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PubMed1990

Oxygen uptake by isolated perfused fish hearts with differing myoglobin concentrations under hypoxic conditions.

Hearts from three species of fish with varying myoglobin content were perfused with stepwise changes in input perfusate PO2 from approximately 160 to 10 mmHg. Flow through the heart, rate of contraction, and afterload were kept constant. This standardized stroke volume and bulk flow of perfusate to the myocytes since these hearts are nourished by the fluid in the ventricular lumen. In some cases NaNO2 was added to the perfusion medium to decrease existing levels of functional myoglobin. Myoglobin-rich hearts were able to extract a constant amount of oxygen until perfusate PO2 had fallen below 80 mmHg. At this point oxygen uptake began to decline. These hearts consumed oxygen until input PO2 was 10 mmHg or less. When normoxic conditions were restored the myoglobin-rich hearts showed complete recovery. Performance was maintained at a constant level over the entire range of input PO2. Myoglobin-poor hearts and nitrite-treated hearts were unable to sustain constant levels of oxygen consumption in the face of a declining perfusate PO2. These hearts were unable to extract oxygen from the medium and failed at perfusate PO2's of 40 mmHg for naturally myoglobin-poor hearts and 30 mmHg for nitrite-treated hearts. Half-maximal oxygen consumptions were attained by myoglobin-rich hearts at lower input PO2's than either myoglobin-poor or nitrite-treated hearts. The impact of myoglobin in intact heart is apparent at relatively high extracellular PO2's (40-80 mmHg) in this model system.

Animals↗
PubMed1988

Mini-myoglobin. The structural significance of haem-ligand interactions.

The properties of purified mini-myoglobin, the fragment 32-139 of horse heart myoglobin reconstituted with protohaem, have been investigated from a structural and functional view point. The recovery of secondary structure observed in the carbon monoxide derivative of mini-myoglobin, as shown by circular dichroism, and the overall similarity of the haem pocket to that of myoglobin, as deduced from the fluorescence properties of the complex with 1-anilino-8-naphthalene sulphonate, indicate that, in the presence of the constraints imposed by the haem and its ligands, the miniprotein reacquires a conformation close to that of native myoglobin. These spectroscopic data parallel the conclusions drawn from the results of ligand combination and dissociation kinetics; stopped-flow experiments indicate that carbon monoxide and oxygen bind to mini-myoglobin with rates almost identical with those of myoglobin itself. The significance of mini-myoglobin as a model of an oxygen-carrying protein, with some of the expected functional characteristics of an ancestor haemoprotein, is discussed, with reference to the mosaic structure of the myoglobin gene and the role of different exons in the evolution of proteins.

Anilino Naphthalenesulfonates↗
PubMed1994

Rapid diagnosis of coronary reperfusion by measurement of myoglobin level every 15 min in acute myocardial infarction.

OBJECTIVES: The purpose of this study was to examine whether coronary reperfusion can be diagnosed rapidly and accurately by myoglobin measurements. BACKGROUND: When intravenous thrombolysis is used for acute myocardial infarction, it is important to determine coronary reperfusion rapidly and noninvasively so that further treatment can be initiated. METHODS: We determined myoglobin, creatine kinase (CK) and creatine kinase, MB fraction (CK-MB) isoenzyme levels in 63 patients with acute myocardial infarction with total occlusion of the infarct-related artery that was confirmed by coronary angiography. Myoglobin was measured by turbidimetric latex agglutination, which has an assay time of 10 min. We measured myoglobin, CK and CK-MB every 15 min in 45 patients with and 18 patients without reperfusion. The condition of the infarct-related artery was confirmed every 5 to 8 min by coronary angiography. RESULTS: The rate of increase in myoglobin, CK, and CK-MB at 15, 30, 45 and 60 min after treatment and reperfusion was significantly higher in the reperfused than in the nonreperfused group. In the reperfused group, the rate of increase in myoglobin was significantly higher than the corresponding rate of increase in CK and CK-MB at 15, 30 and 45 min after reperfusion. When reperfusion was evaluated on the basis of a cutoff level (myoglobin > or = 2.0, CK > or = 1.8, CK-MB > or = 1.5), the predictive accuracy of myoglobin (95%) was significantly higher than that of CK (68%) and CK-MB (73%) at 15 min after reperfusion. CONCLUSIONS: Coronary reperfusion can be rapidly and accurately detected by measurement of the plasma myoglobin every 15 min.

