Acta Physiologica Hungarica
Volume/Issue:
Volume 96: Issue 3
Role of 14-3-3 protein and oxidative stress in diabetic cardiomyopathy
Authors:
Kenichi Watanabe

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R. Thandavarayan Niigata University of Pharmacy and Applied Life Sciences Department of Clinical Pharmacology 265-1 Higashijima, Akiha-ku Niigata City Japan

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N. Gurusamy University of Connecticut School of Medicine Cardiovascular Research Center Farmington USA

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S. Zhang Lightlab Imaging, Inc. Westford USA

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A. Muslin Washington University School of Medicine Department of Internal Medicine, Center for Cardiovascular Research St. Louis USA

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K. Suzuki Niigata University Graduate School of Medical and Dental Sciences Third Department of Medicine Niigata Japan

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H. Tachikawa Niigata University Graduate School of Medical and Dental Sciences First Department of Medicine Niigata Japan

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M. Kodama Niigata University Graduate School of Medical and Dental Sciences First Department of Medicine Niigata Japan

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Y. Aizawa Niigata University Graduate School of Medical and Dental Sciences First Department of Medicine Niigata Japan

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Pages:
277–287
Online Publication Date:
25 Aug 2009
Publication Date:
01 Sep 2009
Article Category:
Journal Article
DOI:
https://doi.org/10.1556/aphysiol.96.2009.3.3
Keywords:
diabetes mellitus; 14-3-3 protein; oxidative stress; cardiomyopathy; apoptosis; hypertrophy; mitogen-activated protein kinase; protein kinase C; glycogen synthase kinase 3 beta
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Cardiovascular disease is a leading cause of death worldwide. Diabetes mellitus is a well-known and important risk factor for cardiovascular diseases. The occurrence of diabetic cardiomyopathy is independent of hypertension, coronary artery disease, or any other known cardiac diseases. There is growing evidence that excess generation of highly reactive free radicals, largely due to hyperglycemia, causes oxidative stress, which further exacerbates the development and progression of diabetes and its complications. Diabetic cardiomyopathy is characterized by morphologic and structural changes in the myocardium and coronary vasculature mediated by the activation of various signaling pathways. Myocardial apoptosis, hypertrophy and fibrosis are the most frequently proposed mechanisms to explain cardiac changes in diabetic cardiomyopathy. Mammalian 14-3-3 proteins are dimeric phosphoserine-binding proteins that participate in signal transduction and regulate several aspects of cellular biochemistry. 14-3-3 protein regulates diabetic cardiomyopathy via multiple signaling pathways. This review focuses on emerging evidence suggesting that 14-3-3 protein plays a key role in the pathogenesis of the cardiovascular complications of diabetes, which underlie the development and progression of diabetic cardiomyopathy.

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Cover Acta Physiologica Hungarica
Acta Physiologica Hungarica
Print ISSN:
0231-424X
Online ISSN:
1588-2683

Senior editors

Editor(s)-in-Chief: Rosivall, László

Honorary Editor(s)-in-Chief): Monos, Emil

Managing Editor(s): Bartha, Jenő; Berhidi, Anna

Co-editor(s): Koller, Ákos; Lénárd, László; Szénási, Gábor

Assistant Editor(s): G. Dörnyei (Budapest), Zs. Miklós (Budapest), Gy. Nádasy (Budapest)

Hungarian Editorial Board

    1. Benedek, György (Szeged)
    1. Benyó, Zoltán (Budapest)
    1. Boros, Mihály (Szeged)
    1. Chernoch, László (Debrecen)
    1. Détári, László (Budapest)
    1. Hamar, János (Budapest)
    1. Hantos, Zoltán (Szeged)
    1. Hunyady, László (Budapest)
    1. Imre, Sándor (Debrecen)
    1. Jancsó, Gábor (Szeged)
    1. Karádi, Zoltán (Pécs)
    1. Kovács, László (Debrecen)
    1. Palkovits, Miklós (Budapest)
    1. Papp, Gyula (Szeged)
    1. Pavlik, Gábor (Budapest)
    1. Spät, András (Budapest)
    1. Szabó, Gyula (Szeged)
    1. Szelényi, Zoltán (Pécs)
    1. Szolcsányi, János (Pécs)
    1. Szollár, Lajos (Budapest)
    1. Szücs, Géza (Debrecen)
    1. Telegdy, Gyula (Szeged)
    1. Toldi, József (Szeged)
    1. Tósaki, Árpád (Debrecen)

International Editorial Board

    1. R. Bauer (Jena)
    1. W. Benjelloun (Rabat)
    1. A. W. Cowley Jr. (Milwaukee)
    1. D. Djuric (Belgrade)
    1. C. Fry (London)
    1. S. Greenwald (London)
    1. O. Hänninen (Kuopio)
    1. H. G. Hinghofer-Szalkay (Graz)
    1. Th. Kenner (Graz)
    1. Gy. Kunos (Richmond)
    1. M. Mahmoudian (Tehran)
    1. T. Mano (Seki, Gifu)
    1. G. Navar (New Orleans)
    1. H. Nishino (Nagoya)
    1. O. Petersen (Liverpool)
    1. U. Pohl (Münich)
    1. R. S. Reneman (Maastricht)
    1. A. Romanovsky (Phoenix)
    1. G. M. Rubanyi (Richmond)
    1. T. Sakata (Oita)
    1. A. Siddiqui (Karachi)
    1. Cs. Szabo (Beverly)
    1. E. Vicaut (Paris)
    1. N. Westerhof (Amsterdam)
    1. L. F. Zhang (Xi'an)

Editorial Office:
Akadémiai Kiadó Zrt.
Prielle Kornélia u. 21–35, H-1117 Budapest, Hungary

Editorial Correspondence:
Acta Physiologica Hungarica
Semmelweis University, Faculty of Medicine Institute of Pathophysiology
Nagyvárad tér 4, H-1089 Budapest, Hungary
Phone/Fax: +36-1-2100-100
E-mail: aph@semmelweis-univ.hu

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Acta Physiologica Hungarica
Language English
Size  
Year of
Foundation		 1950
Publication
Programme		 changed title
Volumes
per Year		  
Issues
per Year		  
Founder Magyar Tudományos Akadémia
Founder's
Address		 H-1051 Budapest, Hungary, Széchenyi István tér 9.
Publisher Akadémiai Kiadó
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 0231-424X (Print)
ISSN 1588-2683 (Online)

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