Experimental conditions leading to a low degree of thyroglobulin iodination without loss in coupling efficiency.
The hormone content of in vitro iodinated thyroglobulin is a constant fraction of the iodine content of the protein under most, but not all, experimental conditions. In contrast, in vivo iodinated human thyroglobulin may contain as little as 10% or as much as 50% of its total iodine in the T4 molecules. Surprisingly, in some poorly iodinated thyroglobulins up to 30% of the iodine may be found in T4. The mechanism of the apparent dissociation between iodination and coupling efficiency (i.e. percentage of total iodine present as iodothyronines) may be dilution of pre-existing high iodinated thyroglobulin stores by non-iodinated prethyroglobulin. This hypothesis was tested by feeding rate PTU and KClo4 for 9 days and injecting T4 during the last 2 days. Thyroglobulin iodination dropped from 0.9 ot 0.13% but the coupling efficiency remained unchanged at 25.7 and 23.9%. The exchange of highly iodinated thyroglobulin molecules for non-iodinated ones is one of the two in vivo mechanisms suggested so far which can lead to an apparent dissociation of thyroglobulin iodination and coupling efficiency.
D000818:Animals; D005260:Female; D007455:Iodine / Q000378:metabolism*; D010281:Parathyroid Hormone / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D011919:Rats, Inbred Strains; D013954:Thyroglobulin / Q000378:metabolism*; D013974:Thyroxine / Q000096:biosynthesis
D010281:Parathyroid Hormone; D013954:Thyroglobulin; D007455:Iodine; D013974:Thyroxine; D011188:Potassium