Adult↗
PubMed1988

Adsorption of the protein antigen myoglobin affects the binding of conformation-specific monoclonal antibodies.

Five monoclonal antibodies against sperm whale myoglobin have been used to investigate the physical state of the antigen adsorbed onto a polydimethylsiloxane surface. The binding of each antibody is sensitive to the antigen's conformation in solution while the locations of the antigenic sites on the myoglobin molecule for three of the antibodies have been determined (Berzofsky, J.A., G.K. Buckenmeyer, G. Hicks, F.R.N. Gurd, R.J. Feldmann, and J. Minna. 1982. J. Biol. Chem. 257:3189-3198). The binding of the fluorescein isothiocyanate-labeled IgG and Fab antibodies to previously adsorbed myoglobin has been observed using total internal reflection fluorescence. Three of the antibodies bind specifically to surface-adsorbed myoglobin with affinities at least 50% relative to myoglobin in solution whereas two of the antibodies show affinities for the surface-adsorbed myoglobin diminished by at least two orders of magnitude relative to myoglobin in solution. The specific loss of certain antigenic determinants on the adsorbed myoglobin, coupled with the retention of others, indicates a nonrandom adsorption of the myoglobin molecules.

Adsorption↗
PubMed1998

Diagnostic strategies using myoglobin measurement in myocardial infarction.

Myoglobin, a low molecular-weight heme protein (17800 D) present in both cardiac and skeletal muscle, is an old test with new perspectives. Advantages and disadvantages of myoglobin determination are well known. Myoglobin is the earliest known, commercially available, biochemical marker of acute myocardial infarction (AMI) and its rapid kinetics make it an early, good marker of reperfusion. However, since myoglobin is present in both skeletal and cardiac muscle, any damage to these muscle types results in its release into blood. Serum myoglobin levels are falsely elevated in conditions unrelated to AMI as skeletal muscle and neuromuscular disorders, renal failure, intramuscular injection, strenuous exercise, and after several toxins and drugs intake. New strategies for myoglobin measurement may resolve this limitation. These strategies include both the combined measurement of myoglobin and a skeletal specific marker (carbonic anhydrase III) or a cardiac specific marker (troponin I), as well as the myoglobin evaluation on serial samples. In particular, the diagnostic algorithm based on the combined measurement of myoglobin and troponin I, assuring a satisfactory analytical turnaround time, significantly improves the diagnostic efficiency of laboratory assessment of suspected AMI patients, allowing the successive monitoring of coronary reperfusion.

Biomarkers↗
PubMed1984

Myoglobin determination by high-performance liquid chromatography.

Urine and serum myoglobin have been separated on an anion-exchange column, packed by the slurry technique. Urine or serum was injected directly into the column and eluted isocratically with Tris buffer. Freshly prepared myoglobin from human muscle gives two peaks in the chromatogram. Upon storage, one peak slowly decreases while the other increases in size and has the same capacity factor as horse myoglobin. In myoglobinuria, the latter peak is usually detected in urine, while in serum both peaks are detected. For routine assays, horse myoglobin is used as a standard. The minimum detectable level is 2 mg/l. Urine myoglobin from patients with myoglobinuria ranged from 20 to 3000 mg/l, while normal subjects had undetectable levels. Patients with myoglobinuria also had detectable levels of myoglobin in their serum. Urine myoglobin was found to be unstable; it should be analyzed immediately. Although the present method is not sensitive enough to detect myoglobin in the urine of normal subjects, it is clinically useful for confirming and determining myoglobin in patients with myoglobinuria. It has the advantage of speed and simplicity. Using more sensitive detectors would enhance the usefulness of this method.

