Salabè H, Dominici R, Salabè G B
Clin Exp Immunol. 1976 Aug;25(2):234-43.
Immunoreaction of desialylated and native thyroglobulin was compared in sera of patients with anti-thyroglobulin antibodies by radioimmunoassay with 125I-labelled thyroglobulin. Two human thyroglobulins were iodinated both in vivo and by lactoperoxidase. After desialylation enhancement of immunoreaction was observed in several sera ranging from marginal to more than 100%. The effect was not due to iodination since it was reproducible with desialylated thyroglobulin labelled in vivo. In one serum (B.P.) a marked enhancement was only seen with one thyroglobulin suggesting that desialylation may unmask isoantigens of thyroglobulin. Glycopeptides prepared from human thyroglobulin inhibited the immunoreaction between native thyroglobulin and autoantisera. The results indicate that sialic acid masks antigenic determinants in human thyroglobulin and that carbohydrates might be the determinants involved in the process of autoimmunization.
通过用¹²⁵I标记的甲状腺球蛋白进行放射免疫测定,比较了去唾液酸化甲状腺球蛋白和天然甲状腺球蛋白在抗甲状腺球蛋白抗体患者血清中的免疫反应。两种人甲状腺球蛋白分别在体内和通过乳过氧化物酶进行碘化。去唾液酸化后,在几例血清中观察到免疫反应增强,增强幅度从轻微到超过100%不等。该效应并非由于碘化所致,因为用体内标记的去唾液酸化甲状腺球蛋白可重现此效应。在一份血清(B.P.)中,仅对一种甲状腺球蛋白观察到明显增强,这表明去唾液酸化可能会暴露甲状腺球蛋白的同种抗原。从人甲状腺球蛋白制备的糖肽可抑制天然甲状腺球蛋白与自身抗血清之间的免疫反应。结果表明,唾液酸掩盖了人甲状腺球蛋白中的抗原决定簇,并且碳水化合物可能是自身免疫过程中涉及的决定簇。