TNF Proteins), IL-1beta (show IL1B Proteins), and IL-18 (show IL18 Proteins).
A cell-specific role for MyD88 was determined in the development of chronic ETOH-induced liver injury.
MyD88 signaling in myeloid and dendritic cells is dispensable for IFN-gamma (show IFNG Proteins)-dependent control of type A F. tularensis infection.
Myd88 is a crucial mediator of local and systemic Sjogren's syndrome disease manifestations.
These results demonstrate that PTX targets the innate immunity through DAP12, FcRgamma, and MyD88 providing new insights into the immunobiology of PTX.
the role of the adaptor molecule MyD88 in a mouse model of adenovirus keratitis, is reported.
TLR9 (show TLR9 Proteins)/MyD88 signaling selectively in CD11c (show ITGAX Proteins)(+) dendritic cells (DCs) strongly enhances murine cytomegalovirus clearance.
Taken together, the data demonstrate a critical role of MyD88 in DCs and of IL-33 (show IL33 Proteins) signaling via ST2 (show SULT2A1 Proteins) in MC903-induced Atopic dermatitis (AD). These data suggest that IL-33 (show IL33 Proteins)/IL-33R may be a therapeutic target of AD.
CD103 (show ITGAE Proteins)(-)CD11b (show ITGAM Proteins)(+) dendritic cells instruct both IFNgamma(+) and IL-17 (show IL17A Proteins)(+) T cells, and only the IL-17 (show IL17A Proteins)-inducing antigen presenting cell functions require MyD88.
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
, 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