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Conference Article| November 01 1993 Evidence for a redox-sensitive protein tyrosine kinase in nuclear factor kappa B activation and interleukin 2 production in EL4.NOB1 cells TARA M. MAHON; TARA M. MAHON 1Biochemistry Department and Biotechnology Institute, Trinity College, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar PAUL BRENNAN; PAUL BRENNAN 1Biochemistry Department and Biotechnology Institute, Trinity College, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar L. A. J. O'NEILL L. A. J. O'NEILL 1Biochemistry Department and Biotechnology Institute, Trinity College, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1993) 21 (4): 389S. https://doi.org/10.1042/bst021389s Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Twitter LinkedIn Cite Icon Cite Get Permissions Citation TARA M. MAHON, PAUL BRENNAN, L. A. J. O'NEILL; Evidence for a redox-sensitive protein tyrosine kinase in nuclear factor kappa B activation and interleukin 2 production in EL4.NOB1 cells. Biochem Soc Trans 1 November 1993; 21 (4): 389S. doi: https://doi.org/10.1042/bst021389s Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1993 Biochemical Society1993 Article PDF first page preview Close Modal You do not currently have access to this content.
No abstract is provided for this article.
No abstract is provided for this article.
Research into the five Toll/IL1 receptor (TIR) adaptor proteins involved in innate immunity continues to advance. Here we outline some of the more recent findings. MyD88 has a key role in signalling by the IL1 receptor complex and TLRs. However, a MyD88-independent pathway of IL1β signalling in neurons has been described which involves the protein kinase Akt, and which has an anti-apoptotic effect. This pathway may also be important for the mechanism whereby Alum exerts its adjuvant effect since this depends on IL1β but is MyD88-independent. MyD88 is also involved in tumourigenesis in models of hepatocarcinoma and familial associated polyposis (FAP); negative regulation of TLR3 signalling and in PKCε activation. The adaptor Mal is regulated by phosphorylation and caspase-1 cleavage. A variant form of Mal in humans termed S180L confers protection in multiple infectious diseases. TRAM is controlled by myristoylation and phosphorylation and the localisation of TRAM with TLR4 to endosomes is required for activation of IRF3 and induction of IFNβ. Finally SARM has been shown to regulate TRIF and also appears to be involved in neuronal injury mediated by oxidative stress in mouse neurons. These advances confirm the importance for the TIR domain-containing adapters in host defence and inflammation.
Conference Article| February 01 1995 EFFECTS OF PERTUSSIS TOXIN AND ITS BINDING SUBUNIT ON IL-1 SIGNALLING IN T CELLS Leone M. McCarthy; Leone M. McCarthy 1Dept. of Biochemistry and Biotechnology Institute, Trinity College, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar Luke A.J. O'Neill Luke A.J. O'Neill 1Dept. of Biochemistry and Biotechnology Institute, Trinity College, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1995) 23 (1): 112S. https://doi.org/10.1042/bst023112s Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Facebook Twitter LinkedIn MailTo Cite Icon Cite Get Permissions Citation Leone M. McCarthy, Luke A.J. O'Neill; EFFECTS OF PERTUSSIS TOXIN AND ITS BINDING SUBUNIT ON IL-1 SIGNALLING IN T CELLS. Biochem Soc Trans 1 February 1995; 23 (1): 112S. doi: https://doi.org/10.1042/bst023112s Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1995 Biochemical Society1995 Article PDF first page preview Close Modal You do not currently have access to this content.
Summary Innate immune responses vary in a circadian manner, and more recent investigations aim to understand the underlying molecular mechanisms. Cytokine production varies significantly over the course of a day depending on the time of stimulation by pathogens or Toll‐like receptor ligands, and multiple signaling pathways linked to the cell‐autonomous circadian clock modulate innate immunity. Recognition of foreign material, especially by innate immune cells, engages a myriad of receptors, which trigger inflammatory responses, as well as endocytosis and degradation and/or processing for antigen presentation. Because of the close connection between particle engulfment and inflammation, it has been proposed that phagocytic uptake may drive cytokine production in phagocytes. Here we show that bacterial particle ingestion by mouse peritoneal macrophages displays temporal variation, but is independent of the cell‐intrinsic circadian clock in an ex vivo setting. Although cytokine production is dependent on phagocytosis, uptake capacity across 12 hr does not translate into 24‐hr rhythms in cytokine production. In vivo , time‐of‐day variations in phagocytic capacity are not found, whereas a time of day and clock‐dependent cytokine response is maintained. These data show that efficiency of bacterial phagocytosis and the 24‐hr rhythmicity of cytokine production by macrophages are independent of one another and should be studied separately.
Conference Article| February 01 1996 Interleukin I receptors and signal transduction L A. J. O'neill L A. J. O'neill 1Department of Biochemistry, Trinity College Dublin, Dublin 2, Ireland Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1996) 24 (1): 207–211. https://doi.org/10.1042/bst0240207 Article history Received: August 14 1995 Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share MailTo Twitter LinkedIn Cite Icon Cite Get Permissions Citation L A. J. O'neill; Interleukin I receptors and signal transduction. Biochem Soc Trans 1 February 1996; 24 (1): 207–211. doi: https://doi.org/10.1042/bst0240207 Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search Keywords: hsp27, heat-shock protein 27, IL, interleukin, IL1RA, interleukin 1 receptor antagonist, IL1RI/II, Type I and II IL1 receptors, MAP kinase, mitogen-activated protein kinase This content is only available as a PDF. © 1996 Biochemical Society1996 Article PDF first page preview Close Modal You do not currently have access to this content.
No abstract is provided for this article.
No abstract is provided for this article.
The proinflammatory danger signal IL-33, which is released from damaged or dying cells, achieves its effects via the IL-1R family member ST2L. The detection of IL-33 by ST2L initiates downstream signaling pathways that result in the activation of MAPKs and NF-κB. Here, we show that TMED1 associates with ST2L. Using a series of mutation and deletion constructs, we demonstrate that this interaction is mediated by the GOLD domain of TMED1 and the TIR domain of ST2L. Our findings also demonstrate that TMED1 is required for optimal IL-33-induced IL-8 and IL-6 production. This discovery provides additional support to the concept that the TMED family members are important players in innate immune signaling.