Animals↗
PubMed2002

The effect of anions on azide binding to myoglobin: an unusual functional modulation.

The effect of increasing concentrations of several anions on the azide (N(-)(3)) binding properties of sperm whale and horse ferric myoglobin has been studied. Surprisingly, a number of anions may act as heterotropic effectors, decreasing the affinity of myoglobins for N(-)(3), in the following order: ClO(-)(4)=I(-)>Br(-)>Cl(-) and SO(2-)(4), which mirrors the increase in their charge density. The largest effects were measured using ClO(-)(4) and I(-), which produce a 4-fold and 8-fold reduction of the N(-)(3) binding affinity in horse and sperm whale myoglobins, respectively. A dissociation equilibrium constant (K(d)) ranging from 150 to 250 mM was estimated for ClO(-)(4) and I(-) binding to myoglobins. In order to analyse the molecular mechanism producing the reduction of the N(-)(3) binding affinity to ferric myoglobin, the potential anionic binding sites within ferric myoglobin were investigated by a molecular modelling study using the program Grid. Analysis of the theoretical results suggests two particularly favourable binding sites: the first, next to the distal side of the haem, whose occupancy might alter the electrostatic potential surrounding the bound N(-)(3); the second, involving residues of helices B and G which are far from the haem iron atom, thus implying a long range effect on the bound N(-)(3). Based on the evidence that no significant conformational changes are found in the three-dimensional structures of N(-)(3)-free and N(-)(3)-bound myoglobin and on previous results on N(-)(3) binding to ferric myoglobin mutants in CD3 positions, we favour the first hypothesis, suggesting that the functional heterotropic modulation of monomeric myoglobin is mainly depending on a decrease of the positive charge density induced by the binding of anions to the haem distal side.

Allosteric Regulation↗
PubMed1997

Comparative studies of the indoleamine dioxygenase-like myoglobin from the abalone Sulculus diversicolor.

The abalone Sulculus diversicolor contains abundant myoglobin in its buccal mass. The myoglobin is homodimeric and the molecular mass of the constituent polypeptide chain is 41,000 Da. The amino acid sequence and gene structure are highly homologous with those of a vertebrate tryptophan-degrading enzyme, indoleamine dioxygenase (IDO). Thus Sulculus myoglobin evolved from an IDO gene, and represents a typical case of functional convergence. The oxygen equilibrium properties of Sulculus myoglobin were examined and compared with those of myoglobins from other sources. It binds oxygen reversibly, and the P50 was determined to be 3.8 mmHg at 20 degrees C and pH 7.4, showing that the oxygen affinity of Sulculus myoglobin is significantly lower than those of usual 16 kDa myoglobins. It also displays no cooperativity (nmax: 1.02-1.06) and no alkaline Bohr effect between pH 7.0 and 7.9. The cDNA-derived amino acid sequences of vertebrate IDOs, molluscan IDO-like myoglobins and a homolog in the yeast Saccharomyces were aligned, and several amino acid residues were proposed as candidates for key residues to control the function of IDO or myoglobin.

Amino Acid Sequence↗
PubMed2002

The prognostic value of serum myoglobin in patients with non-ST-segment elevation acute coronary syndromes. Results from the TIMI 11B and TACTICS-TIMI 18 studies.

