Gene/Protein Disease Symptom Drug Enzyme Compound
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 47,337 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The excessive release of myoglobin following extensive skeletal muscle trauma, burns, and myopathies may result in renal dysfunction. Due to its molecular size, myoglobin is filtered through the glomerulus and is in part reabsorbed by the tubular system. intraluminal deposition of myoglobin following renal hypoperfusion and the impact of endogenous mediators on cell function contribute to the pathogenesis of acute renal failure. The present study was aimed to investigate the relation between myoglobin and renal function in polytraumatized patients. Thirty-four patients with an Injury Severity Score (ISS) of 28 +/- 3.1 (SEM) and a mean age of 39.5 years (range 18-70) were studied prospectively. Myoglobin, sodium, and creatinine concentrations in plasma and urine were determined 8-hourly. Myoglobin excretion, fractional myoglobin excretion, myoglobin clearance, creatinine clearance, and fractional excretion of sodium were calculated. The mean concentration of plasma myoglobin on the 1st day post-trauma was 3087 ng/ml. A continuous decrease in plasma myoglobin concentration could be observed, with a mean value of 497 ng/ml on day 7. The myoglobin concentration in urine showed marked fluctuations: the mean values were 3.37-4.12 mg/ml on day 1 and 0.78-1.34 mg/ml on day 7. There was no correlation between plasma and urine myoglobin concentrations. The myoglobin concentration increased during the period of observation, but there was no correlation with the creatinine clearance. The fractional excretion of myoglobin was in the range of 1% to 14%. There was no correlation between the fractional excretions of myoglobin and sodium.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Myoglobin release and renal function in polytraumatized patients in intensive care]. 237 88

Enzyme-linked immunosorbent assay (ELISA) was used to detect the presence of protein-acetaldehyde adducts (-AAs) in human serum samples. Two methods were compared: (1) direct ELISA: samples, rabbit anti-hemocyanin-AA IgG, and beta-galactosidase (beta-gal) conjugated goat anti-rabbit serum IgG added to a 96-well ELISA plate in a stepwise manner; and (2) two-site or sandwich ELISA: serum samples added to an ELISA plate that had been precoated with anti-hemocyanin-AA IgG (the capture antibody) and incubated stepwise with biotinated anti-hemocyanin-AA IgG (the signal antibody) and avidin-beta-gal conjugates. Serum protein-AA levels were then assayed by bound beta-gal activities at OD405. When human hemoglobin (Hgb)-AA was used as a model protein-AA for the sandwich ELISA, the EC50 (estimated concentration that corresponds to 50% of the OD405 response range) was 7 ng/ml. Direct ELISA was less sensitive (EC50 of 120 ng/ml). Adding control human serum to Hgb-AA increased the EC50 of the direct ELISA more than the sandwich ELISA. Intra- and interassay coefficients of variance for sandwich ELISA were both about 8%. Detection of Hgb-AA by sandwich ELISA was highly specific. The above results with anti-hemocyanin-AA IgG were also obtained when anti-myoglobin-AA IgG was used in sandwich ELISA. Using sandwich ELISA and anti-hemocyanin-AA IgG, OD405 for sera of control subjects and alcoholic patients were 0.036 +/- 0.033 (+/- SEM, n = 28) and 0.150 +/- 0.088 (n = 28), respectively. Serum protein-AAs reacted more strongly with anti-myoglobin-AA IgG than anti-hemocyanin-AA IgG.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Protein-acetaldehyde adducts in serum of alcoholic patients. 237 29

