HETEROGENEITY OF HUMAN T-CELL GROWTH FACTOR(S) DUE TO VARIABLE GLYCOSYLATION
HETEROGENEITY OF HUMAN T-CELL GROWTH FACTOR(S) DUE TO VARIABLE GLYCOSYLATION
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DOI：
10.1016/0161-5890(81)90024-9
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发表时间：
1981-01-01
影响因子：
3.6
通讯作者：
SMITH, KA
中科院分区：
文献类型：
--
作者：
ROBB, RJ;SMITH, KA
从人扁桃体细胞中提取的T细胞生长因子(TCGF)经等电聚焦凝胶和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法可分离出多个活性峰。用神经氨酸酶和糖苷酶处理或抑制糖基化表明，这种异质性主要是由于唾液酸化，其次是其他糖残基的差异。从人类T-白血病细胞系制备的TCGF在电荷和大小上都是一致的，与扁桃体衍生活动的asialo形式没有区别。唾液酸化和去唾液酸化的TCGF均可在连续传代中介导T细胞的持续体外增殖。因此，一种可变的糖基化蛋白显然是负责T细胞生长的实体。
T-cell growth factor (TCGF) prepared from human tonsil cells was shown to separate into multiple peaks of activity on isoelectric focusing gels and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Treatment with neuraminidase and glycosidases or inhibition of glycosylation demonstrated that this heterogeneity was primarily due to sialylation and, to a lesser extent, differences in other sugar residues. TCGF prepared from a human T-leukemia cell line was uniform in charge and size and indistinguishable from the asialo form of tonsil-derived activity. Both sialylated and asialo-TCGF mediated continuous in vitro T-cell proliferation over successive passages. Thus, a variably glycosylated protein is evidently the entity responsible for T-cell growth.