Regulation of Cardiac Transcription Factor GATA4 by Post-Translational Modification in Cardiomyocyte Hypertrophy and Heart Failure

• Katanasaka Yasufumi

  Division of Molecular Medicine, School of Pharmaceutical Sciences, University of Shizuoka Division of Translational Research, Kyoto Medical Center, National Hospital Organization Shizuoka General Hospital

• Suzuki Hidetoshi

  Division of Molecular Medicine, School of Pharmaceutical Sciences, University of Shizuoka

• Sunagawa Yoichi

  Division of Molecular Medicine, School of Pharmaceutical Sciences, University of Shizuoka Division of Translational Research, Kyoto Medical Center, National Hospital Organization Shizuoka General Hospital

• Hasegawa Koji

  Division of Translational Research, Kyoto Medical Center, National Hospital Organization

• Morimoto Tatsuya

  Division of Molecular Medicine, School of Pharmaceutical Sciences, University of Shizuoka Division of Translational Research, Kyoto Medical Center, National Hospital Organization Shizuoka General Hospital

Abstract

Heart failure is a leading cause of cardiovascular mortality in industrialized countries. During development and deterioration of heart failure, cardiomyocytes undergo maladaptive hypertrophy, and changes in the cellular phenotype are accompanied by reinduction of the fetal gene program. Gene expression in cardiomyocytes is regulated by various nuclear transcription factors, co-activators, and co-repressors. The zinc finger protein GATA4 is one such transcription factor involved in the regulation of cardiomyocyte hypertrophy. In response to hypertrophic stimuli such as those involving the sympathetic nervous and renin-angiotensin systems, changes in protein interaction and/or post-translational modifications of GATA4 cause hypertrophic gene transcription in cardiomyocytes. In this article, we focus on cardiac nuclear signaling molecules, especially GATA4, that are promising as potential targets for heart failure therapy.

Journal

• International Heart Journal

  International Heart Journal 57 (6), 672-675, 2016

  International Heart Journal Association

Keywords

• Acetylation
• Phosphorylation
• Protein interaction
• Metylation
• SUMOylation

Details

• CRID: 1390282680201446656
• NII Article ID: 130005172007
• DOI: 10.1536/ihj.16-404
• ISSN: 13493299
• ISSN: 13492365
• PubMed: 27818483
• Web Site: https://www.jstage.jst.go.jp/article/ihj/57/6/57_16-404/_pdf
• Web Site: https://search.jamas.or.jp/link/ui/2017239604
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • PubMed
  • CiNii Articles
  • KAKEN
• Abstract License Flag: Disallowed