Deiodinases: How Nonmammalian Research Helped Shape Our Present View

In relation to their structure, we discovered for instance that biochemical properties such as inhibition by 6-propyl-2-thiouracil, stimulation by dithiothreitol, and temperature optimum are subject to variation

Veerle M Darras

2021

Scholarcy highlights

  • Iodothyronine deiodinases are enzymes capable of activating and inactivating thyroid hormones and have an important role in regulatingTH action in tissues throughout the body
  • Over the years, increasing genomic information revealed that deiodinases are present in all chordates, vertebrates, and nonvertebrates and that they can even be found in some mollusks and annelids, pointing to an ancient origin
  • In relation to their structure, we discovered for instance that biochemical properties such as inhibition by 6-propyl-2-thiouracil, stimulation by dithiothreitol, and temperature optimum are subject to variation
  • With the present possibilities for rapid and precise gene silencing in any species of interest, comparative research will certainly further contribute to a better understanding of the importance of deiodinases for adequateTH action, in humans
  • Twelve years later an in vitro study in different tissues of hagfish showed the presence of T4 outer ring deiodination, T4 inner ring deiodination, and T3 IRD activities. Both ORD and IRD of T4 in hagfish were inhibited by PTU, suggesting this primitive chordate, situated in the evolutionary tree just before the transition to vertebrates, expresses a deiodinase type 1-like deiodinase that is PTU-sensitive
  • It is clear that comparative research has broadened our view on the impact of these important enzymes on TH action throughout life
  • With the present possibilities for rapid and precise gene silencing in any species of interest, it will continue to do so in the future

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