| 过表达磷脂酶D3影响成肌细胞中Akt磷酸化水平 |
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| 引用本文： | 张军林,陈帅,张淑金,卢智娟,杨和平,王华岩.过表达磷脂酶D3影响成肌细胞中Akt磷酸化水平[J].生物工程学报,2009,25(10):1524-1531. |
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| 作者姓名： | 张军林 陈帅 张淑金 卢智娟 杨和平 王华岩 |
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| 作者单位： | 1. 西北农林科技大学动物医学院陕西省干细胞工程技术研究中心陕西省农业分子生物学重点实验室,杨凌,712100
2. 杨陵职业技术学院动物工程系,杨凌,712100 |
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| 基金项目： | 国家高技术研究发展计划(863计划)(No.2008AA101005);;国家自然科学基金(No.30871786)资助~~ |
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| 摘 要： | 磷脂酶D(PLD)催化卵磷脂(Phosphatidylc holine,PC)水解产生胆碱(Choline)和磷脂酸(Phosphatidic acid,PA),其代谢产物参与调控细胞内许多生理和生化过程。在过表达磷脂酶D3(PLD3)的成肌细胞(C2C12细胞)中,研究了PLD3对胰岛素刺激后Akt通路激活的影响。研究结果表明,PLD3过表达细胞的Akt磷酸化水平比对照组低,并且不受胰岛素浓度变化的调控。虽然PLD3过表达细胞中Akt磷酸化水平随胰岛素刺激时间的延长而有所增加,但磷酸化总水平比对照组低。磷脂酶D抑制剂丁-1醇能够抑制对照组胰岛素刺激下Akt磷酸化,却不能抑制PLD3过表达细胞的Akt磷酸化,并且PLD3过表达细胞Akt磷酸化水平比对照组高6倍。用磷脂酸(PA)做刺激时,对照组的Akt磷酸化明显增加,而PLD3过表达细胞株的Akt磷酸化没有显著变化;用PA和胰岛素同时刺激时,PLD3过表达株和对照组的Akt磷酸化均比PA单独刺激时降低。这说明PLD3的过表达抑制成肌细胞内胰岛素信号的传导。
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| 关 键 词： | 磷脂酶D3 Akt 胰岛素 C2C12细胞 |
| 收稿时间： | 5/5/2009 12:00:00 AM |
Over-expression of phospholipase D3 inhibits Akt phosphorylation in C2C12 myoblasts |
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| Junlin Zhang,Shuai Chen,Shujin Zhang,Zhijuan Lu,Heping Yang and Huayan Wang.Over-expression of phospholipase D3 inhibits Akt phosphorylation in C2C12 myoblasts[J].Chinese Journal of Biotechnology,2009,25(10):1524-1531. |
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| Authors: | Junlin Zhang Shuai Chen Shujin Zhang Zhijuan Lu Heping Yang and Huayan Wang |
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| Institution: | Shaanxi Center of Stem Cell Engineering and Technology, Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Veterinary Medicine, Northwest A&F University, Yangling 712100, China;Shaanxi Center of Stem Cell Engineering and Technology, Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Veterinary Medicine, Northwest A&F University, Yangling 712100, China;Shaanxi Center of Stem Cell Engineering and Technology, Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Veterinary Medicine, Northwest A&F University, Yangling 712100, China;Shaanxi Center of Stem Cell Engineering and Technology, Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Veterinary Medicine, Northwest A&F University, Yangling 712100, China;Yangling Vocational & Technical College, Department of Animal Engineering, Yangling 712100, China;Shaanxi Center of Stem Cell Engineering and Technology, Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Veterinary Medicine, Northwest A&F University, Yangling 712100, China |
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| Abstract: | Phospholipase D (PLD) hydrolyzes phosphocholine into choline and phosphatide acid, and these metabolites play an important role in regulating cell physiology and biochemistry. To study the biological function of phospholipase D3 (PLD3) during the insulin stimulation in C2C12 myoblasts, we constructed PLD3 over-expressed cell lines (C2C12/pPLD3) and investigated the phosphorylation of Akt. The results showed that the level of phosphorylated Akt (P-Akt) was significantly increased in control C2C12 cells when ... |
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| Keywords: | phospholipase D3 Akt insulin C2C12 cell |
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