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Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species.

Publication ,  Journal Article
Roberts, SC; Noyes, PD; Gallagher, EP; Stapleton, HM
Published in: Environmental science & technology
March 2011

Previous studies have suggested that there may be species-specific differences in the metabolism of polybrominated diphenyl ethers (PBDEs) among different fish species. In this study, we investigated the in vitro hepatic metabolism of eleven individual PBDE congeners (tri- through decaBDEs) in three different fish species: rainbow trout (Oncorhynchus mykiss), common carp (Cyprinus carpio), and Chinook salmon (O. tschwatcha). In addition, we evaluated the influence of PBDE structural characteristics (i.e., bromine substitution patterns) on metabolism. Six of the eleven congeners we evaluated, BDEs 99, 153, 183, 203, 208, and 209, were metabolically debrominated to lower brominated congeners. All of the congeners that were metabolized contained at least one meta-substituted bromine. Metabolites were not detected for congeners without one meta-substituted bromine (e.g., BDEs 28, 47, and 100). Metabolite formation rates were generally 10 to 100 times faster in carp than in trout and salmon. BDEs 47, 49, 101, 154, and 183 were the major metabolites observed in all three species with the exception of BDE 47, which was only detected in carp. Carp demonstrated a preference toward meta-debromination, while trout and salmon debrominated meta- and para-bromine atoms to an equal extent. We compared glutathione-S-transferase (GST) and deiodinase (DI) activity among all three species as these enzyme systems have been hypothesized to play a role in PBDE debromination in teleosts. Carp exhibited a preference for meta-deiodination of the thyroid hormone thyroxine, which was consistent with the preference for meta-debromination of PBDEs observed in carp.

Duke Scholars

Published In

Environmental science & technology

DOI

EISSN

1520-5851

ISSN

0013-936X

Publication Date

March 2011

Volume

45

Issue

5

Start / End Page

1999 / 2005

Related Subject Headings

  • Water Pollutants, Chemical
  • Structure-Activity Relationship
  • Salmon
  • Oncorhynchus mykiss
  • Liver
  • Iodide Peroxidase
  • Halogenation
  • Halogenated Diphenyl Ethers
  • Glutathione Transferase
  • Flame Retardants
 

Citation

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MLA
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Roberts, S. C., Noyes, P. D., Gallagher, E. P., & Stapleton, H. M. (2011). Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species. Environmental Science & Technology, 45(5), 1999–2005. https://doi.org/10.1021/es103934x
Roberts, Simon C., Pamela D. Noyes, Evan P. Gallagher, and Heather M. Stapleton. “Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species.Environmental Science & Technology 45, no. 5 (March 2011): 1999–2005. https://doi.org/10.1021/es103934x.
Roberts SC, Noyes PD, Gallagher EP, Stapleton HM. Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species. Environmental science & technology. 2011 Mar;45(5):1999–2005.
Roberts, Simon C., et al. “Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species.Environmental Science & Technology, vol. 45, no. 5, Mar. 2011, pp. 1999–2005. Epmc, doi:10.1021/es103934x.
Roberts SC, Noyes PD, Gallagher EP, Stapleton HM. Species-specific differences and structure-activity relationships in the debromination of PBDE congeners in three fish species. Environmental science & technology. 2011 Mar;45(5):1999–2005.
Journal cover image

Published In

Environmental science & technology

DOI

EISSN

1520-5851

ISSN

0013-936X

Publication Date

March 2011

Volume

45

Issue

5

Start / End Page

1999 / 2005

Related Subject Headings

  • Water Pollutants, Chemical
  • Structure-Activity Relationship
  • Salmon
  • Oncorhynchus mykiss
  • Liver
  • Iodide Peroxidase
  • Halogenation
  • Halogenated Diphenyl Ethers
  • Glutathione Transferase
  • Flame Retardants