The role of protein arginine methyltransferases in kidney diseases

被引:7
作者
Zhang, Chunyun [1 ,2 ]
Zhuang, Shougang [1 ,2 ,3 ]
机构
[1] Brown Univ, Dept Med, Rhode Isl Hosp, Providence, RI 02912 USA
[2] Brown Univ, Alpert Med Sch, Providence, RI 02912 USA
[3] Tongji Univ, Shanghai East Hosp, Dept Nephrol, Sch Med, Shanghai, Peoples R China
基金
中国国家自然科学基金; 美国国家卫生研究院;
关键词
OXIDE SYNTHASE INHIBITOR; ASYMMETRIC DIMETHYLARGININE; SELECTIVE INHIBITOR; INSULIN-RESISTANCE; EPITHELIAL-CELLS; POTENTIAL ROLE; BREAST-CANCER; RAT MODEL; IN-VIVO; METHYLATION;
D O I
10.1042/CS20200680
中图分类号
R-3 [医学研究方法]; R3 [基础医学];
学科分类号
1001 ;
摘要
The methylation of arginine residues by protein arginine methyltransferases (PRMTs) is a crucial post-translational modification for many biological processes, including DNA repair, RNA processing, and transduction of intra- and extracellular signaling. Previous studies have reported that PRMTs are extensively involved in various pathologic states, including cancer, inflammation, and oxidative stress reaction. However, the role of PRMTs has not been well described in kidney diseases. Recent studies have shown that aberrant function of PRMTs and its metabolic products-symmetric dimethylarginine (SDMA) and asymmetric dimethylarginine (ADMA)-are involved in several renal pathological processes, including renal fibrosis, acute kidney injury (AKI), diabetic nephropathy (DN), hypertension, graft rejection and renal tumors. We aim in this review to elucidate the possible roles of PRMTs in normal renal function and various kidney diseases.
引用
收藏
页码:2037 / 2051
页数:15
相关论文
共 50 条
  • [31] Exploration of Cyanine Compounds as Selective Inhibitors of Protein Arginine Methyltransferases: Synthesis and Biological Evaluation
    Hu, Hao
    Owens, Eric A.
    Su, Hairui
    Yan, Leilei
    Levitz, Andrew
    Zhao, Xinyang
    Henary, Maged
    Zheng, Yujun George
    JOURNAL OF MEDICINAL CHEMISTRY, 2015, 58 (03) : 1228 - 1243
  • [32] Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases
    Dowden, James
    Hong, Wei
    Parry, Richard V.
    Pike, Richard A.
    Ward, Stephen G.
    BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, 2010, 20 (07) : 2103 - 2105
  • [33] Purification and Identification of Natural Inhibitors of Protein Arginine Methyltransferases from Plants
    Wang, Zhengxin
    Xiong, Ling
    Xiong, Quanbo
    MOLECULAR AND CELLULAR BIOLOGY, 2022, 42 (04)
  • [34] Peptidic Partial Bisubstrates as Inhibitors of the Protein Arginine N-Methyltransferases
    't Hart, Peter
    Lakowski, Ted M.
    Thomas, Dylan
    Frankel, Adam
    Martin, Nathaniel I.
    CHEMBIOCHEM, 2011, 12 (09) : 1427 - 1432
  • [35] Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases
    Jain, Kanishk
    Jin, Cyrus Y.
    Clarke, Steven G.
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2017, 114 (38) : 10101 - 10106
  • [36] Protein arginine methyltransferases: insights into the enzyme structure and mechanism at the atomic level
    Tewary, Sunil Kumar
    Zheng, Y. George
    Ho, Meng-Chiao
    CELLULAR AND MOLECULAR LIFE SCIENCES, 2019, 76 (15) : 2917 - 2932
  • [37] Nη-Substituted Arginyl Peptide Inhibitors of Protein Arginine N-Methyltransferases
    Lakowski, Ted M.
    't Hart, Peter
    Ahem, Christopher A.
    Martin, Nathaniel I.
    Frankel, Adam
    ACS CHEMICAL BIOLOGY, 2010, 5 (11) : 1053 - 1063
  • [38] Mutations in protein N-arginine methyltransferases are not the cause of FTLD-FUS
    Ravenscroft, Thomas A.
    Baker, Matt C.
    Rutherford, Nicola J.
    Neumann, Manuela
    Mackenzie, Ian R.
    Josephs, Keith A.
    Boeve, Bradley F.
    Petersen, Ronald
    Halliday, Glenda M.
    Kril, Jillian
    van Swieten, John C.
    Seeley, William W.
    Dickson, Dennis W.
    Rademakers, Rosa
    NEUROBIOLOGY OF AGING, 2013, 34 (09) : 2235.e11 - 2235.e13
  • [39] Hetero-oligomeric interaction as a new regulatory mechanism for protein arginine methyltransferases
    Bae, Angela A.
    Zheng, Y. George
    BIOCHEMICAL SOCIETY TRANSACTIONS, 2024, : 2193 - 2201
  • [40] Arginine Methyltransferases as Regulators of RNA-Binding Protein Activities in Pathogenic Kinetoplastids
    Campagnaro, Gustavo D.
    Nay, Edward
    Plevin, Michael J.
    Cruz, Angela K.
    Walrad, Pegine B.
    FRONTIERS IN MOLECULAR BIOSCIENCES, 2021, 8