内质网对膜蛋白的滞留
Retention of membrane proteins by the endoplasmic reticulum.
作者信息
Brands R, Snider M D, Hino Y, Park S S, Gelboin H V, Rothman J E
出版信息
J Cell Biol. 1985 Nov;101(5 Pt 1):1724-32. doi: 10.1083/jcb.101.5.1724.
Abstract
We have used a monoclonal antibody specific for a hydrocarbon-induced cytochrome P450 to localize, by electron microscopy, the epitope-specific cytochrome P450. The cytochrome was found in the rough and smooth endoplasmic reticulum (ER) and the nuclear envelope of hepatocytes. Significant quantities of cytochrome P450 were not found in Golgi stacks. We also could not find any evidence of Golgi-associated processing of the Asn-linked oligosaccharide chains of two well-characterized ER membrane glycoprotein enzymes (glucosidase II and hexose-6-phosphate dehydrogenase), or of the oligosaccharides attached to the bulk of the glycoproteins of the ER membrane. We conclude that these ER membrane proteins are efficiently retained during a process of highly selective export from this organelle.
摘要
我们使用了一种对烃诱导的细胞色素P450特异的单克隆抗体，通过电子显微镜来定位表位特异性细胞色素P450。该细胞色素存在于肝细胞的粗面和滑面内质网（ER）以及核膜中。在高尔基体堆叠中未发现大量的细胞色素P450。我们也未找到任何证据表明高尔基体参与了两种已充分表征的内质网膜糖蛋白酶（葡糖苷酶II和6-磷酸己糖脱氢酶）的天冬酰胺连接寡糖链的加工，或者参与了内质网膜大部分糖蛋白所连接的寡糖的加工。我们得出结论，这些内质网膜蛋白在从该细胞器进行高度选择性输出的过程中被有效地保留了下来。
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