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Fas/Fas ligand up-regulation and Bcl-2 down-regulation may be significant in the pathogenesis of Hashimoto's thyroiditis.

TitleFas/Fas ligand up-regulation and Bcl-2 down-regulation may be significant in the pathogenesis of Hashimoto's thyroiditis.
Publication TypeJournal Article
Year of Publication1998
AuthorsMitsiades, N., Poulaki V., Kotoula V., Mastorakos G., Tseleni-Balafouta S., Koutras D. A., & Tsokos M.
JournalJ Clin Endocrinol Metab
Volume83
Issue6
Pagination2199-203
Date Published1998 Jun
ISSN0021-972X
KeywordsAdolescent, Adult, Apoptosis, Cross-Linking Reagents, Fas Ligand Protein, fas Receptor, Female, Humans, Male, Membrane Glycoproteins, Middle Aged, Proto-Oncogene Proteins c-bcl-2, Thyroid Gland, Thyroiditis, Autoimmune
Abstract

Hashimoto's thyroiditis (HT) is an autoimmune disorder characterized by diffuse thyroid lymphocytic infiltration and follicle destruction. Cross-linking of the Fas receptor with its own ligand (FasL) triggers apoptosis in various systems, whereas the Bcl-2 protooncogene inhibits apoptotic cell death. The involvement of Fas, FasL, and Bcl-2 in the apoptotic process in HT was evaluated in 15 thyroid tissue samples from patients with HT stained for apoptosis and for Fas, FasL, and Bcl-2 protein expression. Eight samples from healthy thyroid tissue were used for comparison. Thyroid follicles in HT samples exhibited strong staining for Fas and FasL and a high percentage of apoptosis (30.3 +/- 14.5%, mean +/- SD), in contrast to normal control follicles that exhibited moderate Fas, minimal or no FasL, and hardly any apoptosis. Immunostaining for Bcl-2 was high in normal, and weak in involved, thyroid follicles. Infiltrating lymphocytes stained weakly for FasL and strongly for Bcl-2. We conclude that follicular cells in HT undergo apoptosis by concomitant up-regulation of FasL and Fas and down-regulation of Bcl-2 protein. The lymphocytes do not seem to be directly engaged in the process with their own FasL, but they may provide the appropriate cytokine milieu that, in turn, up-regulates Fas and/or FasL leading to apoptosis.

DOI10.1210/jcem.83.6.4853
Alternate JournalJ Clin Endocrinol Metab
PubMed ID9626160

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