SO₂ emissions from basaltic eruptions, and the excess sulfur issue

Volcanic SO2 can affect the Earth's environment. Where no direct measurements of SO2 in the atmosphere are available, a petrologic method of assessing sulfur release from the magma must be used. However, in studies of arc-derived eruptions, satellite-based measurements of SO2 emissions using Total Ozone Mapping Spectrometer (TOMS) data are orders of magnitude greater than those calculated petrologically, implying that a separate S-rich gas phase in the magma chamber may be responsible for the excess sulfur. We test whether this applies in other settings. For Icelandic and Hawaiian basalts we find that petrologic SO2 values are comparable to measurements of SO2 by TOMS. Thus, for non-arc basalts, the petrologic method gives reliable estimates of SO2 released. The implied absence of excess sulfur in non-arc basaltic magmas is a reflection of source magma conditions, notably lower fO2 and volatile contents than arc magmas, inhibiting the exsolution of a S-rich gas prior to eruption

Storage time of platelet concentrates and all-cause bacteremia in hematologic patients

Stemcel biology/Regenerative medicine (incl. bloodtransfusion

TILRR, a Novel IL-1RI Co-receptor, Potentiates MyD88 Recruitment to Control Ras-dependent Amplification of NF-κB*

Host defense against infection is induced by Toll-like and interleukin (IL)-1 receptors, and controlled by the transcription factor NF-κB. Our earlier studies have shown that IL-1 activation impacts cytoskeletal structure and that IL-1 receptor (IL-1RI) function is substrate-dependent. Here we identify a novel regulatory component, TILRR, which amplifies activation of IL-1RI and coordinates IL-1-induced control with mechanotransduction. We show that TILRR is a highly conserved and widely expressed enhancer of IL-1-regulated inflammatory responses and, further, that it is a membrane-bound glycosylated protein with sequence homology to members of the FRAS-1 family. We demonstrate that TILRR is recruited to the IL-1 receptor complex and magnifies signal amplification by increasing receptor expression and ligand binding. In addition, we show that the consequent potentiation of NF-κB is controlled through IL-1RI-associated signaling components in coordination with activation of the Ras GTPase. Using mutagenesis, we demonstrate that TILRR function is dependent on association with its signaling partner and, further, that formation of the TILRR-containing IL-1RI complex imparts enhanced association of the MyD88 adapter during ligand-induced activation of NF-κB. We conclude that TILRR is an IL-1RI co-receptor, which associates with the signaling receptor complex to enhance recruitment of MyD88 and control Ras-dependent amplification of NF-κB and inflammatory responses