Document Detail

Correlation between the loss of thyroglobulin iodination and the expression of thyroid-specific proteins involved in iodine metabolism in thyroid carcinomas.
MedLine Citation:
PMID:  14557483     Owner:  NLM     Status:  MEDLINE    
Progress in biotechnology has provided useful tools for tracing proteins involved in thyroid hormone synthesis in vivo. Mono- or polyclonal antibodies are now available to detect on histological sections the Na(+)/I(-) symporter (NIS) at the basolateral pole of the cell, the putative iodide channel (pendrin) at the apical plasma membrane, thyroperoxidase (TPO), and members of the NADPH-oxidase family, thyroid oxidase 1 and 2 (ThOXs), part of the H(2)O(2)-generating system. The aim of this study was to correlate thyroglobulin (Tg) iodination with the presence of these proteins. Tg, T(4)-containing Tg, NIS, pendrin, TPO, ThOXs, and TSH receptor (TSHr) were detected by immunohistochemistry on tissue sections of normal thyroids and various benign and malignant thyroid disorders. Tg was present in all cases. T(4)-containing Tg was found in the adenomas, except in Hurthle cell adenomas. It was never detected in carcinomas. NIS was reduced in all types of carcinomas, whereas it was detected in noncancerous tissues. Pendrin was not expressed in carcinomas, except in follicular carcinomas, where weak staining persisted. TPO expression was present in insular, follicular carcinomas and in follicular variants of papillary carcinomas, but in a reduced percentage of cells. It was below the level of detection in papillary carcinomas. The H(2)O(2)-generating system, ThOXs, was found in all carcinomas and was even increased in papillary carcinomas. Its staining was apical in normal thyroids, whereas it was cytoplasmic in carcinomas. The TSHr was expressed in all cases, but the intensity of the staining was decreased in insular carcinomas. In conclusion, our work shows that all types of carcinomas lose the capacity to synthesize T(4)-rich, iodinated Tg. In follicular carcinomas, this might be due to a defect in iodide transport at the basolateral pole of the cell. In papillary carcinomas, this defect seems to be coupled to an altered apical transport of iodide and probably TPO activity. The TSHr persists in virtually all cases.
A-C Gérard; C Daumerie; C Mestdagh; S Gohy; C De Burbure; S Costagliola; F Miot; M-C Nollevaux; J-F Denef; J Rahier; B Franc; J J M De Vijlder; I M Colin; M-C Many
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of clinical endocrinology and metabolism     Volume:  88     ISSN:  0021-972X     ISO Abbreviation:  J. Clin. Endocrinol. Metab.     Publication Date:  2003 Oct 
Date Detail:
Created Date:  2003-10-14     Completed Date:  2003-11-12     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0375362     Medline TA:  J Clin Endocrinol Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4977-83     Citation Subset:  AIM; IM    
Histology, Université Catholique de Louvain Medical School, B-1070 Brussels, Belgium.
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MeSH Terms
Biological Markers
Carcinoma, Papillary / metabolism*,  pathology
Carrier Proteins / metabolism
Flavoproteins / metabolism
Goiter / metabolism*,  pathology
Iodide Peroxidase / metabolism
Iodine / metabolism*
Membrane Transport Proteins*
NADPH Oxidase*
Receptors, Thyrotropin / metabolism
Symporters / metabolism
Thyroglobulin / metabolism*
Thyroid Neoplasms / metabolism*,  pathology
Thyroxine / metabolism
Reg. No./Substance:
0/Biological Markers; 0/Carrier Proteins; 0/Flavoproteins; 0/Membrane Transport Proteins; 0/Receptors, Thyrotropin; 0/SLC26A4 protein, human; 0/Symporters; 0/sodium-iodide symporter; 7488-70-2/Thyroxine; 7553-56-2/Iodine; 9010-34-8/Thyroglobulin; EC Peroxidase; EC protein, human; EC protein, human; EC Oxidase

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