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

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dc.citation.issue1
dc.citation.volume60
dc.contributor.authorXavier, Ana Carolina W. [UNIFESP]
dc.contributor.authorMaciel, Rui M. B. [UNIFESP]
dc.contributor.authorVieira, Jose Gilberto H. [UNIFESP]
dc.contributor.authorDias-da-Silva, Magnus R. [UNIFESP]
dc.contributor.authorMartins, Joao R. M. [UNIFESP]
dc.coverageRio De Janeiro, Rj
dc.date.accessioned2020-08-21T17:00:25Z
dc.date.available2020-08-21T17:00:25Z
dc.date.issued2016
dc.description.abstractThyroglobulin (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.en
dc.description.affiliationUniv Fed Sao Paulo EPM Unifesp, Escola Paulista Med, Lab Endocrinol Mol & Translac, Div Endocrinol & Metab,Dept Med, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Mato Grosso do Sul UFMS, Fac Med Famed, Dept Med, Clin Integrada 5,Endocrinol & Metab, Campo Grande, MS, Brazil
dc.description.affiliationUniv Fed Sao Paulo, EPM, Dept Bioquim, Div Mol Biol, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo EPM Unifesp, Escola Paulista Med, Lab Endocrinol Mol & Translac, Div Endocrinol & Metab,Dept Med, Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, EPM, Dept Bioquim, Div Mol Biol, Sao Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFapesp
dc.description.sponsorshipCNPq
dc.description.sponsorshipCapes
dc.format.extent66-75
dc.identifierhttp://dx.doi.org/10.1590/2359-3997000000103
dc.identifier.citationArchives Of Endocrinology Metabolism. Rio De Janeiro, Rj, v. 60, n. 1, p. 66-75, 2016.
dc.identifier.doi10.1590/2359-3997000000103
dc.identifier.fileS2359-39972016000100066-en.pdf
dc.identifier.issn2359-3997
dc.identifier.scieloS2359-39972016000100066
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/57991
dc.identifier.wosWOS:000378602500013
dc.language.isoeng
dc.publisherSbem-Soc Brasil Endocrinologia & Metabologia
dc.relation.ispartofArchives Of Endocrinology Metabolism
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectThyroglobulinen
dc.subjectposttranslational protein modificationsen
dc.subjectheterogeneityen
dc.subjectthyroid diseasesen
dc.titleInsights into the posttranslational structural heterogeneity of thyroglobulin and its role in the development, diagnosis, and management of benign and malignant thyroid diseasesen
dc.typeinfo:eu-repo/semantics/article
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