The effects of 30 min running with stepwise increasing intensity (exhaustive, energy demand approx. 50----100% of VO2max), 60 s supramaximal running (anaerobic, greater than or equal to 125% of VO2max) and 40-60 min low-intensity running (aerobic, 40-60% of VO2max) on serum concentration of muscle-derived proteins were studied in 5 male and 5 female elite orienteerers. S-Carbonic anhydrase III (S-CA III) was used as a marker of protein leakage from type I (slow oxidative) muscle fibres and S-myoglobin (S-Mb) as a non-selective (type I + II) muscular marker. The fractional increase in S-CA III (delta S-Ca III) was 0.37 +/- 0.09 (mean +/- SEM, p less than 0.001), 0.10 +/- 0.05 (N. S.) and 0.46 +/- 0.09 (p less than 0.001) 1 h after exhaustive, anaerobic and aerobic exercise, respectively. The corresponding values for delta S-Mb were 1.45 +/- 0.36 (p less than 0.001), 0.39 +/- 0.13 (p less than 0.01) and 0.67 +/- 0.18 (p less than 0.001). The value for the delta S-CA III/delta S-Mb ratio was 0.68 +/- 0.03 after the aerobic exercise, but only 0.25-0.26 (p vs. aerobic exercise less than 0.001) after the two high-intensity forms of exercise. Since type I fibres of skeletal muscle are known to be responsible for power production during low-intensity exercise, whereas fibres of both type I and type II are active at higher intensities, the delta S-CA III/delta S-Mb ratio may depend on the recruitment profile of type I vs. type I + II fibres.
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PMID:Serum carbonic anhydrase III, an enzyme of type I muscle fibres, and the intensity of physical exercise. 250 Jun 39

To better define the usefulness of blood myoglobin measurements in evaluating the effectiveness of attempted thrombolysis, we studied the kinetics of myoglobin entry into and removal from the circulation after coronary artery reperfusion and the relation between directly measured depletion of myocardial myoglobin after coronary occlusion and reperfusion and the amount of depletion predicted from plasma myoglobin concentration-time curves. Initially, canine myoglobin was administered to 11 dogs by both bolus injection and 40-minute infusion, and the subsequent disappearance patterns of myoglobin from plasma monitored by radioimmunoassay. A monoexponential regression line (corresponding to a one-compartment model) and a biexponential regression line (corresponding to a two-compartment model) were determined for each set of washout data, the kinetic parameters were calculated, and the goodness of fit of each model was assessed. Results were similar after both methods of myoglobin administration. In five of 11 animals, the one-compartment model described the myoglobin kinetics better; in the other six animals, the two-compartment model was statistically superior, but values for the volume of distribution and elimination rate constant differed by only 10% from the one-compartment estimates. After bolus administration of myoglobin and with a one-compartment model, the volume of distribution of myoglobin was determined to be 1,601 +/- 77 (SEM) ml, representing 6.8 +/- 0.2% of total body weight; the elimination rate constant averaged 0.132 +/- 0.006/min and corresponded to a mean half-time of disappearance of 5.5 +/- 0.2 minutes.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Kinetics of myoglobin release and prediction of myocardial myoglobin depletion after coronary artery reperfusion. 276 16

This paper describes the preparation of charged and uncharged protein molecular probes for study of the permselectivity of renal capillaries. Horse heart myoglobin was used as a neutral myoglobin. Since it contained several fractions with different isoelectric points, it was purified by fast protein liquid chromatography (FPLC). To obtain a negatively charged myoglobin, the original horse heart myoglobin was treated with cyanate, resulting in net charge of -5.7 +/- 0.3 at physiological pH (mean +/- SEM). The charge was determined from the Donnan potential which develops over a semipermeable membrane separating the inside solution in which the protein was dissolved from a surrounding bath of equal ionic strength. Sperm whale myoglobin was similarly purified by FPLC and used as a positively (+1.7 +/- 0.2) charged isomer. Horseradish peroxidase (HRP) was purified by means of gel and ion-exchange chromatography and found to be neutral at physiological pH. Negatively charged (-14.0 +/- 0.5) HRP was obtained by succinylation. Two isomers of lactate dehyrogenase (LDH) were used, namely the slightly positive (+2) LDH-M4 and the strongly negative (-19) LDH-H4. These isomers, which occur naturally, did not require further purification. The Stokes-Einstein radii, as measured by gel chromatography, of inulin, myoglobin, HRP and LDH were 11, 17.5, 32 and 46 A, respectively. The chemical modifications did not alter the Stokes-Einstein radii. In biological studies on rat kidneys samples of both plasma and renal hilar lymph were found to contain radioactive low molecular weight degradation products in addition to the intact proteins. This necessitated separation of all individual samples on small Sephadex columns prior to analysis.
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PMID:Permeability of renal capillaries. I. Preparation of neutral and charged protein probes. 357 14

