TFPI-2 suppresses breast cancer cell proliferation and invasion through regulation of ERK signaling and interaction with actinin-4 and myosin-9

被引:34
|
作者
Wang, Guangli [1 ,4 ]
Huang, Wenhe [2 ,3 ]
Li, Wei [1 ]
Chen, Shaoying [1 ]
Chen, Weibin [1 ]
Zhou, Yanchun [1 ]
Peng, Pei [1 ]
Gu, Wei [1 ]
机构
[1] Shantou Univ, Coll Med, Dept Pathophysiol, Key Immunopathol Lab Guangdong Prov, Shantou 515041, Guangdong, Peoples R China
[2] Shantou Univ, Coll Med, Tumor Hosp, Shantou 515041, Guangdong, Peoples R China
[3] Xiamen Univ, Xiangan Hosp, Xiamen 361101, Fujian, Peoples R China
[4] Guilin Med Univ, Affiliated Hosp, Dept Prepotency & Genet, Guilin 541001, Guangxi, Peoples R China
来源
SCIENTIFIC REPORTS | 2018年 / 8卷
基金
美国国家卫生研究院; 中国国家自然科学基金;
关键词
FACTOR PATHWAY INHIBITOR-2; KUNITZ-TYPE DOMAIN; MATRIX METALLOPROTEINASES; TUMOR PROGRESSION; EXPRESSION; ERLOTINIB; MOTILITY; ROLES;
D O I
10.1038/s41598-018-32698-3
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
TFPI-2 has been recognized as a potent tumor suppressor gene. Low expression of TFPI-2 results in enhanced growth and metastasis of a variety of human tumors. In the present study, we investigated the mechanism responsible for the tumor suppressive effect of TFPI-2. Overexpression of TFPI-2 decreased phosphorylation of ERK1/2 and the translocation of p-ERK1/2 from cytoplasm into the nucleus, and eventually resulted in a reduced cell proliferation. Immunoprecipitation assays identified myosin-9 and actinin-4 as TFPI-2-interacting proteins. Full-length TFPI-2 was required for binding to actinin-4, whereas the N + KD1 regions of TFPI-2 were sufficient to interact with myosin-9. Although overexpression of TFPI-2 or TFPI-2/N + KD1 does not affect the expression of actinin-4 and myosin-9, it inhibits the migration and invasion of human breast cancer cells. Our results suggest that TFPI-2 suppresses cancer cell proliferation and invasion partly through the regulation of the ERK1/2 signaling and through interactions with myosin-9 and actinin-4.
引用
收藏
页数:12
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