[1]樊　龙,朱翠翠,皮玉瑞,等.基质金属蛋白酶-14和Bst-2通过蛋白质结构域相互作用而抑制Bst-2的生物活性[J].南京师范大学学报(自然科学版),2016,39(03):79.[doi:10.3969/j.issn.1001-4616.2016.03.014]
　Fan Long,Zhu Cuicui,Pi Yurui,et al.Matrix Metalloproteinase-14 Inhibits the Activity of Bst-2 viaTheir Cytoplasmic Domains Dependent Interaction[J].Journal of Nanjing Normal University(Natural Science Edition),2016,39(03):79.[doi:10.3969/j.issn.1001-4616.2016.03.014]
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基质金属蛋白酶-14和Bst-2通过蛋白质结构域相互作用而抑制Bst-2的生物活性()
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《南京师范大学学报》（自然科学版）[ISSN:1001-4616/CN:32-1239/N]

卷:
第39卷
期数:
2016年03期
页码:
79
栏目:
·生命科学·
出版日期:
2016-09-30

文章信息/Info

Title:
Matrix Metalloproteinase-14 Inhibits the Activity of Bst-2 viaTheir Cytoplasmic Domains Dependent Interaction
文章编号:
1001-4616（2016）03-0079-10
作者:
樊　龙; 朱翠翠; 皮玉瑞; 吴朝蒙; 卢　山; 刘　平
南京师范大学生命科学学院，江苏 南京 210023
Author(s):
Fan Long; Zhu Cuicui; Pi Yurui; Wu Zhaomeng; Lu Shan; Liu Ping
School of Life Sciences，Nanjing Normal University，Nanjing 210023，China
关键词:
骨髓基质细胞抗原-2; 基质金属蛋白酶-14; 病毒释放
Keywords:
Bst-2; MT1-MMP; virus release
分类号:
Q291
DOI:
10.3969/j.issn.1001-4616.2016.03.014
文献标志码:
A
摘要:
Bst-2（骨髓基质细胞抗原-2）是一种II型膜蛋白，其主要功能是抑制病毒从感染细胞释放；基质金属蛋白酶-14（MT1-MMP）是一种膜蛋白酶，其主要功能是通过激活proMMP2在细胞生长和迁移中扮演重要角色. 本研究主要探讨了MT1-MMP抑制Bst-2生物活性的分子机制. 实验结果表明，MT1-MMP通过与Bst-2相互作用进而抑制Bst-2的活性和功能；并且，在此相互作用中，这两种膜蛋白的细胞质结构域（Bst-2的N-末端结构域和MT1-MMP的C-末端结构域）起到了极为关键的作用. 此外，还发现Bst-2的N-末端结构域在Bst-2抑制MT1-MMP活性的过程中也不可或缺. 这些结果为临床上探索抑制病毒感染和肿瘤转移的新方法和新药物研制开发提供了理论依据.
Abstract:
Bst-2（bone marrow stromal cell antigen 2）is a type II membrane protein and acts as a tetherin to inhibit virion releasing from infectious cells. Membrane type-1 matrix metalloproteinase（MT1-MMP）is a protease and plays a pivotal role in cellular growth and migration by activating proMMP-2 into active MMP2. In this study，we explored the molecular mechanism of MT1-MMP inhibiting the activity of Bst-2. From experimental data，it’s elaborated that MT1-MMP inhibited the tetherin activity of Bst-2 via the interaction within，and the cytoplasmic domains of both Bst-2 and MT1-MMP play critical roles in the interaction. Furthermore，we found that that N-terminal domain of Bst-2 is not only important in relating to the activity of Bst-2 itself，but important for inhibiting the activities of MT1-MMP and MT1-MMP/proMMP2/MMP2 pathway. These findings suggest that MT1-MMP is a novel inhibitor of Bst-2 in MT1-MMP expressed cell lines and indicate that both N-terminal domain of Bst-2 and C-terminal domain of MT1-MMP are crucial in their activity down-regulation.

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备注/Memo

备注/Memo:
收稿日期：2016-02-22.　
基金项目：国家自然科学基金（81272850、81172007、81472415）.　
通讯联系人：刘平，教授，博士生导师，研究方向：肿瘤发生与发展的分子机制. E-mail：08201@njnu.edu.cn
更新日期/Last Update: 2016-09-30