Insights into the posttranslational structural heterogeneity of thyroglobulin and its role in the development, diagnosis, and management of benign and malignant thyroid diseases

Insights into the posttranslational structural heterogeneity of thyroglobulin and its role in the development, diagnosis, and management of benign and malignant thyroid diseases

Author Xavier, Ana Carolina W. Autor UNIFESP Google Scholar
Maciel, Rui M. B. Autor UNIFESP Google Scholar
Vieira, Jose Gilberto H. Autor UNIFESP Google Scholar
Dias-da-Silva, Magnus R. Autor UNIFESP Google Scholar
Martins, Joao R. M. Autor UNIFESP Google Scholar
Abstract Thyroglobulin (Tg) is the major glycoprotein produced by the thyroid gland, where it serves as a template for thyroid hormone synthesis and as an intraglandular store of iodine. Measurement of Tg levels in serum is of great practical importance in the follow-up of differentiated thyroid carcinoma (DTC), a setting in which elevated levels after total thyroidectomy are indicative of residual or recurrent disease. The most recent methods for serum Tg measurement are monoclonal antibody-based and are highly sensitive. However, major challenges remain regarding the interpretation of the results obtained with these immunometric methods, particularly in patients with endogenous antithyroglobulin antibodies or in the presence of heterophile antibodies, which may produce falsely low or high Tg values, respectively. The increased prevalence of antithyroglobulin antibodies in patients with DTC, as compared with the general population, raises the very pertinent possibility that tumor Tg may be more immunogenic. This inference makes sense, as the tumor microenvironment (tumor cells plus normal host cells) is characterized by several changes that could induce posttranslational modification of many proteins, including Tg. Attempts to understand the structure of Tg have been made for several decades, but findings have generally been incomplete due to technical hindrances to analysis of such a large protein (660 kDa). This review article will explore the complex structure of Tg and the potential role of its marked heterogeneity in our understanding of normal thyroid biology and neoplastic processes.
Keywords Thyroglobulin
posttranslational protein modifications
heterogeneity
thyroid diseases
xmlui.dri2xhtml.METS-1.0.item-coverage Rio De Janeiro, Rj
Language English
Sponsor Fapesp
CNPq
Capes
Date 2016
Published in Archives Of Endocrinology Metabolism. Rio De Janeiro, Rj, v. 60, n. 1, p. 66-75, 2016.
ISSN 2359-3997 (Sherpa/Romeo, impact factor)
Publisher Sbem-Soc Brasil Endocrinologia & Metabologia
Extent 66-75
Origin http://dx.doi.org/10.1590/2359-3997000000103
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000378602500013
SciELO ID S2359-39972016000100066 (statistics in SciELO)
URI https://repositorio.unifesp.br/handle/11600/57991

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