Myoglobinuria in myocardial infarction

Levine, Richard S.; Alterman, Marvin; Gubner, Richard; Adams, Ernest C.

doi:10.1097/00000441-197109000-00006

Cited by 33 publications

(7 citation statements)

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“…These results also lead us to a new view that a good supply of oxygen provides a rather important defense against the oxidation of myoglobin with hydrogen peroxide, one of the most potent oxidants found in situ. This view seems to be of clinical importance in the oxygen supply to red muscles, because ischemia is known to cause abrupt cell destruction in cardiac and skeletal muscle tissues (Levine et al, 1971;Kagen et al, 1975).…”

Section: Calculations and Discussionmentioning

confidence: 99%

Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation

Wazawa

Matsuoka

Tajima

et al. 1992

Biophysical Journal

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The stability properties of the iron(II)-dioxygen bond in myoglobin and hemoglobin are of particular importance, because both proteins are oxidized easily to the ferric met-form, which cannot be oxygenated and is therefore physiologically inactive. In this paper, we have formulated all the possible pathways leading to the oxidation of myoglobin to metmyoglobin with each required rate constant in 0.1 M buffer (pH 7.0) at 25 degrees C, and have set up six rate equations for the elementary processes going on in a simultaneous way. By using the Runge-Kutta method to solve these differential equations, the concentration progress curves were then displayed for all the reactive species involved. In this complex reaction, the primary event was the autoxidation of MbO2 to metMb with generation of the superoxide anion, this anion being converted immediately and almost completely into H2O2 by the spontaneous dismutation. Under air-saturated conditions (PO2 = 150 Torr), the H2O2 produced was decomposed mostly by the metMb resulting from the autoxidation of MbO2. At lower pressures of O2, however, H2O2 can act as the most potent oxidant of the deoxyMb, which increases with decreasing O2 pressures, so that there appeared a well defined maximum rate in the formation of metMb at approximately 5 Torr of oxygen. Such examinations with the aid of a computer provide us, for the first time, with a full picture of the oxidation reaction of myoglobin as a function of oxygen pressures. These results also seem to be of primary importance from a point of view of clinical biochemistry of the oxygen supply, as well as of pathophysiology of ischemia, in red muscles such as cardiac and skeletal muscle tissues.

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Section: Calculations and Discussionmentioning

confidence: 99%

Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation

Wazawa

Matsuoka

Tajima

et al. 1992

Biophysical Journal

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“…In several studies, single daily samples only were tested (Levine et al, 1971;Saranchak and Bernstein, 1974). Kessler and his associates (1975) examined samples of all urine passed in the first 24 hours, with analysis of single random samples over the next 3 days.…”

Section: Discussionmentioning

confidence: 99%

“…It has been shown recently that after acute myocardial infarction, myoglobin is released from damaged heart muscle into the blood stream and is then cleared rapidly from the circulation and excreted in the urine (Kagen, 1973). Several studies have indicated that the detection of myoglobin in the urine may be a useful additional test in the diagnosis of acute myocardial necrosis in man (Strausser, Rothfeld, and Bucsi, 1966;Adams and Elliott, 1970;Levine et al, 1971;Saranchak and Bernstein, 1974;Kessler et al, 1975). If the total amount is related to the amount of muscle necrosis, then measurements of myoglobinuria could be relevant to an understand-Received for publication 8 July 1976 ing of the evolution of the infarction process.…”

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confidence: 99%

Excretion of myoglobin in urine after actue myocardial infarction.

Donald¹,

Cloonan²,

Neale³

et al. 1977

Heart

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We studied myoglobin excretion in 33 patients admitted to the coronary care unit with a provisional diagnosis of acute myocardial infarction. Sixteen proved to have definite and uncomplicated acute myocardial infarction and 17 possible infarction, using WHO criteria. For 5 days after admission, aliquots of every urine specimen voided by each patient were analysedfor myoglobin using an immunochemical method able to detect a minimum urinary myoglobin concentration of 0-02 mg/ml. Myoglobinuria was detected in 14 of the 16 patients with definite infarction but was not found in any of the 1 7 patients with possible infarction. There were 3 patterns of myoglobin excretion. In 8 of the 14 patients it was excreted in one episode starting 10 to 40 hours after the onset of chest pain and lasting for 5 to 45 hours. In 3 of the remaining patients it was excreted over a much longer period (mean 83 hours) and in the final 3 patients myoglobinuria occurred in 2 or 3 intermittent episodes with periods of between 10 and 20 hours during which it was not detected. Total myoglobin excretion, which varied between 2 and 100 mg (mean 51 mg), did not correlate with peak serum enzyme levels. We concluded that in the appropriate clinical setting, the finding of myoglobinuria provides additional evidence for a diagnosis of acute myocardial infarction. The variable myoglobin excretion pattern suggests that in seemingly uncomplicated myocardial infarction there is considerable variation between patients in the pattern of evolution of the infarction process. This may be relevant to the assessment of measures directed towards limiting infarct size.

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“…Other organs have also been shown to be the source of such liberated tissue antigens during disease [28], e.g. : myoglobinuria, occurring after strenuous exercise or myocardi al infarction [29,30]; urinary excretion of pepsin in hypertrophic gastritis [31]; excretion of liver antigens in experimental hepatic diseases [32,33], and urinary excretion of testis antigens during experimental testicular necrosis produced surgically or by cadmium poisoning [34].…”

Section: Discussionmentioning

confidence: 99%

Two Pancreas ‘Tissue-Specific’ Antigens in Normal Human Urine, One Being an Esterase

Greene¹,

Halbert²,

Kiefer³

1975

Int Arch Allergy Immunol

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Hyperimmune antiserum to human pancreas was exhaustively absorbed with plasma, kidney, and submaxillary gland. The resulting antiserum showed up to seven antigens in pancreas extracts by gel diffusion methods, but failed to react detectably with extracts of 17 other organs and tissues. However, this apparently ‘tissue-specific’ anti-pancreas reagent regularly revealed two of the pancreas antigens in normal human urine concentrates. One of the latter was an anodal esterase. Although the identity of the second is not yet known, it was shown to be devoid of the following enzyme activities: amylase, catalase, glucosaminidase, glucuronidase, cystine-aminopeptidase, phosphatases and sulfatase.

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Myoglobinuria in myocardial infarction

Cited by 33 publications

References 0 publications

Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation

Hydrogen peroxide plays a key role in the oxidation reaction of myoglobin by molecular oxygen. A computer simulation

Excretion of myoglobin in urine after actue myocardial infarction.

Two Pancreas ‘Tissue-Specific’ Antigens in Normal Human Urine, One Being an Esterase

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