Recombinant albumin and transthyretin transport proteins from two gull species and human: chlorinated and brominated contaminant binding and thyroid hormones.

Environmentally relevant concentrations of selected polychlorinated biphenyl (PCB) and polybrominated diphenyl ether (PBDE) flame retardant congeners and their hydroxylated (OH) and methoxylated (MeO) analogues that can perturb thyroid hormone-dependent processes were comparatively examined with respect to competitive binding with thyroxine (T(4)) and 3,5,3'-triiodothyronine (T(3)) thyroid hormones (THs) on recombinant human and gull albumin and transthyretin transport proteins. The liver tissue was from glaucous gulls (Larus hyperboreus) from Norway and herring gulls (Larus argentatus) from the Great Lakes of North America. We isolated, cloned, sequenced, purified, and expressed the cDNA (cDNA) of albumin from liver of herring and glaucous gull.

Recombinant transthyretin purification and competitive binding with organohalogen compounds in two gull species (Larus argentatus and Larus hyperboreus).

Glaucous gulls (Larus hyperboreus) from Svalbard, Norway (marine), and herring gulls (Larus argentatus) from the Laurentian Great Lakes (freshwater) of North America are differentially exposed to persistent and bioaccumulative anthropogenic contaminants, such as polychlorinated biphenyls (PCBs) and polybrominated diphenyl ether (PBDE) flame retardants and metabolic products. Such compounds can potentially perturb hormone transport via binding interactions with proteins such as transthyretin (TTR, prealbumin). In this present study, we isolated, cloned and sequenced TTR cDNA from the brain and liver of two species (herring and glaucous gull), which, to our knowledge, is the first report describing the TTR nucleic acid and amino acid sequences from any gull species.