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TEM8 functions as a receptor for uPA and mediates uPA-stimulated EGFR phosphorylation.

Cell Commun. Signal. 2018 Sep 21;16(1):62
Lian-Cheng Zhang 1 , Yong Shao 2 , Li-Hua Gao 2 , Jin Liu 3 , Yong-Yi Xi 2 , Yin Xu 3 , Chutse Wu 3 , Wei Chen 2 , Hui-Peng Chen 4 , You-Liang Wang 5 , Hai-Feng Duan 6 , Xian-Wen Hu 7
Lian-Cheng Zhang 1 , Yong Shao 2 , Li-Hua Gao 2 , Jin Liu 3 , Yong-Yi Xi 2 , Yin Xu 3 , Chutse Wu 3 , Wei Chen 2 , Hui-Peng Chen 4 , You-Liang Wang 5 , Hai-Feng Duan 6 , Xian-Wen Hu 7
+ et al

[No authors listed]

Author information
  • 1 Department of Operational Medicine, Tianjin Institute of Environmental and Operational Medicine, Tianjin, 300050, China.
  • 2 Laboratory of Cell Engineering, Beijing Institute of Biotechnology (BIB), No. 20, Dongdajie Street, Fengtai District, Beijing, 100071, China.
  • 3 Key Laboratory of Experimental Hematology, Beijing Institute of Radiation Medicine (BIRM), No. 27, Taiping Road, Haidian District, Beijing, 100850, China.
  • 4 Laboratory of Cell Engineering, Beijing Institute of Biotechnology (BIB), No. 20, Dongdajie Street, Fengtai District, Beijing, 100071, China. chenhp0909@163.com.
  • 5 Laboratory of Cell Engineering, Beijing Institute of Biotechnology (BIB), No. 20, Dongdajie Street, Fengtai District, Beijing, 100071, China. wang_you_liang@aliyun.com.
  • 6 Key Laboratory of Experimental Hematology, Beijing Institute of Radiation Medicine (BIRM), No. 27, Taiping Road, Haidian District, Beijing, 100850, China. duanhf0720@163.com.
  • 7 Laboratory of Cell Engineering, Beijing Institute of Biotechnology (BIB), No. 20, Dongdajie Street, Fengtai District, Beijing, 100071, China. huxw1969@163.com.

摘要

BACKGROUND:TEM8 is a cell membrane protein predominantly expressed in tumor endothelium, which serves as a receptor for the protective antigen (PA) of anthrax toxin. However, the physiological ligands for TEM8 remain unknown. RESULTS:Here we identified uPA as an interacting partner of TEM8. Binding of uPA stimulated the phosphorylation of TEM8 and augmented phosphorylation of EGFR and ERK1/2. Finally, TEM8-Fc, a recombinant fusion protein comprising the extracellular domain of human TEM8 linked to the Fc portion of human IgG1, efficiently abrogated the interaction between uPA and TEM8, blocked uPA-induced migration of HepG2 cells in vitro and inhibited the growth and metastasis of human MCF-7 xenografts in vivo. uPA, TEM8 and EGFR overexpression and ERK1/2 phosphorylation were found co-located on frozen cancer tissue sections. CONCLUSIONS:Taken together, our data provide evidence that TEM8 is a novel receptor for uPA, which may play a significant role in the regulation of tumor growth and metastasis.

KEYWORDS: EGFR, Phosphorylation, Receptor, TEM8, uPA

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