Identification of 4′-O-β-D-glucosyl-5-O-methylvisamminol as a novel epigenetic suppressor of histone H3 phosphorylation at Ser10 and its interaction with 14-3-3ε

被引:6
作者
Kang, Jong-Su [1 ]
Chin, Young-Won [1 ]
Lee, Kyeong [1 ]
Kim, Young-Woo [1 ]
Choi, Bu Young [2 ]
Keum, Young-Sam [1 ]
机构
[1] Dongguk Univ, Coll Pharm, Goyang 410773, Gyeonggi Do, South Korea
[2] Seowon Univ, Dept Phamaceut Sci & Engn, Cheongju 361742, Chungbuk, South Korea
关键词
4 '-O-beta-D-Glucosyl-5-O-methylvisamminol; Histone phosphorylation; 14-3-3; epsilon; Aurora B kinase; 14-3-3; PROTEINS; CANCER;
D O I
10.1016/j.bmcl.2014.07.005
中图分类号
R914 [药物化学];
学科分类号
100701 ;
摘要
Natural compounds are regarded as a rich source for potential anti-inflammatory and anti-carcinogenic agents. Increasing evidence indicates that histone phosphorylation at Ser10 is a marker for cell cycle progression during the mitosis and the induction of immediate pro-inflammatory genes during the interphase. In the present study, we have screened our in-house natural compounds to find out new chemical inhibitor(s) of histone H3 phosphorylation at Ser10. As a result, we observed that alpha-amyrin, oleanolic acid, marliolide, and 4'-O-beta-D-glucosyl-5-O-methylvisamminol decreased the levels of histone H3 phosphorylation at Ser10 and c-Jun. In particular, we observed that 4'-O-beta-D-glucosyl-5-O-methylvisamminol suppressed the direct interaction of histone H3 with 14-3-3 epsilon, inhibited the aurora B kinase activity and delayed the mitotic cell cycle progression. We reports 4'-0-beta-D-glucosyl-5-O-methylvisamminol as the first epigenetic natural chemical inhibitor that can abrogates the mitotic cell cycle progression and immediate pro-inflammatory gene expressions via suppression of histone H3 phosphorylation at Ser10 and its interaction with 14-3-3 epsilon. (C) 2014 Elsevier Ltd. All rights reserved.
引用
收藏
页码:4763 / 4767
页数:5
相关论文
共 14 条
  • [1] When Signaling Kinases Meet Histones and Histone Modifiers in the Nucleus
    Baek, Sung Hee
    [J]. MOLECULAR CELL, 2011, 42 (03) : 274 - 284
  • [2] BODE AM, 2003, SCI STKE, pRE2
  • [3] Covalent histone modifications - miswritten, misinterpreted and mis-erased in human cancers
    Chi, Ping
    Allis, C. David
    Wang, Gang Greg
    [J]. NATURE REVIEWS CANCER, 2010, 10 (07) : 457 - 469
  • [4] MAP kinase-mediated phosphoacetylation of histone H3 and inducible gene regulation
    Clayton, AL
    Mahadevan, LC
    [J]. FEBS LETTERS, 2003, 546 (01) : 51 - 58
  • [5] Cancer Epigenetics: From Mechanism to Therapy
    Dawson, Mark A.
    Kouzarides, Tony
    [J]. CELL, 2012, 150 (01) : 12 - 27
  • [6] 14-3-3 proteins: Structure, function, and regulation
    Fu, HA
    Subramanian, RR
    Masters, SC
    [J]. ANNUAL REVIEW OF PHARMACOLOGY AND TOXICOLOGY, 2000, 40 : 617 - 647
  • [7] UVB-induced COX-2 expression requires histone H3 phosphorylation at Ser10 and Ser28
    Keum, Y-S
    Kim, H-G
    Bode, A. M.
    Surh, Y-J
    Dong, Z.
    [J]. ONCOGENE, 2013, 32 (04) : 444 - 452
  • [8] Chromatin modifications and their function
    Kouzarides, Tony
    [J]. CELL, 2007, 128 (04) : 693 - 705
  • [9] Emerging avenues linking inflammation and cancer
    Kundu, Joydeb Kumar
    Surh, Young-Joon
    [J]. FREE RADICAL BIOLOGY AND MEDICINE, 2012, 52 (09) : 2013 - 2037
  • [10] Molecular basis for the recognition of phosphorylated and phosphoacetylated histone H3 by 14-3-3
    MacDonald, N
    Welburn, JPI
    Noble, MEM
    Nguyen, A
    Yaffe, MB
    Clynes, D
    Moggs, JG
    Orphanides, G
    Thomson, S
    Edmunds, JW
    Clayton, AL
    Endicott, JA
    Mahadevan, LC
    [J]. MOLECULAR CELL, 2005, 20 (02) : 199 - 211