OBJECTIVES: The goal of this study was to define the prognostic value of serum myoglobin in patients with non-ST-elevation acute coronary syndromes (ACS). BACKGROUND: While myoglobin is useful for the early diagnosis of myocardial infarction (MI), its role in the early risk-stratification of patients with ACS has not been established. METHODS: Myoglobin, creatine kinase-MB subfraction (CK-MB) and troponin I (cTnI) were measured at randomization in 616 patients from the Thrombolysis In Myocardial Ischemia/Infarction (TIMI) 11B study and 1,841 patients from the Treat Angina with Aggrastat and Determine Cost of Therapy with an Invasive or Conservative Therapy-Thrombolysis In Myocardial Ischemia/Infarction (TACTICS-TIMI) 18 study. The risks for death and nonfatal MI through six months of follow-up were compared between patients with and without myoglobin elevation (>110 microg/l) in each study and in a dataset combining all eligible patients from both studies (n = 2,457). RESULTS: In a multivariate model adjusting for baseline characteristics, ST changes and CK-MB and cTnI levels, an elevated baseline myoglobin was associated with increased six-month mortality in TIMI 11B (adjusted odds ratio [OR] 2.9 [95% confidence interval [CI] 1.2 to 7.1]), TACTICS-TIMI 18 (adjusted OR 3.0 [95% CI 1.5 to 5.9]) and the combined dataset (adjusted OR 3.0 [95% CI 1.8 to 5.0]). In contrast, there was no significant association between myoglobin elevation and nonfatal MI (combined dataset adjusted OR 1.55, 95% CI 0.9 to 2.6). In TACTICS-TIMI 18, patients with versus those without myoglobin elevation were more likely to have an occluded culprit artery (28% vs. 10%; p < 0.0001) and visible thrombus (49% vs. 34%; p = 0.006) and less likely to have TIMI 3 flow (53% vs. 68%; p = 0.009). CONCLUSIONS: A serum concentration of myoglobin above the MI detection threshold (>110 microg/l) is associated with an increased risk of six-month mortality, independent of baseline clinical characteristics, electrocardiographic changes and elevation in CK-MB and cTnI. These findings suggest that myoglobin may be a useful addition to cardiac biomarker panels for early risk-stratification in ACS.

Acute Disease↗
PubMed2002

Blue myoglobin reconstituted with an iron porphycene shows extremely high oxygen affinity.

Myoglobin will be a good scaffold for engineering a function into proteins. To modulate the physiological function of myoglobin, almost all approaches have been demonstrated by site-directed mutagenesis, however, there are few studies which show a significant improvement in the function. In contrast, we focused on the replacement of heme in the protein with an artificial prosthetic group. Recently, we prepared a novel myoglobin reconstituted with an iron porphycene as a structural isomer of mesoheme. The bluish colored reconstituted myoglobin is relatively stable and the deoxymyoglobin reversibly binds ligands. Interestingly, the O2 affinity of the reconstituted myoglobin, 1.1 x 109 M-1, is a significant 1,400-fold higher than that of the native myoglobin. Furthermore, the unfavorable autoxidation kinetics show 7-fold decrease in rate for the reconstituted myoglobin relative to the native myoglobin, indicating the stable oxy-form against autoxidation. The net results come from the slow dissociation of the O2 ligand in the reconstituted myoglobin, koff = 0.11 s-1, because of the formation of strong hydrogen bond between His64 and negatively charged dioxygen. The present study indicates that the replacement of native heme with an artificially created prosthetic group will give us a unique function into a hemoprotein.

Heme↗
PubMed2004

Ligand binding properties of myoglobin reconstituted with iron porphycene: unusual O2 binding selectivity against CO binding.

Sperm whale myoglobin, an oxygen storage hemoprotein, was successfully reconstituted with the iron porphycene having two propionates, 2,7-diethyl-3,6,12,17-tetramethyl-13,16-bis(carboxyethyl)porphycenatoiron. The physicochemical properties and ligand bindings of the reconstituted myoglobin were investigated. The ferric reconstituted myoglobin shows the remarkable stability against acid denaturation and only a low-spin characteristic in its EPR spectrum. The Fe(III)/Fe(II) redox potential (-190 mV vs NHE) determined by the spectroelectrochemical measurements was much lower than that of the wild-type. These results can be attributed to the strong coordination of His93 to the porphycene iron, which is induced by the nature of the porphycene ring symmetry. The O2 affinity of the ferrous reconstituted myoglobin is 2600-fold higher than that of the wild-type, mainly due to the decrease in the O2 dissociation rate, whereas the CO affinity is not so significantly enhanced. As a result, the O2 affinity of the reconstituted myoglobin exceeds its CO affinity (M' = K(CO)/K(O2) < 1). The ligand binding studies on H64A mutants support the fact that the slow O2 dissociation of the reconstituted myoglobin is primarily caused by the stabilization of the Fe-O2 sigma-bonding. The IR spectra for the carbon monoxide (CO) complex of the reconstituted myoglobin suggest several structural and/or electrostatic conformations of the Fe-C-O bond, but this is not directly correlated with the CO dissociation rate. The high O2 affinity and the unique characteristics of the myoglobin with the iron porphycene indicate that reconstitution with a synthesized heme is a useful method not only to understand the physiological function of myoglobin but also to create a tailor-made function on the protein.

