期刊论文详细信息
American Journal of Cancer Research
An essential role of PRMT1-mediated EGFR methylation in EGFR activation by ribonuclease 5
Hirohito Yamaguchi1  Heng-Huan Lee2  Wei-Jan Wang3  Ying-Nai Wang4  Jung-Mao Hsu5 
[1] Cancer Research Center, Qatar Biomedical Research Institute, College of Health and Life Sciences, Hamad Bin Khalifa University, Education City, Qatar Foundation, P.O. Box 5825 Doha, Qatar;Department of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan 701, Taiwan;Department of Molecular and Cellular Oncology, The University of Texas MD Anderson Cancer Center, Houston 77030, Texas, USA;Graduate Institute of Biomedical Sciences and Center for Molecular Medicine, China Medical University, Taichung 404, Taiwan;Graduate School of Biomedical Sciences, The University of Texas Health Science Center, Houston 77030, Texas, USA
关键词: EGFR;    arginine methylation;    PRMT1;    cetuximab;    RNase;    angiogenin;   
DOI  :  
学科分类:肿瘤学
来源: e-Century Publishing Corporation
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【 摘 要 】

Methylation at Arg198 and Arg200 residues of the EGFR extracellular domain by PRMT1 have been demonstrated to enhance EGFR activation by the canonical ligands, EGF and TGFα. On the other hand, RNase 5 was identified as a new ligand of EGFR recently. However, the interplay between EGFR methylation and RNase 5 in EGFR activation is still unclear. Here, we showed that RNase 5 activated EGFR and enhanced cell proliferation in colorectal cancer cells. PRMT1 positively regulated EGFR signaling activation by RNase 5. Inhibition of EGFR methylation by methylation-site mutagenesis reduced the binding affinity of RNase 5 to EGFR and abrogated RNase 5-mediated EGFR activation, suggesting that PRMT1-mediated EGFR methylation is critical for EGFR activation by RNase 5. Notably, RNase 5 diminished the inhibitory activity of cetuximab on colorectal cancer cells, implying RNase 5 is a potential biomarker to predict cetuximab response in colorectal cancer.

【 授权许可】

CC BY-NC   

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