| A coherent organization of differentiation proteins is required to maintain an appropriate thyroid function in the Pendred thyroid. | |
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MedLine Citation:
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PMID: 20501687 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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CONTEXT: Pendred syndrome is caused by mutations in the gene coding for pendrin, an apical Cl-/I- exchanger. OBJECTIVE: To analyze intrathyroidal compensatory mechanisms when pendrin is lacking, we investigated the thyroid of a patient with Pendred syndrome. The expression of proteins involved in thyroid hormone synthesis, markers of oxidative stress (OS), cell proliferation, apoptosis, and antioxidant enzymes were analyzed. RESULTS: Three morphological zones were identified: nearly normal follicles with iodine-rich thyroglobulin in the colloid (zone 1.a), small follicles without iodine-rich thyroglobulin in lumina (zone 1.b), and destroyed follicles (zone 2). In zones 1.a, dual oxidase (Duox) and thyroid peroxidase (TPO) were localized at the apical pole, OS and cell apoptosis were absent, but ClC-5 expression was strongly increased. In zones 1.b, Duox and TPO were aberrantly present and increased in the cytosol and associated with high OS, apoptosis, cell proliferation, and increased expression of peroxiredoxin-5, catalase, and dehalogenase-1 but moderate ClC-5 expression. CONCLUSION: In conclusion, the absence of pendrin is accompanied by increased ClC-5 expression that may transiently compensate for apical iodide efflux. In more affected follicles, Duox and TPO are relocated in the cytosol, leading to abnormal intracellular thyroid hormone synthesis, which results in cell destruction presumably because intracellular OS cannot be buffered by antioxidant defenses. |
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Authors:
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Maximin Senou; Céline Khalifa; Matthieu Thimmesch; François Jouret; Olivier Devuyst; Vincent Col; Jean-Nicolas Audinot; Pascale Lipnik; Jose C Moreno; Jacqueline Van Sande; Jacques E Dumont; Marie-Christine Many; Ides M Colin; Anne-Catherine Gérard |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-05-25 |
Journal Detail:
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Title: The Journal of clinical endocrinology and metabolism Volume: 95 ISSN: 1945-7197 ISO Abbreviation: J. Clin. Endocrinol. Metab. Publication Date: 2010 Aug |
Date Detail:
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Created Date: 2010-08-05 Completed Date: 2010-08-24 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0375362 Medline TA: J Clin Endocrinol Metab Country: United States |
Other Details:
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Languages: eng Pagination: 4021-30 Citation Subset: AIM; IM |
Affiliation:
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Unité de Morphologie Expérimentale, Université Catholique de Louvain, UCL-5251, 52 Avenue E. Mounier, B-1200 Brussels, Belgium. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Apoptosis
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genetics Blotting, Western Cell Proliferation Chloride Channels / genetics, metabolism Female Humans Immunohistochemistry Iodide Peroxidase / genetics, metabolism Membrane Transport Proteins / genetics*, metabolism Middle Aged NADPH Oxidase / genetics, metabolism Oxidative Stress / genetics Reverse Transcriptase Polymerase Chain Reaction Thyroid Function Tests Thyroid Gland / metabolism*, physiopathology |
| Chemical | |
Reg. No./Substance:
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0/CLC-5 chloride channel; 0/Chloride Channels; 0/Membrane Transport Proteins; 0/SLC26A4 protein, human; EC 1.11.1.8/Iodide Peroxidase; EC 1.6.3.1/DUOX1 protein, human; EC 1.6.3.1/NADPH Oxidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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