Recombinant Albumin and Transthyretin Transport Proteins from Two Gull Species and Human: Chlorinated and Brominated Contaminant Binding and Thyroid Hormones
Why this work is in the frame
A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.
Bibliographic record
Abstract
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. Albumin amino acid sequences were identical for both gull species. Concentration-dependent, competitive binding curves were generated for T(4) and T(3) binding alone and for selected substrates using gull and human recombinant albumin (recALB). Human recALB had high preference for T(4) relative to T(3), whereas it was reversed for gull recALB. Binding assays with recALB and recTTR gull proteins showed that relative to 2,2',4,4'-tetrabromoDE (BDE-47) and 2,2',3,4',5,5',6-heptaCB (CB-187) and the MeO-substituted (4-MeO-CB187 and 6-MeO-BDE47) analogues, 4-OH-CB187, 6-OH-BDE47, and 4'-OH-BDE49 had the greatest binding affinity and potency, and that competitive binding was greater for T(3) relative to T(4). These results indicate that xenobiotic ligand binding to human ALB or TTR cannot be used as a surrogate for gull binding interactions. The combination of TH-like brominated diphenyl ether backbone (relative to the chlorinated biphenyl backbone), and the presence of OH-group produced a more effective competitive ligand on human and gull recALB and recTTR relative to both T(3) and T(4). This suggests the possibility that OH-substituted organohalogen contaminants may be an exposure concern to the thyroid system in free-ranging gulls as well as for humans.
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Full frame distilled prediction
Teacher imitationNot calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.
Codex and Gemma teacher scores by category
| Category | Codex | Gemma |
|---|---|---|
| Metaresearch | 0.000 | 0.000 |
| Meta-epidemiology (narrow) | 0.000 | 0.000 |
| Meta-epidemiology (broad) | 0.000 | 0.000 |
| Bibliometrics | 0.000 | 0.000 |
| Science and technology studies | 0.000 | 0.002 |
| Scholarly communication | 0.000 | 0.000 |
| Open science | 0.000 | 0.000 |
| Research integrity | 0.000 | 0.000 |
| Insufficient payload (model declined to judge) | 0.000 | 0.000 |
Machine scores (provisional)
The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.
Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.
score_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it