Galectin-1 is expressed by thymic epithelial cells in myasthenia gravis

• Published in: Glycoconjugate journal Vol. 13; no. 4; pp. 591 - 597
• Main Authors: Hafer-Macko, C, Pang, M, Seilhamer, J J, Baum, L G
• Format: Journal Article
• Language: English
• Published: United States 01.08.1996
• Subjects: beta-Galactosidase - metabolism; Cell Adhesion; Epithelial Cells; Epithelium - metabolism; Galectin 1; Hemagglutinins - metabolism; Humans; Myasthenia Gravis - metabolism; T-Lymphocytes - cytology; Thymoma - metabolism; Thymoma - pathology; Thymus Gland - cytology; Thymus Gland - metabolism; Thymus Gland - surgery; Tumor Cells, Cultured
• ISSN: 0282-0080; 1573-4986
• DOI: 10.1007/bf00731447

Galectin-1, a member of a family of carbohydrate binding proteins, is synthesized by thymic epithelial cells in normal juvenile thymus, and mediates adhesion of immature T cells to thymic epithelium. Because cell adhesion molecules are proposed to play a role in the thymic hyperplasia and neoplasia seen in the autoimmune disease myasthenia gravis, we examined the expression of galectin-1 in myasthenic thymi. We detected abundant galectin-1 expression in thymic epithelial cells in 27 hyperplastic and neoplastic thymi from patients with myasthenia gravis. Primary cultures of neoplastic epithelial cells from a thymoma continued to express galectin-1, and bound immature T cells; T cell binding was inhibited by the addition of the beta-galactosides lactose and thiodigalactoside, suggesting that galectin-1 on the thymoma cells and a saccharide ligand on the T cells participated in cell-cell adhesion. Expression of galectin-1 by thymic epithelial cells may play a role in the thymic pathology seen in myasthenia gravis.