Ultrastructural Localization of Thyroid Peroxidase, Hydrogen Peroxide Generating Sites and Monoamine Oxidase in Benign and Malignant Thyroid Diseases

MASINI-REPISO ANA M, BONATERRA MÓNICA, SPITALE LUIS, DI FULVIO MAURICIO, BONINO MARÍA I., COLEONI ALDO H., ORGNERO-GAISÁN ELSA; MASINI-REPISO ANA M, BONATERRA MÓNICA, SPITALE LUIS, DI FULVIO MAURICIO, BONINO MARÍA I., COLEONI ALDO H., ORGNERO-GAISÁN ELSA

HUMAN PATHOLOGY

Elsevier Inc

Lugar: Saint Louis, USA.; Año: 2004 vol. 35 p. 436 - 436

0046-8177

font size="2"> Despite thyroid tissue heterogeneity, biochemical and morphological features have been associated with certain thyroid diseases. We analyzed the ultracytochemical localization of thyroperoxidase (TPO), TPO-associated hydrogen peroxide–generating sites (H2O2 sites), and monoamine oxidase (MAO) in terms of morphology and biochemical TPO activity in abnormal thyroids. We examined 11 cases of nontoxic multinodular goiter, 5 cases of Hashimoto’s thyroiditis, 1 case of oncocytic (Hu¨rthle or oxyphilic cell) adenoma, 5 cases of Graves’ disease, 4 cases of papillary carcinoma, and 4 cases of perinodular normal tissue. In the perinodular tissue, TPO was detected mainly in the nuclear envelope, rough endoplasmic reticulum (RER), and subapical vesicles, but not in the apical surface. In multinodular goiter, heterogeneous TPO reactivity ranging from almost null to strongly positive was detected in similar locations as in the perinodular tissue, and was in the