Wieland F T, Gleason M L, Serafini T A, Rothman J E
Cell. 1987 Jul 17;50(2):289-300. doi: 10.1016/0092-8674(87)90224-8.
Tripeptides containing the acceptor sequence for Asn-linked glycosylation (Asn-X-Ser/Thr) were added to CHO and HepG2 cells. The tripeptides were glycosylated in the ER and then secreted into the medium, via the Golgi complex in which the oligosaccharide chains were processed. The half-time for secretion, approximately 10 min, was faster than that of known proteins transported through the same pathway. Since much evidence suggests that oligosaccharide chains are not signals for transport, it appears that no signal is necessary for rapid and efficient transport from the ER to the Golgi, or from the Golgi to the cell surface. Rather, it appears that proteins retained as permanent residents en route through the ER-Golgi transport pathway must contain specific retention signals.
将含有天冬酰胺连接糖基化(Asn-X-Ser/Thr)受体序列的三肽添加到中国仓鼠卵巢细胞(CHO)和人肝癌细胞(HepG2)中。这些三肽在内质网中进行糖基化,然后通过高尔基体复合体分泌到培养基中,在高尔基体中寡糖链会进行加工处理。其分泌的半衰期约为10分钟,比通过相同途径运输的已知蛋白质更快。由于大量证据表明寡糖链不是运输信号,因此从内质网到高尔基体,或从高尔基体到细胞表面的快速高效运输似乎不需要信号。相反,似乎在通过内质网-高尔基体运输途径的过程中作为永久驻留蛋白保留下来的蛋白质必须包含特定的保留信号。