Exp Clin Endocrinol Diabetes 1992; 100(6): 124-128
DOI: 10.1055/s-0029-1211191
Original

© J. A. Barth Verlag in Georg Thieme Verlag KG Stuttgart · New York

Altered Terminal Glycosylation of Thyroglobulin in Papillary Thyroid Carcinoma

J. Sinadinović1 , Dubravka Cvejić1 , Svetlana Savin1 , Marija Jančić-Zuguricas2 , J. V. Mićić3
  • 1INEP, Institute of Endocrinology, Immunology and Nutrition University of Belgrade, Zemun-Belgrade
  • 2Medical Faculty Institute of Pathology, Serbia/Yugoslavia
  • 3Medical Faculty Institute of Endocrinology, Diabetes and Metabolic Diseases, Clinical University Center, Belgrade, Serbia/Yugoslavia
Further Information

Publication History

Publication Date:
16 July 2009 (online)

Summary

Samples of thyroglobulin (Tg) were isolated from specimens of differentiated thyroid carcinoma of the papillary type and from normal adjacent glandular tissue, and the content of sialic acid was estimated. Also the in vitro incorporation of 14C-sialic acid, in the form of both CMP (cytidine 5'-monophos-pho-) — activated and non-activated N-acetyl-neuraminic acid, into Tg of malignant and morphologically normal thyroid.

The sialic acid content of Tg preparations from papillary thyroid carcinomas varied considerably (0.27-0.92 mg/100 mg Tg). In six cancerous Tg samples the content of sialic acid was markedly lower than that in Tg from the corresponding apparently normal thyroid tissue (0.71:1.11 mg per 100 mg Tg). In addition, in comparison with the control, the incorporation of non-activated 14C-sialic acid into Tg of malignant thyroid tissue was considerably lower (—41 %). However, the incorporation of CMP-activiated 14C-sialic acid into cancerous Tg was greater than into Tg of morphologically unchanged tissue of the same gland (+29 %).

The reduced content and incorporation rate of sialic acid into Tg of differentiated thyroid carcinoma is probably the consequence of disturbances in terminal glycosylation of the Tg molecule in malignantly transformed thyroid tissue. The enhanced incorporation of CMP-sialic acid into cancerous Tg suggests that Tg sialylation in carcinoma is probably altered in the sialic acid activation phase.

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