Fukuda M, Carlsson S R
Med Biol. 1986;64(6):335-43.
Most blood cells derived from the bone-marrow are known to possess only a limited number of heavily sialylated glycoproteins. We have recently isolated a major sialoglycoprotein on leukocytes and found that this glycoprotein, termed leukosialin, is ubiquitously present on various human leukocytes, granulocytes, monocytes/macrophages and T- and B-lymphocytes. Our studies showed that leukosialin is significantly glycosylated by O-linked oligosaccharides (90 chains/molecule). The structures of those O-linked oligosaccharides are characteristic to each cell lineage and maturation stage. The polypeptide portion of these molecules are, however, apparently the same, with a molecular size of 52 KDa. So it will be interesting to explore the possibility that leukosialin expresses different functions by having different O-glycosylation in a variety of hematopoietic cells.
已知大多数源自骨髓的血细胞仅拥有数量有限的高度唾液酸化糖蛋白。我们最近在白细胞上分离出一种主要的唾液酸糖蛋白，发现这种糖蛋白，即白细胞唾液酸蛋白，普遍存在于各种人类白细胞、粒细胞、单核细胞/巨噬细胞以及T淋巴细胞和B淋巴细胞上。我们的研究表明，白细胞唾液酸蛋白被O-连接寡糖显著糖基化（每个分子有90条链）。这些O-连接寡糖的结构对于每个细胞谱系和成熟阶段都具有特征性。然而，这些分子的多肽部分显然是相同的，分子大小为52千道尔顿。因此，探索白细胞唾液酸蛋白在多种造血细胞中通过具有不同的O-糖基化而表达不同功能的可能性将是很有趣的。
