Quantitative Proteomic Survey of Endoplasmic Reticulum in Mouse Liver

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• 作者：Yanping Song ; Ying Jiang ; Wantao Ying ; Yan Gong ; Yujuan Yan ; Dong Yang ; Jie Ma ; Xiaofang Xue ; Fan Zhong ; Songfeng Wu ; Yunwei Hao ; Aihua Sun ; Tao Li ; Wei Sun ; Handong Wei ; Yunping Zhu ; Xiaohong Qian ; Fu
• 刊名：Journal of Proteome Research
• 出版年：2010
• 出版时间：March 5, 2010
• 年：2010
• 卷：9
• 期：3
• 页码：1195-1202
• 全文大小：295K
• 年卷期：v.9,no.3(March 5, 2010)
• ISSN：1535-3907

文摘

To gain a better understanding of the critical function of the endoplasmic reticulum (ER) in liver, we carried out a proteomic survey of mouse liver ER. The ER proteome was profiled with a new three-dimensional, gel-based strategy. From 6152 and 6935 MS spectra, 903 and 1042 proteins were identified with at least two peptides matches at 95% confidence in the rough (r) and smooth (s) ER, respectively. Comparison of the rER and sER proteomes showed that calcium-binding proteins are significantly enriched in the sER suggesting that the ion-binding function of the ER is compartmentalized. Comparison of the rat and mouse ER proteomes showed that 662 proteins were common to both, comprising 53.5% and 49.3% of those proteomes, respectively. We proposed that these proteins were stably expressed proteins that were essential for the maintenance of ER function. GO annotation with a hypergeometric model proved this hypothesis. Unexpectedly, 210 unknown proteins and some proteins previously reported to occur in the cytosol were highly enriched in the ER. This study provides a reference map for the ER proteome of liver. Identification of new ER proteins will enhance our current understanding of the ER and also suggest new functions for this organelle.