组蛋白赖氨酸甲基化修饰与先天性心脏病研究进展

doi:10.3724/SP.J.1005.2010.00650

遗传 ›› 2010, Vol. 32 ›› Issue (7): 650-655.doi: 10.3724/SP.J.1005.2010.00650

组蛋白赖氨酸甲基化修饰与先天性心脏病研究进展

盛伟1, 2, 马端1

1. 复旦大学上海医学院分子医学教育部重点实验室, 复旦大学出生缺陷研究中心, 上海 200053; 2. 安徽科技学院生命科学学院, 凤阳 200032

收稿日期:2009-10-28 修回日期:2010-01-12 出版日期:2010-07-20 发布日期:2010-07-20
通讯作者: 马端 E-mail:duanma@shmu.edu.cn
基金资助:
国家重点基础研究发展规划(973计划)项目(编号：2009CB941704)资助

Research progress in modification of histone lysine methylation and congenital heart defect

SHENG Wei^{1, 2}, MA Duan¹

1. Key Laboratory of Molecular Medicine, Ministry of Education,Shanghai Medical College, Fudan University, Birth Defects Research Center, Fudan University, Shanghai 200053, China; 2. College of Life Science, Anhui Science and Technology University, Fengyang 200032, China

Received:2009-10-28 Revised:2010-01-12 Online:2010-07-20 Published:2010-07-20
Contact: MA Duan E-mail:duanma@shmu.edu.cn

摘要/Abstract

摘要： 组蛋白修饰是表观遗传调控的一个重要组成部分, 它通过改变染色质的结构以及与其他调控蛋白相互作用, 调节真核基因的表达。组蛋白修饰异常可能导致多种疾病的发生, 同时, 组蛋白修饰的可逆性为疾病的治疗提供了新的思路。文章主要对组蛋白赖氨酸甲基化修饰与先天性心脏病发生的有关机制进行了综述, 以期能够为从事该领域研究的科研人员提供有价值的参考。

关键词: 表观遗传调控, 蛋白甲基化, 天性心脏病

Abstract: Histone modification is an important component of epigenetic regulation, which can regulate eukaryotic gene expression by changing the structure of chromatin and interacting with other regulatory proteins. Abnormal histone modifications may lead to a variety of diseases, while the reversibility of histone modification provides a new way of thinking for treatment of these diseases. In this paper, we discussed the mechanism of histone lysine methylation related to congenital heart defect in order to provide a useful reference for researchers working in this area.

Key words: epigenetic regulation, istone methylation, ongenital heart defect

盛伟，马端. 组蛋白赖氨酸甲基化修饰与先天性心脏病研究进展[J]. 遗传, 2010, 32(7): 650-655.

CHENG Wei, MA Duan. Research progress in modification of histone lysine methylation and congenital heart defect[J]. HEREDITAS, 2010, 32(7): 650-655.

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组蛋白赖氨酸甲基化修饰与先天性心脏病研究进展

Research progress in modification of histone lysine methylation and congenital heart defect

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