S1.21 Characterization of a rat corpus sulfotransferase for the 6-O-sulfation ofß-d-N-acetylglucosamine residues on oligosaccharides
S1.21 Characterization of a rat corpus sulfotransferase for the 6-O-sulfation ofß-d-N-acetylglucosamine residues on oligosaccharides
复制标题
S1.21 大鼠体内磺基转移酶对寡糖上β-d-N-乙酰葡糖胺残基进行 6-O-硫酸化的表征
DOI：
10.1007/bf01209822
复制
发表时间：
1993
影响因子：
3
通讯作者：
K. Hotta
中科院分区：
文献类型：
--
作者：
Y. Goso;K. Hotta
人红白血病(HEL)细胞含有高活性的GDP-L-Fuc-N-乙酰基-f1-D-氨基葡萄糖苷α1~3岩藻糖基转移酶，尽管在HEL细胞的糖蛋白上没有发现Fucal~3GlcNAc残基。为了研究这些不同的结果，推测 HEL 细胞的分化可能会导致膜糖蛋白的糖基化变化。用佛波醇 12-肉豆蔻酸酯 13-乙酸酯 (PMA) 处理可使 HEL 细胞分化，包括在几个小时内粘附的能力，而它们通常在悬浮培养物中生长。 HEL细胞用0.1/aM PMA处理，用L-[3H]岩藻糖标记作为贴壁细胞两天并收获。与未经PMA处理的HEL细胞相反，源自PMA处理的细胞的糖肽含有少量Fucal_3GlcNAc残基，如用杏仁α1_3(4)岩藻糖苷酶检测到的。同时，无论是否处理，细胞提取物中的t~1~3岩藻糖基转移酶活性相似。因此，控制Fucal 3GlcNAc细胞表面表达的并不是α1-3岩藻糖基转移酶本身的活性。对HEL细胞中α1-3岩藻糖基转移酶岩藻糖基化糖蛋白的需要的研究可以提供关于选择素配体的激活以及与其他类型细胞在远端位点形成实体瘤的能力相关的信息。由 NIH RO1 CA 37853 和复杂碳水化合物协会 (LIS) 颁发的旅行奖支持
Human erythroleukemic (HEL) cells contain high activity for GDP-L-Fuc-N-acetyl-fl-D-glucosaminide al~ 3fucosyltransferase, although Fucal~ 3GlcNAc residues are not found on the glycoproteins of HEL cells. To investigate these disparate results it was reasoned that differentiation of HEL ceils may bring about glycosylation changes in the membrane glycoproteins. Treatment with phorbol 12-myristate 13-acetate (PMA) differentiates the HEL cells including the ability to adhere within a few hours whereas they normally grow in suspension culture. HEL cells were treated with 0.1/aM PMA, labeled with L-[3H] fucose for two days as adherent cells and harvested. In contrast to HEL cells non PMA-treated, the glycopeptides derived from the PMA-treated cells contained a small amount of Fucal~ 3GlcNAc residues as detected with almond al~ 3 (4) fucosidase. At the same time, t~ l~ 3fucosyltransferase activity in the cell extracts was similar with or without treatment. Therefore it is not the activity of al~ 3fucosyltransferase per se which controls the cell surface expression of Fucal 3GlcNAc. A study of the requirements of al~ 3fucosyltransferase to fucosylate glycoproteins in HEL cells may provide information regarding the activation of ligands for Selectins as well as relate to the ability of other types of cells to form solid tumors at distal sites. Supported by NIH RO1 CA 37853 and Travel Award from Society for Complex Carbohydrates (LIS)