Glutathione transferases with vanadium-binding activity isolated from the vanadium-rich ascidian Ascidia sydneiensis samea

Biochimica et Biophysica Acta - General Subjects Volume 1760 Issue 3 Page 495-503 published_at 2006-03
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Title ( eng )
Glutathione transferases with vanadium-binding activity isolated from the vanadium-rich ascidian Ascidia sydneiensis samea
Creator
Yoshinaga Masafumi
Yamaguchi Nobuo
Kamino Kei
Michibata Hitoshi
Source Title
Biochimica et Biophysica Acta - General Subjects
Volume 1760
Issue 3
Start Page 495
End Page 503
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.
Keywords
Ascidian
Digestive system
Glutathione transferase
Metal accumulation
Vanadium
NDC
Biology [ 460 ]
Language
eng
Resource Type journal article
Publisher
Elsevier B.V.
Date of Issued 2006-03
Rights
Copyright (c) 2006 Elsevier B.V.
Publish Type Author’s Original
Access Rights open access
Source Identifier
[ISSN] 0304-4165
[DOI] 10.1016/j.bbagen.2006.01.008
[PMID] 16503380
[NCID] AA00564679
[DOI] http://dx.doi.org/10.1016/j.bbagen.2006.01.008 isVersionOf