Ethanol‐induced myocardial ischemia: Close relation between blood acetaldehyde level and myocardial ischemia

Ando, Hiroshi; Abe, Hirohiko; Hisanou, Ryuuichi

doi:10.1002/clc.4960160514

Cited by 20 publications

(14 citation statements)

References 15 publications

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“…While the levels of acetaldehyde in normal subjects are 0.2-5 μM, after ingestion of alcohol or in subjects with liver disease the level is increased 3-30 fold [51]. The salivary acetaldehyde levels of smoking and drinking subjects are quite high with values of 370 μM reported [52].…”

Section: Discussionmentioning

confidence: 99%

Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues

Kundu

Hille

Murugesan

et al. 2007

Archives of Biochemistry and Biophysics

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Aldehyde oxidase, a molybdoflavoenzyme that plays an important role in aldehyde biotransformation, requires oxygen as substrate and produces reduced oxygen species. However, little information is available regarding its importance in cellular redox stress. Therefore, studies were undertaken to characterize its superoxide and hydrogen peroxide production. Aldehyde oxidase was purified to >98% purity and exhibited a single band at ∼290 kDa on native polyacrylamide gradient gel electrophoresis. Superoxide generation was measured and quantitated by cytochrome c reduction and EPR spin trapping with p-dimethyl aminocinnamaldehyde as reducing substrate. Prominent superoxide generation was observed with an initial rate of 295 nmol/min/mg. Electrochemical measurements of oxygen consumption and hydrogen peroxide formation yielded values of 650 nmol/min/mg and 355 nmol/min/mg. In view of the ubiquitous distribution of aldehydes in tissues, aldehyde oxidase can be an important basal source of superoxide that would be enhanced in disease settings where cellular aldehyde levels are increased. KeywordsAldehyde oxidase; Xanthine oxidase; Superoxide; Hydrogen peroxide; Electron paramagnetic resonance; Spin trapping; Cytochrome c reduction; Reactive oxygen species; Free radicals; Oxygen consumption Aldehyde oxidase (AO; EC 1.2.3.1) 1 is a prominent member of the molybdenum hydroxylase family of enzymes, which also includes xanthine oxidoreductase (XOR). XOR has two interconvertible forms, xanthine dehydrogenase (XDH; EC 1.1.1.204) and xanthine oxidase (XO; 1. 1.3.22). Both forms of XOR are involved in the catabolism of purines, * To whom correspondence should be addressed: Davis Heart and Lung Research Institute, 473 W. 12th Ave, Room 110G, The Ohio State University, Columbus, OH 43210. Phone: (614) . E-Mail: Jay.Zweier@osumc.edu. Publisher's Disclaimer: This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain. Both XOR and AO are homodimeric consisting of two identical subunits with an approximate molecular mass of 145 kDa each. Each subunit consists of four discrete regions -two N-terminal domains contain distinct [2Fe-2S] centers. A linker peptide connects it to a 40 kDa FAD binding domain that positions the flavin ring in close proximity and a second linker peptide connects the FAD domain with the 85 kDa C-terminal portion of the protein that contains the molybdenum center and the substrate binding pocket [3,4]. The structure of XOR is well conserved among human, chicken, mouse and rat enzymes [5] and the amino acid sequences reveal that the molybdenum binding site is the most conserved region with 94% homo...

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Section: Discussionmentioning

confidence: 99%

Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues

Kundu

Hille

Murugesan

et al. 2007

Archives of Biochemistry and Biophysics

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“…It has been suggested that acetaldehyde may be instrumental in inducing myocardial ischemia and coronary vasospasm (assessed by both ECG and thallium 201 scintograms) after alcohol consumption (68). The abnormalities were not perturbed by treadmill exercise alone (68). Studies with troponin-T in the rat (described below) support a mechanism involving ischemia.…”

