CLINICAL RESEARCH: HEART FAILURE
Increased myocardial NADPH oxidase activity in human heart failure
Christophe Heymes, PhD*,
Jennifer K. Bendall, MSc*,
Philippe Ratajczak ,
Alison C. Cave, PhD*,
Jane-Lise Samuel, MD, PhD,
Gerd Hasenfuss, MD and
Ajay M. Shah, MD, FRCP, FAHA*,*
* Department of Cardiology, Guy’s King’s and St. Thomas’s School of Medicine, King’s College London, United Kingdom
INSERM U572, IFR Circulation, Hôpital Lariboisiere, Paris, France
Department of Cardiology, University of Göttingen, Germany
Manuscript received October 14, 2002;
revised manuscript received December 2, 2002,
accepted December 12, 2002.
* Reprint requests and correspondence: Prof. Ajay M. Shah, Department of Cardiology, GKT School of Medicine, Bessemer Road, London SE5 9PJ, United Kingdom.
ajay.shah{at}kcl.ac.uk
OBJECTIVES: This study was designed to investigate whether nicotinamide adenine dinucleotide 3-phosphate (reduced form) (NADPH) oxidase is expressed in the human heart and whether it contributes to reactive oxygen species (ROS) production in heart failure.
BACKGROUND: A phagocyte-type NADPH oxidase complex is a major source of ROS in the vasculature and is implicated in the pathophysiology of hypertension and atherosclerosis. An increase in myocardial oxidative stress due to excessive production of ROS may be involved in the pathophysiology of congestive heart failure. Recent studies have suggested an important role for myocardial NADPH oxidase in experimental models of cardiac disease. However, it is unknown whether NADPH oxidase is expressed in the human myocardium or if it has any role in human heart failure.
METHODS: Myocardium of explanted nonfailing (n = 9) and end-stage failing (n = 13) hearts was studied for the expression of NADPH oxidase subunits and oxidase activity.
RESULTS: The NADPH oxidase subunits p22phox, gp91phox, p67phox, and p47phox were all expressed at messenger ribonucleic acid and protein level in cardiomyocytes of both nonfailing and failing hearts. NADPH oxidase activity was significantly increased in end-stage failing versus nonfailing myocardium (5.86 ± 0.41 vs. 3.72 ± 0.39 arbitrary units; p < 0.01). The overall level of oxidase subunit expression was unaltered in failing compared with nonfailing hearts. However, there was increased translocation of the regulatory subunit, p47phox, to myocyte membranes in failing myocardium.
CONCLUSIONS: This is the first report of the presence of NADPH oxidase in human myocardium. The increase in NADPH oxidase activity in the failing heart may be important in the pathophysiology of cardiac dysfunction by contributing to increased oxidative stress.
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Abbreviations and Acronyms
| | CHF | = congestive heart failure | | DPI | = diphenyleneiodonium | | L-NAME | = N -nitro-L-arginine methyl ester hydrochloride | | mRNA | = messenger ribonucleic acid | | NADPH | = nicotinamide adenine dinucleotide3-phosphate (reduced form) | | O2– | = superoxide | | ROS | = reactive oxygen species |
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