Uehara F, Yanagita T, Iwakiri N, Ohba N
Department of Ophthalmology, Kagoshima University Faculty of Medicine, Japan.
Nippon Ganka Gakkai Zasshi. 1997 Jul;101(7):571-4.
The glycoconjugates in neonate rat eyelids at postnatal day 0 or 1 were examined by lectin histochemistry. Maackia amurensis lectin II, which recognizes sialic acid alpha 2, 3 galactose beta 1, 3 N-acetylgalactosamine (Gal beta 1, 3 GalNAc) or sialic acid alpha 2, 3 galactose beta 1, 4 N-acetylglucosamine, bound to the cell membranes of the epithelial basal cells, suggesting that the glycoconjugates containing these sugar chains are present on their cell membranes. With respect to the binding of the Gal beta 1, 3 GalNAc-specific lectin, jacalin, whose binding is not inhibited by the terminal sialic acid, bound to the cell membranes of the epithelial basal cells, whereas peanut agglutinin, whose binding is inhibited by the terminal sialyl residue, did not bind to their cell membranes. These findings suggest that all the residues of Gal beta 1, 3 GalNAc in the glycoconjugates of their cell membranes are sialylated as the mature form.
采用凝集素组织化学方法检测出生后0天或1天新生大鼠眼睑中的糖缀合物。山黧豆凝集素II可识别唾液酸α2,3半乳糖β1,3N-乙酰半乳糖胺（Galβ1,3GalNAc）或唾液酸α2,3半乳糖β1,4N-乙酰葡糖胺，它与上皮基底细胞的细胞膜结合，这表明含有这些糖链的糖缀合物存在于其细胞膜上。关于Galβ1,3GalNAc特异性凝集素红豆凝集素的结合情况，其结合不受末端唾液酸抑制，它与上皮基底细胞的细胞膜结合，而结合受末端唾液酸残基抑制的花生凝集素则不与它们的细胞膜结合。这些发现表明，其细胞膜糖缀合物中所有的Galβ1,3GalNAc残基均已唾液酸化成为成熟形式。
