高尔基体中与天冬酰胺连接的寡糖加工的区室化
Compartmentation of asparagine-linked oligosaccharide processing in the Golgi apparatus.
作者信息
Dunphy W G, Rothman J E
出版信息
J Cell Biol. 1983 Jul;97(1):270-5. doi: 10.1083/jcb.97.1.270.
Abstract
Golgi-associated processing of complex-type oligosaccharides linked to asparagine involves the sequential action of at least six enzymes. By equilibrium sucrose density gradient centrifugation of membranes from Chinese hamster ovary cells, we have partially resolved the set of four initial enzymes in the pathway (Mannosidase I, N-acetylglucosamine (GlcNAc) Transferase I, Mannosidase II, and GlcNAc Transferase II) from two later-acting activities (galactosyltransferase and sialyltransferase). In view of the recent demonstration that galactosyltransferase is restricted to the trans face of the Golgi complex in HeLa cells (Roth, J., and E.G. Berger, 1982, J. Cell Biol., 93:223-229), our results suggest that removal of mannose and attachment of peripheral N-acetylglucosamine may occur in some or all of the remaining cisternae on the cis side of the Golgi stack.
摘要
与天冬酰胺相连的复合型寡糖的高尔基体相关加工过程涉及至少六种酶的顺序作用。通过对中国仓鼠卵巢细胞的膜进行平衡蔗糖密度梯度离心，我们已将该途径中最初的四种酶（甘露糖苷酶I、N-乙酰葡糖胺（GlcNAc）转移酶I、甘露糖苷酶II和GlcNAc转移酶II）与两种后期起作用的活性（半乳糖基转移酶和唾液酸转移酶）部分分离。鉴于最近已证明半乳糖基转移酶局限于HeLa细胞中高尔基体复合体的反面（罗斯，J.，和E.G. 伯杰，1982，《细胞生物学杂志》，93:223 - 229），我们的结果表明，甘露糖的去除以及外周N-乙酰葡糖胺的附着可能发生在高尔基体堆叠顺面的一些或所有剩余潴泡中。
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