Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation

Yumi Abiko, Eiko Yoshida, Isao Ishii, Jon M. Fukuto, Takaaki Akaike, Yoshito Kumagai

研究成果: Article

29 引用 (Scopus)

抄録

Bismethylmercury sulfide (MeHg)<inf>2</inf>S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)<inf>2</inf>S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H<inf>2</inf>S or HS<sup>-</sup>), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)<inf>2</inf>S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na<inf>2</inf>S<inf>4</inf> react readily with MeHg to give (MeHg)<inf>2</inf>S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)<inf>2</inf>S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)<inf>2</inf>S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)<inf>2</inf>S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.

元の言語English
ページ(範囲)1301-1306
ページ数6
ジャーナルChemical Research in Toxicology
28
発行部数6
DOI
出版物ステータスPublished - 2015 6 15

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Sulfides
Cystathionine
Liver
Lyases
Sulfur
Proteins
Glutathione S-Transferase pi
Atomic Spectrophotometry
Hydrogen Sulfide
Column chromatography
Spectrophotometry
Metabolites
Knockout Mice
Chromatography
Rats
High Pressure Liquid Chromatography
Tissue
persulfides
cysteine persulfide

ASJC Scopus subject areas

  • Toxicology

これを引用

Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation. / Abiko, Yumi; Yoshida, Eiko; Ishii, Isao; Fukuto, Jon M.; Akaike, Takaaki; Kumagai, Yoshito.

:: Chemical Research in Toxicology, 巻 28, 番号 6, 15.06.2015, p. 1301-1306.

研究成果: Article

Abiko, Y, Yoshida, E, Ishii, I, Fukuto, JM, Akaike, T & Kumagai, Y 2015, 'Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation', Chemical Research in Toxicology, 巻. 28, 番号 6, pp. 1301-1306. https://doi.org/10.1021/acs.chemrestox.5b00101
Abiko, Yumi ; Yoshida, Eiko ; Ishii, Isao ; Fukuto, Jon M. ; Akaike, Takaaki ; Kumagai, Yoshito. / Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation. :: Chemical Research in Toxicology. 2015 ; 巻 28, 番号 6. pp. 1301-1306.
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abstract = "Bismethylmercury sulfide (MeHg)2S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)2S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H2S or HS-), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)2S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na2S4 react readily with MeHg to give (MeHg)2S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)2S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)2S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)2S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.",
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T1 - Involvement of Reactive Persulfides in Biological Bismethylmercury Sulfide Formation

AU - Abiko, Yumi

AU - Yoshida, Eiko

AU - Ishii, Isao

AU - Fukuto, Jon M.

AU - Akaike, Takaaki

AU - Kumagai, Yoshito

PY - 2015/6/15

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N2 - Bismethylmercury sulfide (MeHg)2S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)2S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H2S or HS-), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)2S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na2S4 react readily with MeHg to give (MeHg)2S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)2S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)2S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)2S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.

AB - Bismethylmercury sulfide (MeHg)2S has been found to be a detoxified metabolite of methylmercury (MeHg) that is produced by SH-SY5Y cells and in livers of rats exposed to MeHg. (MeHg)2S could be formed through the interactions between MeHg and sulfur species such as hydrogen sulfide (H2S or HS-), but the origin of its sulfur has not been fully identified. We herein examined the formation of (MeHg)2S through interactions between MeHg and persulfides, polysulfides, and protein preparations. Investigations using HPLC/atomic absorption spectrophotometry and EI-MS revealed that NaHS and Na2S4 react readily with MeHg to give (MeHg)2S, and similar results were found using GSH persulfide (GSSH) formed endogenously or generated enzymatically in vitro. (MeHg)2S was also formed by incubation of MeHg with liver and heart cytosolic fractions prepared from wild-type mice but not with those from mice lacking cystathionine γ-lyase (CSE) that catalyzes the formation of cysteine persulfide. Consistent with this, (MeHg)2S was detected in a variety of tissues taken from wild-type mice intraperitoneally injected with MeHg in vivo but not in those from MeHg-injected CSE knockout mice. By separating liver fractions by column chromatography, we found numerous proteins that contain persulfides: one of the proteins was identified as being glutathione S-transferase pi 1. These results indicate that the formation of (MeHg)2S can be attributed to interactions between MeHg and endogenous free persulfide species, as well as protein-bound cysteine persulfide.

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