Sulfated Metabolites of Polychlorinated Biphenyls Are High-Affinity Ligands for the Thyroid Hormone Transport Protein Transthyretin | Zendy

Fabian A. Grimm | Zendy; HansJoachim Lehmler | Zendy; Xianran He | Zendy; Larry W. Robertson | Zendy; Michael W. Duffel | Zendy

Open Access

Sulfated Metabolites of Polychlorinated Biphenyls Are High-Affinity Ligands for the Thyroid Hormone Transport Protein Transthyretin

Author(s) -

Fabian A. Grimm,

HansJoachim Lehmler,

Xianran He,

Larry W. Robertson,

Michael W. Duffel

Publication year - 2013

Publication title -

environmental health perspectives

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.257

H-Index - 282

eISSN - 1552-9924

pISSN - 0091-6765

DOI - 10.1289/ehp.1206198

Subject(s) - chemistry , transthyretin , sulfation , binding site , sulfotransferase , docking (animal) , plasma protein binding , biochemistry , biphenyl , stereochemistry , organic chemistry , medicine , nursing

The displacement of l-thyroxine (T4) from binding sites on transthyretin (TTR) is considered a significant contributing mechanism in polychlorinated biphenyl (PCB)-induced thyroid disruption. Previous research has discovered hydroxylated PCB metabolites (OH-PCBs) as high-affinity ligands for TTR, but the binding potential of conjugated PCB metabolites such as PCB sulfates has not been explored.

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