Scanning X-ray Microscopy of Living and Freeze-Dried Blood Cells in Two Vanadium-Rich Ascidian Species, Phallusia mammillata and Ascidia sydneiensis samea

Ueki, Tomoyuki; Takemoto, Kuniko; Fayard, Barbara; Salomé, Murielle; Yamamoto, Akira; Kihara, Hiroshi; Susini, J.; Scippa, Silvia; Uyama, Takeshi; Michibata, Hitoshi

doi:10.2108/zsj.19.27

Cited by 44 publications

(33 citation statements)

References 27 publications

(29 reference statements)

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“…The biologically unique highly acidic intracellular vacuolar aqua vanadium (III, IV) solutions, concentrated primarily in so-called signet ring blood cells, has been successfully described [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22]. Biologically exotic intracellular V(III) and V(IV) complexes have also been detected in high concentrations with blood cells from Phallusia nigra [19], as well as possibly V(III,IV) micro-granules within the blood cells of Ascidia sydneiensis samea [23].…”

Section: Nih-pa Author Manuscriptmentioning

confidence: 99%

The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopic study

Frank

Carlson²,

Carlson³

et al. 2008

Journal of Inorganic Biochemistry

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Vanadium K-edge x-ray absorption spectroscopy (XAS) has been used to track the uptake and fate of VO 2+ ion in blood cells from Ascidia ceratodes, following exposure to dithiothreitol (DTT) or to DTT plus VO 2+ . The full range of endogenous vanadium was queried by fitting the XAS of blood cells with the XAS spectra of model vanadium complexes. In cells exposed only to DTT, ~0.4% of a new V(III) species was found in a site similar to Na[V(edta)(H 2 O)]. With exposure to DTT and VO 2+ , average intracellular [VO(aq)] 2+ increased from 3% to 5%, and 6% of a new complexed form of vanadyl ion appeared evidencing a ligand array similar to [VO(edta)] 2− . At the same time, the relative ratio of blood cell [V(H 2 O) 6 ] 3+ increased at the expense of [V(H 2 O) 5 (SO 4 )] + in a manner consistent with a significant increase in endogenous acidity. In new UV/visible experiments, VO 2+ could be reduced to 7-coordinate [V(nta)(H 2 O) 3 ] or [V(nta)(ida)] 2− with cysteine methyl ester in pH 6.5 solution. Ascorbate reduced [VO(edta)] 2− to 7-coordinate [V(edta)(H 2 O)] − , while [VO (trdta)] 2− was unreactive. These results corroborate the finding that the reductive EMF of VO 2+ is increased by the availability of a 7-coordinate V(III) product. Finally a new and complete hypothesis is proposed for an ascidian vanadate reductase. The structure of the enzyme active site, the vanadatevanadyl-vanadic reduction mechanism, the cellular locale, and elements of the regulatory machinery governing the biological reduction of vanadate and vanadyl ion by ascidians are all predicted. Together these constitute the new field of vanadium redox enzymology.Phlebobranch ascidians (tunicates) are vanadium-concentrating, filter-feeding marine Urochordates that have a continuous evolutionary history reaching back into the upper Cambrian [1][2][3][4]. Although vanadium in ascidian blood cells has been under active investigation for almost 100 years [5][6][7], the mechanisms of uptake, transport, and reduction of oceanic © 2008 Elsevier Inc. All rights reserved.Contact Information: Dr. Patrick Frank, Tel: 1-650-723-2479, Fax: 1-650-723-4817, frank@ssrl.slac.stanford.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. NIH Public Access NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author Manuscript vanadate remain largely unknown. The biologically unique highly acidic intracellular vacuolar aqua vanadium (III, IV) solutions, concentrated primarily in so-called signet ring blood cells, has been successfully described [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22]. Biologically ex...

