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Related Experiment Videos

Thyroid hormone deiodination in fish.

Aurea Orozco1, Carlos Valverde-R

  • 1Laboratorio de Fisiología Evolutiva, Instituto de Neurobiología, Campus UNAM-UAQ, Juriquilla, Querétaro, México. aureao@servidor.unam.mx

Thyroid : Official Journal of the American Thyroid Association
|September 1, 2005
PubMed
Summary

This review explores fish iodothyronine deiodinases (IDs), crucial for thyroid hormone (TH) activity. Fish IDs show unique traits, like PTU-resistant ID1 and high liver ID2 activity in teleosts.

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Area of Science:

  • Endocrinology
  • Comparative Physiology
  • Molecular Biology

Background:

  • Iodothyronine deiodinases (IDs) are critical enzymes regulating thyroid hormone (TH) bioactivity.
  • Understanding fish IDs is essential for comprehending TH action in diverse vertebrate species.

Purpose of the Study:

  • To review experimental evidence on piscine iodothyronine deaminases (IDs) over the last decade.
  • To characterize the physiology, biochemistry, and molecular aspects of fish IDs.

Main Methods:

  • Literature review of experimental evidence on fish IDs.
  • Comparative analysis of ID1, ID2, and ID3 isotypes across agnathans, chondrichthyes, and teleosts.

Main Results:

  • All major fish groups express ID1, ID2, and ID3, fine-tuning TH bioactivity.
  • Teleostean ID1 exhibits propylthiouracil (PTU) resistance and unique thyroidal status response.
  • Teleosts uniquely display high ID2 activity and liver expression among vertebrates.

Conclusions:

  • Fish IDs share conserved properties with other vertebrates but possess distinct piscine features.
  • IDs likely play a tissue-specific role in coordinating iodothyronine and other hormone actions in fish.
  • The precise physiological role of iodothyronine deiodination in TH-regulated functions in fish requires further elucidation.

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