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• W2014648910 abstract "Previous results (Brouwer and van den Berg, Toxicol. Appl. Pharmacol., 85 (1986) 301) indicated preferential binding of a hydroxylated metabolite of tetrachlorobiphenyl to transthyretin (TTR) a carrier of thyroxine (T4). In the present study it was investigated whether the T4 binding site of TTR could be occupied specifically by hydroxylated chlorinated aromatic compounds using chlorinated phenol congeners as model compounds in a competition assay with [125I]T4. Chlorinated aromatics such as 2,3-dichlorobenzene and 3,4,3′,4′-tetrachlorobiphenyl, and phenols such as 4-hydroxybiphenyl and phenol were inefficient competitors. All chlorinated phenols tested were competitors for the T4 binding site of TTR. The ranking in competition was pentachlorophenol (PCP) > trichlorophenols > dichlorophenols > monochlorophenols. Structures with chlorine in both ortho positions to the hydroxyl group were more efficient competitiors. The relative affinity of binding of pentachlorophenol (PCP) to TTR was about twice that of T4. Scatchard analysis showed that PCP mainly decreased the affinity constant K11 while the binding capacity R1 was not altered, indicating a competitive type of inhibition. PCP was also able to compete with T4 sites on albumin with a relative affinity of 0.25. T4 binding to thyroid binding globulin (TBG) was much less affected by interference of PCP (relative affinity 0.001). The results indicate a specific interaction of chlorophenols with the T4 binding site of TTR." @default.
• W2014648910 created "2016-06-24" @default.
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• W2014648910 date "1990-01-01" @default.
• W2014648910 modified "2023-10-01" @default.
• W2014648910 title "Interaction of chlorinated phenols with thyroxine binding sites of human transthyretin, albumin and thyroid binding globulin" @default.
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• W2014648910 doi "https://doi.org/10.1016/0009-2797(90)90034-k" @default.
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