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Brazilin Isolated from Caesalpinia sappan suppresses nuclear envelope reassembly by inhibiting barrier-to-autointegration factor phosphorylation.

Abstract
To date, many anticancer drugs have been developed by directly or indirectly targeting microtubules, which are involved in cell division. Although this approach has yielded many anticancer drugs, these drugs produce undesirable side effects. An alternative strategy is needed, and targeting mitotic exit may be one alternative approach. Localization of phosphorylated barrier-to-autointegration factor (BAF) to the chromosomal core region is essential for nuclear envelope compartment relocalization. In this study, we isolated brazilin from Caesalpinia sappan Leguminosae and demonstrated that it inhibited BAF phosphorylation in vitro and in vivo. Moreover, we demonstrated direct binding between brazilin and BAF. The inhibition of BAF phosphorylation induced abnormal nuclear envelope reassembly and cell death, indicating that perturbation of nuclear envelope reassembly could be a novel approach to anticancer therapy. We propose that brazilin isolated from C. sappan may be a new anticancer drug candidate that induces cell death by inhibiting vaccinia-related kinase 1-mediated BAF phosphorylation.
AuthorsSeong-Hoon Kim, Ha-Na Lyu, Ye Seul Kim, Yong Hyun Jeon, Wanil Kim, Sangjune Kim, Jong-Kwan Lim, Ho Won Lee, Nam-In Baek, Kwan-Yong Choi, Jaetae Lee, Kyong-Tai Kim
JournalThe Journal of pharmacology and experimental therapeutics (J Pharmacol Exp Ther) Vol. 352 Issue 1 Pg. 175-84 (Jan 2015) ISSN: 1521-0103 [Electronic] United States
PMID25369797 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2014 by The American Society for Pharmacology and Experimental Therapeutics.
Chemical References
  • Antineoplastic Agents
  • BANF1 protein, human
  • Benzopyrans
  • DNA-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Nuclear Proteins
  • Protein-Serine-Threonine Kinases
  • VRK1 protein, human
  • brazilin
Topics
  • Animals
  • Antineoplastic Agents (isolation & purification, metabolism, pharmacology)
  • Benzopyrans (isolation & purification, metabolism, pharmacology)
  • Caesalpinia (chemistry)
  • Cell Death (drug effects)
  • DNA-Binding Proteins (metabolism)
  • Drug Evaluation, Preclinical
  • HeLa Cells
  • Humans
  • Intracellular Signaling Peptides and Proteins (metabolism)
  • Male
  • Mice
  • Nuclear Envelope (drug effects, metabolism)
  • Nuclear Proteins (metabolism)
  • Phosphorylation (drug effects)
  • Protein-Serine-Threonine Kinases (metabolism)
  • Telophase (drug effects)

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