IMR Press / FBL / Volume 24 / Issue 2 / DOI: 10.2741/4714

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

Open Access Article
Thyroid hormone binding motifs and iodination pattern of thyroglobulin
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1 Department of Clinical and Experimental Medicine - Endocrinology, University of Messina, via Consolare Valeria, Gazzi, 98125 Messina, Italy
2 Master Program on Childhood, Adolescent and Women's Endocrine Health, University of Messina, via Consolare Valeria, Gazzi, 98125 Messina, Italy
3 Interdepartmental Program on Molecular and Clinical Endocrinology and Women's Endocrine Health, AOU Policlinico G. Martino, via Consolare Valeria, Gazzi, 98125 Messina, Italy
4 Department of Clinical and Experimental Medicine, Dermatology, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy
*Correspondence: f.guarneri@tiscali.it (Fabrizio Guarneri)
Front. Biosci. (Landmark Ed) 2019, 24(2), 212–230; https://doi.org/10.2741/4714
Published: 1 January 2019
(This article belongs to the Special Issue Digging deep into thyroid pathophysiology)
Abstract

A phylogenetically conserved 5-residue thyroid hormone (TH)- binding motif was originally found in a few TH plasma carriers and, more recently, in all known plasma and cell-associated proteins interacting with TH as well as in proteins involved in iodide uptake. Minor variations of the motif were found, depending on the particular class of those proteins. Since thyroglobulin (Tg) is the protein matrix for TH synthesis starting from iodination of a selected number of tyrosines (to form first monoiodotyrosine (MIT) and diiodotyrosine (DIT) and then T3 and T4), we hypothesized that by searching the presence of perfect or imperfect versions of that motif in two Tg species (human and murine) in which the iodinated tyrosines and pattern of iodotyrosine/iodothyronine formation are known, we could have found relevant explanations. Explanations, which are not furnished by the simple possession of tyrosine-iodination motifs and sequence of the iodination motif, concern why only some (but not other) tyrosine residues in one species are iodinated and why they have a particular iodination pattern. In this bioinformatics study, we provide such explanations.

Keywords
Thyroglobulin
Monoiodotyrosine
Diiodotyrosine
Iodination
Thyroid hormones
Congenital hypothyroidism
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