Neoplastic transformation of the thyroid gland is accompanied by changes in cellular sialylation.
Cancer of the thyroid gland is one of the most common endocrine diseases. Histological evaluation is often complicated by difficulty in distinguishing between benign and malignant lesions. Abnormal glycosylation of cell structures, including changes in sialylation, is a feature of the neoplastic transformation process. The aim of this study was to evaluate associations between neoplastic changes in the thyroid gland and changes in sialylation, with reference to its terminal linkage type. Lectin histochemistry using three sialic acid-binding lectins: Tritrichomonas mobilensis lectin (TML), which recognizes sialic acid without linkage preference; Maackia amurensis leukoagglutinin (MAL), which preferentially binds alpha-2,3-linked sialic acid; and Sambucus nigra agglutinin (SNA), which preferentially binds alpha-2,6-linked sialic acid, were used for detection of sialylated glycoconjugates in 50 human thyroid gland specimens. These included papillary, follicular, oncocytic, medullary and anaplastic carcinomas, follicular adenomas and benign follicular and parenchymatous goiter. The luminal surface of follicular cells in normal thyroid glands, adenomas and goiters showed weak or absent labelling for sialic acid. Malignant transformation of the gland was accompanied by an increase of sialic acid positivity on follicular epithelial cells, especially of alpha-2,3-linked sialic acid. Strong luminal positivity for sialic acid was found in papillary carcinomas, whereas moderate positivity was seen in follicular carcinomas. Inconsistent, weak positivity for sialic acid was documented in medullary and anaplastic carcinomas. Increased membrane sialic acid on thyroid gland cells may be an important diagnostic pathological finding, that could be useful in distinction of malignant from benign thyroid lesions, especially with respect to aspiration cytology diagnostics.