Measurement of the Density of Base Fluids at Pressures 0.422 to 2.20 Gpa

The influence of pressure on the density of six base fluids is experimentally studied for a range of pressures from 0.422 to 2.20 GPa. An important parameter used to describe the results is the change in relative volume with change in pressure dv sub r/dp. For pressures less than the solidification pressure (p ps) a small change in pressure results in a large change in dv sub r/ps. For pressures greater than the solidification pressure (p ps) there is no change in dv sub r/dp with changing pressure. The solidification pressures of the base fluids varies considerably, as do the slopes that the experimental data assumes for p ps. A new formula is developed that describes the effect of pressure on density in terms of four constants. These constants vary for the different base fluids tested

A role for the adaptor proteins TRAM and TRIF in toll-like receptor 2 signaling

Toll-like receptors (TLRs) are involved in sensing invading microbes by host innate immunity. TLR2 recognizes bacterial lipoproteins/lipopeptides, and lipopolysaccharide activates TLR4. TLR2 and TLR4 signal via the Toll/interleukin-1 receptor adaptors MyD88 and MAL, leading to NF-kappaB activation. TLR4 also utilizes the adaptors TRAM and TRIF, resulting in activation of interferon regulatory factor (IRF) 3. Here, we report a new role for TRAM and TRIF in TLR2 regulation and signaling. Interestingly, we observed that TLR2-mediated induction of the chemokine Ccl5 was impaired in TRAM or TRIF deficient macrophages. Inhibition of endocytosis reduced Ccl5 release, and the data also suggested that TRAM and TLR2 co-localize in early endosomes, supporting the hypothesis that signaling may occur from an intracellular compartment. Ccl5 release following lipoprotein challenge additionally involved the kinase Tbk-1 and Irf3, as well as MyD88 and Irf1. Induction of Interferon-beta and Ccl4 by lipoproteins was also partially impaired in cells lacking TRIF cells. Our results show a novel function of TRAM and TRIF in TLR2-mediated signal transduction, and the findings broaden our understanding of how Toll/interleukin-1 receptor adaptor proteins may participate in signaling downstream from TLR2