Aspects of Sino-Japan Complementary and Alternative Medicine and Development on the Traditional Uighur Medicine

Two consecutive conferences on ‘Sino-Japan Complementary and Alternative Medicine and Development on the Traditional Uighur Medicine’ were held in Xinjiang Medical University on July 3 and Kanazawa Medical University on October 6, 2007. The Vice president Halmurat Upur presided over the meeting and gave congratulatory address on holding of the conference. In order to understand mutually and discuss the possibility of the Uighur Medicine as CAM and the situation of medicine in the global sense, specialist scholars of Traditional Uighur Medicine and postgraduates attended this conference. In the meeting of the CAM, the achievements on the research of Traditional Uighur Medicine were exchanged and warmly discussed. Presentations were made in the consecutive conference

共生学の思想史のためのノート

近年、「共生」ということばが非常に多用されている。紀伊国屋のネット検索で６６１点、国立国会図書館では８８０点、岡山大学図書館でも１６９点の図書がこのことばに関わっている。一方、フランス国立図書館では、convivialiteに関するものは、１０点（ドイツ語、イタリア語をふくめて）にすぎない。一方、symbioseに関しては、２７点存在するが、その多くは生態学、衛生学に関わるものである。なぜ、日本で「共生」ということばが多く使われるのだろうか

In Vitro Anti-Cytomegalovirus Activity of Kampo (Japanese Herbal) Medicine

We examined the effect of three types of Kampo medicines on human cytomegalovirus (CMV) replication in the human embryonic fibroblast cell line, MRC-5. Treatment of cells with at least 0.01 μg/ml of Kampo medicines inhibited the cytopathic effects of CMV-infected MRC-5 cells. Moreover, Kampo medicine decreased the replication of CMV without affecting the inhibition of host cells, with a concomitant decrease in CMV DNA levels. However, Kampo medicine demonstrated no virocidal effect on cell-free CMV. Furthermore, western blotting analysis demonstrated that the Kampo medicine decreased the amount of 65 kDa late antigen expression in the infected cells. These results suggest that Kampo medicine may be sufficient to inhibit viral DNA replication and late protein synthesis, resulting in anti-CMV effects. Therefore, these three Kampo medicines have the potential of being a source of new powerful anti-CMV compounds

Chloride Channel in Vanadocytes of a Vanadium-Rich Ascidian Ascidia sydneiensis samea

Ascidians, so-called sea squirts, can accumulate high levels of vanadium in the vacuoles of signet ring cells, which are one type of ascidian blood cell and are also called vanadocytes. In addition to containing high concentrations of vanadium in the +3 oxidation state, the proton concentrations in vanadocyte vacuoles are extremely high. In order to elucidate the entire mechanism of the accumulation and reduction of vanadium by ascidian vanadocytes, it is necessary to clarify the participation of anions, which might be involved as counter ions in the active accumulation of both vanadium and protons. We examined the chloride channel, since chloride ions are necessary for the acidification of intracellular vesicles and coexist with H+ ATPase. We cloned cDNA encoding a chloride channel from blood cells of a vanadium-rich ascidian, Ascidia sydneiensis samea. It encoded a 787-amino-acid protein, which showed striking similarity to mammalian ClC3/4/5-type chloride channels. Using a whole-mount in situ hybridization method that we developed for ascidian blood cells, the chloride channel was revealed to be transcribed in vanadocytes, suggesting its participation in the process of vanadium accumulation

Novel vanadium-binding proteins (Vanabins) identified in cDNA libraries and the genome of the ascidian Ciona intestinalis

Ascidians, especially those belonging to the suborder Phlebobranchia, can accumulate high levels of vanadium. Vanadium-binding proteins (vanabins) were first isolated from a vanadium-accumulating ascidian, Ascidia sydneiensis samea, and then the vanabins were cloned, their expression was studied, and metal-binding assays were conducted. In order to unravel the mechanism of vanadium accumulation, we searched for vanabin-like genes in other animals, including other ascidians. A database search revealed five groups of cDNAs that encoded vanabin-like proteins in another ascidian, Ciona intestinalis. The genes encoding C. intestinalis vanabins, CiVanabin1 to CiVanabin5, were clustered in an 8.4-kb genomic region. The direction of transcription of each gene was identical and each gene had a single intron. All the C. intestinalis vanabins were cysteine rich, and the repetitive pattern of cysteines closely resembled that of A. sydneiensis samea vanabins. Using immobilized metal ion affinity chromatography, we found that a recombinant protein of at least one of the C. intestinalis vanabins (CiVanabin5) bound to vanadium(IV) ions

Molecular biological approaches to the accumulation and reduction of vanadium by ascidians

About 90 years ago, Henze discovered high levels of vanadium in the blood (coelomic) cells of an ascidian collected from the Bay of Naples. His discovery attracted the interdisciplinary attention of chemists, physiologists, and biochemists. Two decades ago, we quantified the vanadium levels in several ascidian tissues definitively using neutron-activation analysis and revealed that some species in the family Ascidiidae accumulate vanadium at concentrations in excess of 350 mM, corresponding to about 107 times that found in seawater. Vanadium accumulated is reduced to the +3 oxidation state via the +4 oxidation state and stored in vacuoles of vanadocytes (vanadium-containing blood cells) where high levels of protons and sulfate are also contained. To investigate this unusual phenomenon, we isolated several proteins and genes that are expressed in vanadocytes. To date, three types of vanadium-binding protein, designated as Vanabins, have been isolated, with molecular masses of 12.5, 15, and 16 kDa, along with the cDNAs encoding these proteins. In addition, four types of enzyme related to the pentose phosphate pathway that produces NADPH were revealed to be located in vanadocytes. The pentose phosphate pathway participates in the reduction of vanadium(V) to vanadium(IV). The cDNA for each of the vacuolar-type H+-ATPase (V-ATPase) A, B, C, and D subunits, which are located on the vacuolar membranes of vanadocytes, has been isolated and analyzed. V-ATPase generates a proton-motive force, and is thought to provide the energy for vanadium accumulation.To clarify the entire mechanism involved in the accumulation and reduction, much more genes and proteins expressed in the blood cells need to be systematically identified. Thus, we have performed an expressed sequence tag (EST) analysis of blood cells and have established the functional assay system to elucidate the functions of genes and proteins obtained from ascidian blood cells