Section: Alcohol and Cardiac Ischemic Damagementioning

confidence: 98%

“…Thus it is not unreasonable to propose mechanisms involving ischemic heart muscle damage in the aetiology of alcoholic heart muscle disease and if this occurs, then a re-perfusion type injury will also ensue. It has been suggested that acetaldehyde may be instrumental in inducing myocardial ischemia and coronary vasospasm (assessed by both ECG and thallium 201 scintograms) after alcohol consumption (68). The abnormalities were not perturbed by treadmill exercise alone (68).…”

Section: Alcohol and Cardiac Ischemic Damagementioning

confidence: 99%

Oxidants antioxidants and alcohol implications for skeletal and cardiac muscle

Preedy¹

1999

Front Biosci

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“…Increased blood AcH level might be responsible for the development of coronary vasospasm and myocardial ischemia [4][5][6]. We suspected according to our patient_s description and clinical presentation that disulfiramalcohol interaction might be a causative mechanism for developing myocardial infarction because of the close temporal relationship between those two events.…”

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confidence: 92%

Acute Myocardial Infarction Due to Disulfiram (Antabus)–Alcohol Interaction

Altun

Erdoğan

2006

Cardiovasc Drugs Ther

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Disulfiram is an irreversible inhibitor of the aldehyde dehydrogenase enzyme (ALDH). It is used since 1940 for the treatment of chronic alcoholism [1]. However, it is not a safe drug. It may cause severe harmful adverse effects secondary to ingestion of disulfiram and alcohol [2,3]. We here present a young man who suffered an inferoposterior myocardial infarction that probably be caused by disulfiram-alcohol interaction.A 36-year-old man was admitted to local hospital because of severe epigastric and retrosternal pain with radiation down to his left arm that is accompanied with nausea and sweating. He was then referred to our hospital 20 h after onset of his complaints. He was diagnosed as having inferoposterior myocardial infarction and commenced conventional therapy including heparin, aspirin, metoprolol, atorvastatin, and enalapril. The past medical history revealed chronic alcoholism and smoking. He had no previous history of any cardiac disorder. He was taking disulfiram (0.5 g/daily) and quit alcohol intake for 7 months. Additionally, he revealed that he had not taken any alcoholic beverages before his symptom onset. Approximately 12 h before his symptoms began, he consumed salad with fermented vinegar for dinner and used aftershave lotion in the morning. On his admission to our hospital, physical examination was unremarkable. He had normal spontaneous breathing. His blood pressure and heart rate were 110/70 mm Hg and 60 bpm, respectively. An ECG showed acute inferoposterior myocardial infarction ( Fig. 1a and b). Laboratory findings were within normal limits except myocardialspecific isoenzyme of creatine kinase 200 U/l (normal range: 0-25) and troponin-I 5.67 ng/ml (normal range: 0-0.4). Blood alcohol and acetaldehyde (AcH) levels were not measured. Blood haemostatic and coagulation parameters such as platelets, fibrinogen, factors V, VIII and others, protein C and antithrombin III were found to be within normal limits. His coronary angiogram revealed normal coronary arteries.Disulfiram is therapeutically used as a pharmacologic adjunct in the treatment of chronic alcoholism. Disulfiram is rapidly and completely absorbed from the gastrointestinal tract although a period of 12 h is required for its full action. Its elimination rate from the body is relatively slow, therefore its effect may persist for several days after the last dose. It is a relatively nontoxic substance. It acts by inhibiting ALDH and subsequently AcH accumulates in the blood. In addition, many other drugs, eg, metronidazole, certain cephalosporins, sulfonylurea, hypoglycemic drugs, and chloral hydrate, have disulfiram-like effects on ethanol metabolism. Disulfiram has little effect on nondrinkers. However, the ingestion of alcohol by individuals previously treated with disulfiram gives rise to marked signs and symptoms such as flushing, throb-

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Ethanol‐induced myocardial ischemia: Close relation between blood acetaldehyde level and myocardial ischemia

Cited by 20 publications

References 15 publications

Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues

Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues

Oxidants antioxidants and alcohol implications for skeletal and cardiac muscle

Acute Myocardial Infarction Due to Disulfiram (Antabus)–Alcohol Interaction

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