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Coniferyl aldehyde reduces radiation damage through increased protein stability of heat shock transcriptional factor 1 by phosphorylation.

AbstractPURPOSE:
We previously screened natural compounds and found that coniferyl aldehyde (CA) was identified as an inducer of HSF1. In this study, we further examined the protective effects of CA against ionizing radiation (IR) in normal cell system.
METHODS AND MATERIALS:
Western blotting and reverse transcription-polymerase chain reaction tests were performed to evaluate expression of HSF1, HSP27, and HSP70 in response to CA. Cell death and cleavage of PARP and caspase-3 were analyzed to determine the protective effects of CA in the presence of IR or taxol. The protective effects of CA were also evaluated using animal models.
RESULTS:
CA increased stability of the HSF1 protein by phosphorylation at Ser326, which was accompanied by increased expression of HSP27 and HSP70. HSF1 phosphorylation at Ser326 by CA was mediated by EKR1/2 activation. Cotreatment of CA with IR or taxol in normal cells induced protective effects with phosphorylation- dependent patterns at Ser326 of HSF1. The decrease in bone marrow (BM) cellularity and increase of terminal deoxynucleotidyl transferase dUTP nick end labeling-positive BM cells by IR were also significantly inhibited by CA in mice (30.6% and 56.0%, respectively). A549 lung orthotopic lung tumor model indicated that CA did not affect the IR-mediated reduction of lung tumor nodules, whereas CA protected normal lung tissues from the therapeutic irradiation.
CONCLUSIONS:
These results suggest that CA may be useful for inducing HSF1 to protect against normal cell damage after IR or chemotherapeutic agents.
AuthorsSeo-Young Kim, Hae-June Lee, Joo-Won Nam, Eun-Kyoung Seo, Yun-Sil Lee
JournalInternational journal of radiation oncology, biology, physics (Int J Radiat Oncol Biol Phys) Vol. 91 Issue 4 Pg. 807-16 (Mar 15 2015) ISSN: 1879-355X [Electronic] United States
PMID25752395 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
CopyrightCopyright © 2015 Elsevier Inc. All rights reserved.
Chemical References
  • Antineoplastic Agents, Phytogenic
  • DNA-Binding Proteins
  • HSF1 protein, human
  • HSP27 Heat-Shock Proteins
  • HSP70 Heat-Shock Proteins
  • Heat Shock Transcription Factors
  • RNA, Messenger
  • Radiation-Protective Agents
  • Transcription Factors
  • coniferaldehyde
  • Acrolein
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Paclitaxel
Topics
  • Acrolein (analogs & derivatives, pharmacology)
  • Animals
  • Antineoplastic Agents, Phytogenic (pharmacology)
  • Bone Marrow Cells (drug effects, radiation effects)
  • Cell Line, Tumor
  • DNA-Binding Proteins (genetics, metabolism)
  • Female
  • HSP27 Heat-Shock Proteins (genetics, metabolism)
  • HSP70 Heat-Shock Proteins
  • Heat Shock Transcription Factors
  • Humans
  • In Situ Nick-End Labeling (methods)
  • Lung Neoplasms (radiotherapy)
  • MAP Kinase Signaling System
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred ICR
  • Mice, Nude
  • Mitogen-Activated Protein Kinase 1 (metabolism)
  • Mitogen-Activated Protein Kinase 3 (metabolism)
  • Paclitaxel (pharmacology)
  • Phosphorylation
  • RNA, Messenger (metabolism)
  • Radiation Injuries, Experimental (chemically induced, prevention & control)
  • Radiation-Protective Agents (pharmacology)
  • Transcription Factors (genetics, metabolism)
  • Whole-Body Irradiation (methods)

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