Animals↗
PubMed1997

Myoglobin toxicity in proximal human kidney cells: roles of Fe, Ca2+, H2O2, and terminal mitochondrial electron transport.

The purpose of this study was to gain direct insights into mechanisms by which myoglobin induces proximal tubular cell death. To avoid confounding systemic and hemodynamic influences, an in vitro model of myoglobin cytotoxicity was employed. Human proximal tubular (HK-2) cells were incubated with 10 mg/ml myoglobin, and after 24 hours the lethal cell injury was assessed (vital dye uptake; LDH release). The roles played by heme oxygenase (HO), cytochrome p450, free iron, intracellular Ca2+, nitric oxide, H2O2, hydroxyl radical (-OH), and mitochondrial electron transport were assessed. HO inhibition (Sn protoporphyrin) conferred almost complete protection against myoglobin cytotoxicity (92% vs. 22% cell viability). This benefit was fully reproduced by iron chelation therapy (deferoxamine). Conversely, divergent cytochrome p450 inhibitors (cimetidine, aminobenzotriazole, troleandomycin) were without effect Catalase induced dose dependent cytoprotection, virtually complete, at a 5000 U/ml dose. Conversely, -OH scavengers (benzoate, DMTU, mannitol), xanthine oxidase inhibition (oxypurinol), superoxide dismutase, and manipulators of nitric oxide expression (L-NAME, L-arginine) were without effect. Intracellular (but not extracellular) calcium chelation (BAPTA-AM) caused approximately 50% reductions in myoglobin-induced cell death. The ability of Ca2+ (plus iron) to drive H2O2 production (phenol red assay) suggests one potential mechanism. Blockade of site 2 (antimycin) and site 3 (azide), but not site 1 (rotenone), mitochondrial electron transport significantly reduced myoglobin cytotoxicity. Inhibition of Na, K-ATPase driven respiration (ouabain) produced a similar protective effect. We conclude that: (1) HO-generated iron release initiates myoglobin toxicity in HK-2 cells; (2) myoglobin, rather than cytochrome p450, appears to be the more likely source of toxic iron release; (3) H2O2 generation, perhaps facilitated by intracellular Ca2+/iron, appears to play a critical role; and (4) cellular respiration/terminal mitochondrial electron transport ultimately helps mediate myoglobin's cytotoxic effect. Formation of poorly characterized toxic iron/H2O2-based reactive intermediates at this site seems likely to be involved.

Antioxidants↗
PubMed1986

Muscle cell leakage of myoglobin after long-term exercise and relation to the individual performances.

Muscle protein release was studied during and after prolonged exercise by means of serum myoglobin determinations. Increased serum myoglobin levels were regularly found after performance of long-term exercise. The correlations (P less than 0.001) to muscle enzymes indicated nonselective release from muscle cells. Myoglobin measured after completed exercise was correlated to the finishing time in a ski race, i.e., the fast skiers showed lower myoglobin levels than slow skiers. Inexperienced skiers and also skiers older than 49 years of age were found to have higher myoglobin levels than the others although the mean finishing times were similar. Myoglobin measured during and after 5 h of bicycle exercise showed large differences even though the relative work load was identical. Myoglobin started to rise 1.2 h (median) after the commencement of the bicycle exercise. The time at which myoglobin started to rise correlated (P less than 0.01) with the myoglobin levels after completed exercise and was not related to the physical fitness of the individuals. The results indicated considerable individual differences with regard to muscle protein leakage during exercise. The leakage is not simply related to the individual's apparent physical fitness but probably also to constitutional factors, such as age and metabolic capacity of the muscle cells.

