In the present work, methyl viologen (1,1′-dimethyl-4,4′-bipyridinium dichloride) is used as a scavenger to estimate the radiolytic yields of water decomposition products from room temperature to 400 °C by pulse radiolysis method. {G(e aq -) + G(OH) + G(H)} has been studied using a 0.5 mM MV 2+ solution in the presence of 10 mM NaCOOH up to 200 °C and in the presence of 0.2 M ethanol up to 400 °C. The results show that the {G(e aq -) + G(OH) + G(H)} increases with temperature up to 350 °C at 25 MPa, while it depends also on pressure in supercritical conditions. The G(e aq -) was estimated using MV 2+ solutions in the presence of 0.2 M tert-butyl alcohol. The results agree well with the reported data up to around 300 °C at 25 MPa; however, in supercritical conditions a very significant density effect was observed. At a given temperature, G(e aq -) and {G(e aq -) + G(OH) + G(H)} decrease with increasing density while at a fixed density they decrease with increasing temperature.

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The Tearscope-Plus™ is not interchangeable with either the Oculus® K5M measurement of tear stability (NIKBUT-1) or the LipiView® maximum and minimum lipid thickness.

BackgroundThe DEP domain is a globular domain containing approximately 90 amino acids, which was first discovered in 3 proteins: Drosophila disheveled, Caenorhabditis elegans EGL-10, and mammalian Pleckstrin; hence the term, DEP. DEPDC1B is categorized as a potential Rho GTPase-activating protein. The function of the DEP domain in signal transduction pathways is not fully understood. The DEPDC1B protein exhibits the characteristic features of a signaling protein, and contains 2 conserved domains (DEP and RhoGAP) that are involved in Rho GTPase signaling. Small GTPases, such as Rac, CDC42, and Rho, regulate a multitude of cell events, including cell motility, growth, differentiation, cytoskeletal reorganization and cell cycle progression.ResultsIn this study, we found that it was a guanine nucleotide exchange factor and induced both cell migration in a cultured embryonic fibroblast cell line and cell invasion in cancer cell lines; moreover, it was observed to promote anchorage-independent growth in oral cancer cells. We also demonstrated that DEPDC1B plays a role in regulating Rac1 translocated onto cell membranes, suggesting that DEPDC1B exerts a biological function by regulating Rac1. We examined oral cancer tissue; 6 out of 7 oral cancer tissue test samples overexpressed DEPDC1B proteins, compared with normal adjacent tissue.ConclusionsDEPDC1B was a guanine nucleotide exchange factor and induced both cell migration in a cultured embryonic fibroblast cell line and cell invasion in cancer cell lines; moreover, it was observed to promote anchorage-independent growth in oral cancer cells. We also demonstrated that DEPDC1B exerts a biological function by regulating Rac1. We found that oral cancer samples overexpressed DEPDC1B proteins, compared with normal adjacent tissue. Suggest that DEPDC1B plays a role in the development of oral cancer. We revealed that proliferation was linked to a novel DEPDC1B-Rac1-ERK1/2 signaling axis in oral cancer cell lines.