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Section: Nih-pa Author Manuscriptmentioning

confidence: 99%

The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopic study

Frank

Carlson²,

Carlson³

et al. 2008

Journal of Inorganic Biochemistry

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“…Most of the vanadium ions accumulated in ascidians are ultimately localized in the vacuoles of vanadocytes [5]. However, the mechanism by which these ions are taken in before entry into these cells has not been completely determined.…”

Section: Discussionmentioning

confidence: 99%

“…Vanadium is usually found in the +5 oxidation state (HVO 4 2− or H 2 VO 4 − ; V V ) in the natural aquatic environment, but most of these ions are reduced to +3 (V 3+ ; V III ) via the +4 state (VO 2+ ; V IV ) during assimilation [2,3]. Additionally, most vanadium ions are stored in the vacuoles of signet ring cells, a type of blood cell, and are often referred to as vanadocytes [4,5].…”

Section: Introductionmentioning

confidence: 99%

Metal-binding domains and the metal selectivity of the vanadium(IV)-binding protein VBP-129 in blood plasma

Ueki

Nakagawa

Michibata

2012

Journal of Inorganic Biochemistry

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Ascidians are well known to accumulate extremely high levels of vanadium in their blood cells. Several key proteins related to vanadium accumulation and physiological function have been isolated from vanadium-rich ascidians. Of these, vanadium(IV)-binding protein-129 (VBP-129) is a unique protein that has been identified from the blood plasma of an ascidian Ascidia sydneiensis samea, but its metal binding domains are not known. In this study, several deletion and point mutants of VBP-129 were generated, and their metal binding abilities were assessed by immobilized metal ion affinity chromatography (IMAC) and electron spin resonance spectroscopy (ESR). The internal partial protein, VBP-Int41, did not bind to V(IV), but the two constructs, VBP-N52 and VBP-Int55, added with additional 11 or 14 neighboring amino acids bound to V(IV). Mutations for cysteine-47 and lysine-50 in VBP-Int55 diminished V(IV)-binding in VBP-Int55, suggesting that these amino acid residues play important roles in binding V(IV). ESR titration analysis revealed that VBP-129, VBP-N52 and VBP-Int55 could bind to 6, 3 and 2 V(IV) ions, respectively. ESR spectrum analysis indicated a N(2)O(2) coordination geometry, which is similar to vanabins. The cysteines may contribute to the maintenance of the three-dimensional structure that is necessary for binding V(IV) ions. VBP-129 did not have a V(V)-reductase activity, as expected from its tissue localization in blood plasma. This study provided the evidences that VBP-129 possesses V(IV)-binding domains that make a similar coordination to V(IV) as those by vanabins but VBP-129 acts solely as a V(IV)-chaperon in blood plasma.

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“…The high spatial resolution focusing, combined with spectroscopic methods in the multi-keV range, has been demonstrated in a number of experiments from diverse fields. Sulfur [8][9][10], Calcium [11], Vanadium [12], Chromium [13], and Iron [14] K-edges are the most requested edges/lines. The reduction of air absorption by using the scanning microscope in secondary vacuum is a clear asset for energies below 4 keV.…”

Section: Esrf-id2x-ray Microscopy Beamlinementioning

confidence: 99%

Synchrotron X-Ray Microfluorescence and Microspectroscopy: Application and Perspectives in Materials Science

Bohic

Simionovici

Biquard³

et al. 2005

Oil & Gas Science and Technology - Rev. IFP

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Scanning X-ray Microscopy of Living and Freeze-Dried Blood Cells in Two Vanadium-Rich Ascidian Species, Phallusia mammillata and Ascidia sydneiensis samea

Cited by 44 publications

References 27 publications

The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopic study

The uptake and fate of vanadyl ion in ascidian blood cells and a detailed hypothesis for the mechanism and location of biological vanadium reduction. A visible and X-ray absorption spectroscopic study

Metal-binding domains and the metal selectivity of the vanadium(IV)-binding protein VBP-129 in blood plasma

Synchrotron X-Ray Microfluorescence and Microspectroscopy: Application and Perspectives in Materials Science

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