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Maturation of Growth Differentiation Factor 15 in Human Placental Trophoblast Cells Depends on the Interaction With Matrix Metalloproteinase-26
Li, Sisi1,3; Wang, Yongqing2; Cao, Bin1; Wu, Yujian1; Ji, Lei1; Li, Yu-xia1; Liu, Ming1; Zhao, Yangyu2; Qiao, Jie2; Wang, Haibing1; Wang, Hongmei1; Han, Chunsheng1; Wang, Yan-ling1
刊名JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM
2014-11-01
DOI10.1210/jc.2014-1598
99期:11页:E2277-E2287
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Endocrinology & Metabolism
研究领域[WOS]Endocrinology & Metabolism
关键词[WOS]MACROPHAGE INHIBITORY CYTOKINE-1 ; BETA SUPERFAMILY MEMBER ; ABNORMAL PREGNANCIES ; CANCER-CELLS ; APOPTOSIS ; ACTIVATION ; PROPEPTIDE ; INVASION ; CLONING ; MMP-26
英文摘要

Context: Matrix Metalloproteinase-26 (MMP-26) is the smallest member of matrix metalloproteinase (MMP) family that functions mainly in the extracellular milieu to cleave the extracellular matrix proteins. It is expressed in various cell types of placenta, but its function in placentation has been poorly understood. Considering the existence of a unique cysteine switch sequence in MMP-26 protein sequence, as well as the evidence in cancer cells indicating the digestion of the NH2-terminal domain of ER beta by MMP-26, we hypothesize that MMP-26 may have specific intracellular activity in human placental trophoblast cells.

Objective: This study aimed to identify the intracellular binding partners of MMP-26 and investigate how MMP-26 is involved in placentation through the interactions with its partners.

Setting and Design: Yeast two-hybrid system was employed to screen potential binding partners of MMP-26 in human placenta. Immunoprecipitation and immunofluorescence assays were conducted to verify the interactions between MMP-26 and the binding partners. HEK293T and HTR8/SVneo cell lines were used as in vitro models to investigate the roles of the interaction between MMP-26 and its binding partner on cell behaviors.

Results: Results of yeast two-hybrid assay, immunoprecipitation, and immunofluorescence assays revealed that MMP-26 could bind to growth differentiation factor 15 (GDF15) in the intracellular milieu. The binding of MMP-26 to GDF15 was responsible for the processing and maturation of pro-GDF15, and the process was dependent on the enzymatic activity of MMP-26. In human placental trophoblast cells, MMP-26 could facilitate the pro-apoptotic effect of GDF15.

Conclusions: This is the first report to demonstrate the physiological function of placental MMP-26 in processing GDF15 and subsequently promoting trophoblast cell apoptosis. These findings expand our understanding of the working mechanism of the metalloproteinase in the process of placentation.

语种英语
WOS记录号WOS:000346743100070
项目编号2011CB944400 ; 81025004
资助机构Chinese National Special Fund for Basic Research Project ; National Natural Sciences Foundation
引用统计
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/64954
专题北京大学第三临床医学院
北京大学第三临床医学院_妇产科
北京大学第三临床医学院_生殖医学中心
作者单位1.Chinese Acad Sci, Inst Zool, State Key Lab Reprod Biol, Beijing 100101, Peoples R China
2.Peking Univ, Hosp 3, Dept Obstet & Gynecol, Beijing 100191, Peoples R China
3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式
GB/T 7714
Li, Sisi,Wang, Yongqing,Cao, Bin,et al. Maturation of Growth Differentiation Factor 15 in Human Placental Trophoblast Cells Depends on the Interaction With Matrix Metalloproteinase-26[J]. JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM,2014,99(11):E2277-E2287.
APA Li, Sisi.,Wang, Yongqing.,Cao, Bin.,Wu, Yujian.,Ji, Lei.,...&Wang, Yan-ling.(2014).Maturation of Growth Differentiation Factor 15 in Human Placental Trophoblast Cells Depends on the Interaction With Matrix Metalloproteinase-26.JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM,99(11),E2277-E2287.
MLA Li, Sisi,et al."Maturation of Growth Differentiation Factor 15 in Human Placental Trophoblast Cells Depends on the Interaction With Matrix Metalloproteinase-26".JOURNAL OF CLINICAL ENDOCRINOLOGY & METABOLISM 99.11(2014):E2277-E2287.
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