Adult↗
PubMed1987

Myoglobin-mediated oxygen delivery to mitochondria of isolated cardiac myocytes.

Myoglobin-mediated oxygen delivery to intracellular mitochondria is demonstrated in cardiac myocytes isolated from the hearts of mature rats. Myocytes are held at high ambient oxygen pressure, 40-340 torr (5-45 kPa); sarcoplasmic myoglobin is fully oxygenated. In this condition oxygen availability does not limit respiratory rate; myoglobin-facilitated diffusion contributes no additional oxygen flux and, since oxygen consumption is measured in steady states, the storage function of myoglobin vanishes. Carbon monoxide, introduced stepwise, displaces oxygen from intracellular oxymyoglobin without altering the optical spectrum of the largely oxidized intracellular mitochondria. A large part, about one-third, of the steady-state oxygen uptake is abolished by carbon monoxide blockade of myoglobin oxygenation. The myoglobin-dependent component of the oxygen uptake decreases linearly with decreasing fraction of intracellular oxymyoglobin, with a slope near unity. Studies using inhibitors of mitochondrial electron transport indicate that myoglobin-delivered oxygen uptake depends on electron flow through the mitochondrial electron transport chain. We conclude that cardiac mitochondria accept two additive simultaneous flows of oxygen: a flow of dissolved oxygen to cytochrome oxidase and a flow of myoglobin-bound oxygen to a mitochondrial terminus. Myoglobin-mediated oxygen delivery supports ATP generation by heart cells at physiological ambient oxygen pressure.

Animals↗
PubMed1998

A causative role for redox cycling of myoglobin and its inhibition by alkalinization in the pathogenesis and treatment of rhabdomyolysis-induced renal failure.

Muscle injury (rhabdomyolysis) and subsequent deposition of myoglobin in the kidney causes renal vasoconstriction and renal failure. We tested the hypothesis that myoglobin induces oxidant injury to the kidney and the formation of F2-isoprostanes, potent renal vasoconstrictors formed during lipid peroxidation. In low density lipoprotein (LDL), myoglobin induced a 30-fold increase in the formation of F2-isoprostanes by a mechanism involving redox cycling between ferric and ferryl forms of myoglobin. In an animal model of rhabdomyolysis, urinary excretion of F2-isoprostanes increased by 7.3-fold compared with controls. Administration of alkali, a treatment for rhabdomyolysis, improved renal function and significantly reduced the urinary excretion of F2-isoprostanes by approximately 80%. EPR and UV spectroscopy demonstrated that myoglobin was deposited in the kidneys as the redox competent ferric myoglobin and that it's concentration was not decreased by alkalinization. Kinetic studies demonstrated that the reactivity of ferryl myoglobin, which is responsible for inducing lipid peroxidation, is markedly attenuated at alkaline pH. This was further supported by demonstrating that myoglobin-induced oxidation of LDL was inhibited at alkaline pH. These data strongly support a causative role for oxidative injury in the renal failure of rhabdomyolysis and suggest that the protective effect of alkalinization may be attributed to inhibition of myoglobin-induced lipid peroxidation.

Animals↗
PubMed2002

Analysis of the myoglobin gene in Tibetans living at high altitude.

Myoglobin, a protein with an important role in muscle oxidative metabolism, is increased in high altitude residents. In the closely related hemoglobins, mutations cause or contribute to human disease. Furthermore, heme-containing proteins may be involved in oxygen sensing. We therefore tested the hypotheses that myoglobin allele frequencies differed in Tibetans, a long-resident human high-altitude population, compared with sea-level residents, and varied in relation to altitude among Tibetans. We obtained the sequence of exon 2 of the myoglobin gene in 146 Tibetans with greater than three generations of stable residence at altitude in rural Tibet. We compared the frequency of known polymorphic sites in this gene among Tibetans living at altitudes of 3000, 3700, and 4500 m and to allele frequencies previously obtained in 525 residents of Dallas, Texas. We also examined the association between different myoglobin genotypes and hemoglobin concentration, used as an index of myoglobin levels. The frequency of the myoglobin 79A allele was higher in the high altitude compared with the sea-level residents, but unchanged with increasing altitude among Tibetans. There was no significant deviation from Hardy-Weinberg equilibrium in any of the Tibetan altitude groups, nor was there any association between myoglobin genotype and hemoglobin concentration. Screening of exon 2 of the myoglobin gene in high altitude Tibetans does not show novel polymorphism or selection for specific myoglobin alleles as a function of altitude of residence or hypoxic challenge.

