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RPAP3 enhances cytotoxicity of doxorubicin by impairing NF-kappa B pathway.

Abstract
Activation of anti-apoptotic gene transcription by NF-κB (nuclear factor-kappa B) has been reported to be linked with a resistance of cancer cells against chemotherapy. NEMO (NF-κB essential modulator) interacts with a number of proteins and modulates the activity of NF-κB pathway. In this study, we revealed that RPAP3 (RNA polymerase II-associated protein 3) possesses an activity to bind with NEMO and to inhibit the ubiquitination of NEMO and that RPAP3 enhances doxorubicin-induced cell death in breast cancer cell line T-47D through the marked impairment of NF-κB pathway. These results indicate that RPAP3 may be a novel modulator of NF-κB pathway in apoptosis induced by anti-cancer chemotherapeutic agents.
AuthorsKana Shimada, Makio Saeki, Hiroshi Egusa, Sho Fukuyasu, Yoshiaki Yura, Kazuhiro Iwai, Yoshinori Kamisaki
JournalBiochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 404 Issue 4 Pg. 910-4 (Jan 28 2011) ISSN: 1090-2104 [Electronic] United States
PMID21184742 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2010 Elsevier Inc. All rights reserved.
Chemical References
  • Antibiotics, Antineoplastic
  • Apoptosis Regulatory Proteins
  • Carrier Proteins
  • IKBKG protein, human
  • NF-kappa B
  • RPAP3 protein, human
  • Doxorubicin
  • I-kappa B Kinase
Topics
  • Antibiotics, Antineoplastic (pharmacology)
  • Apoptosis
  • Apoptosis Regulatory Proteins
  • Carrier Proteins (genetics, metabolism)
  • Cell Line, Tumor
  • Doxorubicin (pharmacology)
  • Humans
  • I-kappa B Kinase (metabolism)
  • NF-kappa B (metabolism)
  • Phosphorylation
  • Ubiquitination

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