Intracellular transport of lymphoid surface glycoproteins. Role of the Golgi complex.

Intracellular transport of lymphoid surface glycoproteins. Role of the Golgi complex.
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淋巴表面糖蛋白的细胞内转运。

DOI:
10.1016/0022-2836(81)90378-8
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发表时间:
1981
影响因子:
5.6
通讯作者:
Pierre Vassalli
Pierre Vassalli
中科院分区:
生物学2区
文献类型:
--
作者:
A. Tartakoff;Daniel C. Hoessli;Pierre Vassalli

文献摘要

被引文献

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两种膜糖蛋白重链的生物合成(被鉴定为免疫球蛋白 M 和组织相容性抗原)已通过一维和二维凝胶电泳在 [35S] 蛋氨酸脉冲追踪实验中进行了研究。末端糖添加导致凝胶流动性显着变化,这主要是由于唾液酸添加所致,因为它们对神经氨酸酶敏感。当离子载体莫能菌素在追踪孵育过程中存在时,这些变化就会被阻止。我们得出结论,膜 IgM† 和 H2 重链通常都会穿过莫能菌素定义的高尔基体亚位点,并在该位点远端获得末端唾液酸。对表面碘化对照和莫能菌素处理的细胞的分析表明,在莫能菌素存在的情况下,新合成的、不完全糖基化的 IgM 和 H2 不会转运到细胞表面。因此,这些膜蛋白似乎遵循与分泌蛋白相同的细胞内途径。
The biosynthesis of the heavy chains of two membrane glycoproteins, identified as immunoglobulin M and histocompatibility antigens, has been studied in [35S]methionine pulse-chase experiments by one and two-dimensional gel electrophoresis. Terminal sugar addition results in marked shifts in gel mobility that are mainly due to sialic acid addition, since they are sensitive to neuraminidase. These shifts are prevented when the ionophore monensin is present during the chase incubation. We conclude that both membrane IgM†and H2 heavy chains normally pass through the Golgi subsite defined by monensin and acquire terminal sialic acid distal to this site. Analysis of surface-iodinated control and monensin-treated cells indicates that, in the presence of monensin, newly synthesized, incompletely glycosylated IgM and H2 are not transported to the cell surface. Thus these membrane proteins appear to follow the same intracellular pathway as secretory proteins.