Altitude↗
PubMed2003

Contribution of myoglobin-induced increases in vascular resistance to shock decompensation in experimental Crush-syndrome in anesthetized rats.

Myoglobin is known to become nephrotoxic when released in greater amounts from skeletal muscle into the general circulation during shock. The present study deals with the question as to whether a myoglobin-induced increase in vascular tone additionally contributes to the detrimental role of this protein in hypovolemic shock. Anesthetized rats were subjected to 250 mg kg x h(-1) myoglobin infused i.v. during hemorrhagic hypotension of 50 mmHg. Shock survival time was measured, as were blood flow and vascular resistance in kidney, intestine, brain, and heart, using the microsphere method. Rats subjected to only myoglobin or hemorrhage survived a period of >120 min; in contrast, rats, exposed to both myoglobin and hemorrhage died at 68 +/- 9 min. When the animals subjected to only hemorrhage and to myoglobin/ hemorrhage were compared, significantly lower values were found in the latter group with respect to blood flow in the kidney (1.7 +/- 0.1 vs. 0.2 +/- 0.05 ml x min(-1) x g(-1)), small intestine (1.0 +/- 0.1 vs. 0.5 +/- 0.1 ml x min(-1) x g(-1)), cardiac output (112 +/- 5 vs. 62 +/- 10 ml(-1) x min(-1) x kg(-1)), and significantly higher values of total peripheral vascular resistance (0.45 +/- 0.02 vs. 0.81 +/- 0.12 mmHg x min x ml(-1) x kg) at 50 min of hypotension. It is assumed that these effects of myoglobin are induced by its ability to scavenge endogenous nitric oxide, because a modified, non-nitrosylable myoglobin was unable to induce such effects. The results support the view that a pathological release of myoglobin into the general circulation causes increases in vascular resistance of vital organs that may contribute to decompensation of tissue supply when occurring in hypovolemic shock.

Animals↗
PubMed1996

Serial myoglobin levels for patients with possible myocardial infarction.

OBJECTIVES: To determine the sensitivity and specificity of a new myoglobin assay for acute myocardial infarction (AMI), considering both the total amount of serum myoglobin and its percentage change over 2 hours. METHODS: A prospective, observational test performance study for the recognition of AMI was done using serial myoglobin assays of 42 admitted chest pain patients at a large, urban teaching hospital ED. Myoglobin testing was performed at presentation (time 0) and at 1 and 2 hours after arrival. A myoglobin level > 100 micrograms/L (ng/mL) or a change > or = 50% from baseline (increase or decrease) any time during the 2-hour period was considered positive. Patients and their physicians were blinded to the myoglobin results. The managing clinician's final diagnosis of the presenting event was used as the diagnostic criterion standard. RESULTS: The sensitivity of the myoglobin technique for detection of AMI in the first hours in the ED was 13/14 (93%; 95% CI: 66-100%). The 1 patient who had a false-negative test had evidence of AMI on the ECG and an initially abnormal creatine kinase-MB (CK-MB) assay. The specificity was 22/28 (79%; 59-92%). However, of the 6 patients who had "false-positive" myoglobin tests, all had serious illness: significant cardiac disease (n = 4), in-hospital death (n = 1), or deep venous thrombosis (n = 1). CONCLUSION: Myoglobin level determinations are sensitive tests to detect AMI during the first 2 hours of a patient's stay in the ED and may complement current clinical tools.

Adolescent↗