Kyushu University

About: Kyushu University is a education organization based out in Fukuoka, Japan. It is known for research contribution in the topics: Population & Catalysis. The organization has 68284 authors who have published 135190 publications receiving 3055928 citations. The organization is also known as: Kyūshū Daigaku.

Theory of gas-diffusion controlled sensitivity for thin film semiconductor gas sensor

Abstract: Influences of gas transport phenomena on the sensitivity of a thin film semiconductor gas sensor were investigated theoretically. A diffusion equation was formulated by assuming that an inflammable gas (target gas) moves inside the film by Knudsen diffusion, while it reacts with the adsorbed oxygen following a first-order reaction kinetic. By solving this equation under steady-state conditions, the target gas concentration inside the film was derived as a function of depth (x) from the film surface, Knudsen diffusion coefficient (DK), rate constant (k) and film thickness (L). The gas concentration profile thus obtained allowed to estimate the gas sensitivity (S) defined as the resistance ratio (Ra/Rg), under the assumption that the sheet conductance of the film at depth x is linear to the gas concentration there with a proportionality constant (sensitivity coefficient), a. The derived equation shows that S decreases sigmoidally down to unity with an increase in L k/D K . Further by assuming that the temperature dependence of rate constant (k) and sensitivity coefficient (a) follows Arrenius type ones with respective activation energies, it was possible to derive a general expression of S involving temperature (T). The expression shows that, when the activation energies are selected properly, the S versus T correlation results in a volcano-shaped one, its height increasing with decreasing L. The dependence of S on L at constant T as well as on T at constant L can thus be simulated fairly well based on the equation.

Histamine regulates T-cell and antibody responses by differential expression of H1 and H2 receptors

Abstract: Many pathological processes, including those causing allergies and autoimmune diseases, are associated with the presence of specialized subsets of T helper cells (TH1 and TH2) at the site of inflammation. The diversity of TH1 and TH2 function is not predetermined but depends on signals that drive the cells towards either subset. Histamine, released from effector cells (mast cells and basophils) during inflammatory reactions can influence immune response. Here we report that histamine enhances TH1-type responses by triggering the histamine receptor type 1 (H1R), whereas both TH1- and TH2-type responses are negatively regulated by H2R through the activation of different biochemical intracellular signals. In mice, deletion of H1R results in suppression of interferon (IFN)-gamma and dominant secretion of TH2 cytokines (interleukin (IL)-4 and IL-13). Mutant mice lacking H2R showed upregulation of both TH1 and TH2 cytokines. Relevant to T-cell cytokine profiles, mice lacking H1R displayed increased specific antibody response with increased immunoglobulin-epsilon (IgE) and IgG1, IgG2b and IgG3 compared with mice lacking H2R. These findings account for an important regulatory mechanism in the control of inflammatory functions through effector-cell-derived histamine.

Rad18 guides polη to replication stalling sites through physical interaction and PCNA monoubiquitination

Abstract: The DNA replication machinery stalls at damaged sites on templates, but normally restarts by switching to a specialized DNA polymerase(s) that carries out translesion DNA synthesis (TLS). In human cells, DNA polymerase η (polη) accumulates at stalling sites as nuclear foci, and is involved in ultraviolet (UV)-induced TLS. Here we show that polη does not form nuclear foci in RAD18−/− cells after UV irradiation. Both Rad18 and Rad6 are required for polη focus formation. In wild-type cells, UV irradiation induces relocalization of Rad18 in the nucleus, thereby stimulating colocalization with proliferating cell nuclear antigen (PCNA), and Rad18/Rad6-dependent PCNA monoubiquitination. Purified Rad18 and Rad6B monoubiquitinate PCNA in vitro. Rad18 associates with polη constitutively through domains on their C-terminal regions, and this complex accumulates at the foci after UV irradiation. Furthermore, polη interacts preferentially with monoubiquitinated PCNA, but polδ does not. These results suggest that Rad18 is crucial for recruitment of polη to the damaged site through protein–protein interaction and PCNA monoubiquitination.