[62-65] Our results suggest that RBV enhances the TAA-specific cellular immune response in association with down-modulation of Treg-cell activity. As previously reported for CPA,[66] this hypothesis may contribute to preventing the progression

to hepatocellular carcinoma in patients with HCV infection who were successfully treated with IFN plus RBV. To confirm this hypothesis, long-term observation of patients receiving pegylated IFN plus RBV therapy will be needed. In addition, it must be determined whether continuous Y-27632 in vitro administration of RBV after the elimination of HCV can contribute to the prevention of hepatocellular carcinoma. In this report, we demonstrated the ability of RBV to inhibit the differentiation of naive CD4+ T cells into CD25+ FOXP3+ Tregadapt cells through the inhibition of Treg1-type regulatory cells. Although the mechanism of action by which RBV regulates Treg cells is not fully understood, we expect that these findings will contribute to establishing a new approach

for regulating immune responses in patients with various diseases caused by immunological impairment. We are grateful to Dr Taku Tsukui, Division of Gastroenterology, Department of Medicine, Nippon Medical School, Tokyo, Japan, for critical reading of this manuscript and helpful suggestions. The authors declare that there is no conflict of interest. “
“Aeromonas have been isolated from a wide variety of aquatic environments.

However the number of Aeromonas in sea water is extremely small compared to that in fresh water. In in vitro culture, Aeromonas can grow in mediums containing B-Raf inhibition NaCl at a concentration of 3.0%, this concentration corresponding Acyl CoA dehydrogenase to that of sea water. It is unclear why the number of Aeromonas is low in sea water. Exoproteins of bacteria are thought to be important for bacterial growth and survival in the environment. Previously, the present authors have shown that mediums containing 3.0% NaCl suppress production of two proteases, serine protease and metalloprotease. In this experiment, other exoproteins whose production is influenced by the amount of NaCl in the medium were analyzed. A protein whose production is repressed in medium containing 3.0% NaCl was found and purified. Biological assay of the purified protein showed that it degrades tributyrin and hydrolyzes para-nitrophenyl-fatty acylesters. These results show that the protein is a lipase. Subsequently, the nucleotide sequence of the gene encoding the lipase was determined and the amount of mRNA of the lipase gene in the cells measured. It was found that transcription of the gene is not inhibited by NaCl in the medium. This result indicates that the lipase might be synthesized, but the folding process to become an active structure does not progress smoothly in a medium containing 3.0% NaCl. Motile Aeromonas spp. (A. sobria, A. hydrophila, and A.