Glutathione transferases with vanadium-binding activity isolated from the vanadium-rich ascidian Ascidia sydneiensis samea |
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Authors: | Masafumi Yoshinaga Tatsuya Ueki Nobuo Yamaguchi Kei Kamino Hitoshi Michibata |
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Affiliation: | 1. Molecular Physiology Laboratory, Graduate School of Science, Hiroshima University, Kagamiyama 1-3-1, Higashi-Hiroshima 739-8526, Japan;2. Marine Biological Laboratory, Graduate School of Science, Hiroshima University, Mukaishima 2445, Hiroshima 722-0073, Japan;3. Marine Biotechnology Institute Co, Ltd., 3-75-1 Heita, Kamaishi City, Iwate 026-0001, Japan |
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Abstract: | Some ascidians accumulate vanadium in vanadocytes, which are vanadium-containing blood cells, at high levels and with high selectivity. However, the mechanism and physiological significance of vanadium accumulation remain unknown. In this study, we isolated novel proteins with a striking homology to glutathione transferases (GSTs), designated AsGST-I and AsGST-II, from the digestive system of the vanadium-accumulating ascidian Ascidia sydneiensis samea, in which the digestive system is thought to be involved in vanadium uptake. Analysis of recombinant AsGST-I confirmed that AsGST-I has GST activity and forms a dimer, as do other GSTs. In addition, AsGST-I was revealed to have vanadium-binding activity, which has never been reported for GSTs isolated from other organisms. AsGST-I bound about 16 vanadium atoms as either V(IV) or V(V) per dimer, and the apparent dissociation constants for V(IV) and V(V) were 1.8 × 10−4 M and 1.2 × 10−4 M, respectively. Western blot analysis revealed that AsGSTs were expressed in the digestive system at exceptionally high levels, although they were localized in almost all organs and tissues examined. Considering these results, we postulate that AsGSTs play important roles in vanadium accumulation in the ascidian digestive system. |
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Keywords: | Ascidian Vanadium Metal accumulation Digestive system Glutathione transferase |
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