ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins
ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins
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DOI：
10.1074/mcp.m300053-mcp200
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发表时间：
2003-10-01
影响因子：
7
通讯作者：
Michalak, M
中科院分区：
文献类型：
--
作者：
Knoblach, B;Keller, BO;Michalak, M
利用内质网（ER）腔内环境的蛋白质组学分析，我们鉴定了141种蛋白质，其中6种以前未知。新发现的两个内质网腔蛋白ERp19和ERp46与蛋白二硫异构酶有关。Western和Northern blot分析显示，与其他组织相比，ERp19和ERp46及其各自的mrna在肝脏中均高表达。这两种蛋白均富集于纯化的肝内质网囊泡中，并特异性定位于McA-RH7777肝细胞的内质网。酵母补体功能分析表明，ERp46在体内可以替代蛋白二硫异构酶的功能，而ERp19不能。
Using a proteomic analysis of the luminal environment of the endoplasmic reticulum (ER), we have identified 141 proteins, of which 6 were previously unknown. Two newly discovered ER luminal proteins, designated ERp19 and ERp46, are related to protein disulphide isomerase. Western and Northern blot analyses revealed that both ERp19 and ERp46 and their respective mRNAs are highly expressed in the liver as compared with other tissues. Both proteins were enriched in purified liver ER vesicles and were localized specifically to the ER in McA-RH7777 hepatocytes. Functional analysis with yeast complementation studies showed that ERp46 but not ERp19 can substitute for protein disulphide isomerase function in vivo.