The permselectivity of the renal capillaries was investigated from the transport of a series of molecular probes: inulin, positive (+2, net charge at pH 7.4), neutral (0), and negative (-6) myoglobin, neutral (0) and negative (-14) horseradish peroxidase (HRP) and two isomers of lactate dehydrogenase (LDH), namely the positively charged (+2) LDH-M4 and the negatively charged (-19) LDH-H4. The determination of the concentration of tracer proteins necessitated gel separation of both plasma and renal hilar lymph. The reason for this is that the proteins, after filtration, will be reabsorbed and degraded by the proximal tubular cells into small molecular compounds (amino acids), which will return to both the renal interstitium and systemic plasma. Even if this degradation is of low degree, as for high-molecular-weight proteins, separation is still required, since the relative lymph concentration (plasma concentration put at 1) is also low, that is, even small amounts of low molecular compounds will distort the relative lymph concentration obtained. The transport from plasma to renal hilar lymph of the tracer molecules fell with increasing Stokes-Einstein radius. The relative lymph concentration of the 11 A inulin was 1.06 +/- 0.03 (mean +/- SEM), of the neutral 17.5 A myoglobin 0.76 +/- 0.05, of the neutral 32 A HRP 0.32 +/- 0.02 and of the neutral 46 A LDH 0.12 +/- 0.01. The data are compatible with a two-pore system. The negative tracer molecules were in general proportionally more restricted than the neutral (or positive) moieties (P less than 0.001) thus suggesting a negatively charged peritubular capillary membrane.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Permeability of renal capillaries. II. Transport of neutral and charged protein molecular probes. 357 15

Myoglobin is an intracardiac protein that is released into the blood after myocardial injury and is then cleared rapidly by the kidneys. This study was undertaken to determine whether successful reperfusion of damaged myocardium could be assessed by examination of blood myoglobin concentration-time patterns. After release of a 2 hr occlusion of the mid left anterior descending coronary artery in 11 dogs that had been instrumented over the long term, immunoreactive arterial plasma concentration of myoglobin, [Mb], rose rapidly to a peak within 25 +/- 2(SEM) min (range 20 to 40). Individual peaks were three to 165 times the myoglobin levels immediately before release of the occlusion. Myoglobin was cleared rapidly from plasma, falling to one-half its peak level 38 +/- 3 min after the peak. Similarly well-defined peaks in [Mb] were evident in plasma from the great cardiac vein (GCV), with a mean time to peak of 16 +/- 2 min and a magnitude of two to 177 times prerelease values. In contrast, arterial and GCV creatine kinase activity-time curves showed less defined peaks and they occurred later and with more variability (60 to 330 min after reperfusion). In nine patients with acute infarction, successful coronary artery reopening was also accompanied by a sharp four- to sixteenfold rise in plasma [Mb] within 1 to 2 hr. Elevations in plasma creatine kinase were slower and more prolonged, peaking at 2 to 18 hr.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Patterns of myoglobin release after reperfusion of injured myocardium. 401 15

Serum myoglobin levels were measured longitudinally in patients undergoing therapy because of various thyroid disorders. Elevated myoglobin values - 72.6 (58.7-89.7) micrograms/l (mean +/- SEM) were found in group of hypothyroid subjects. The degree of myoglobin increase seemed related to the severity of hypothyroidism. When rendered euthyroid the myoglobin levels of these patients were normalized - 41.0 (37.3-45.1) micrograms/l. In patients with hyperthyroidism, due to Graves' disease or subacute thyroiditis (de Quervain), only minor changes of myoglobin values within the reference range of health subjects, were measured. This suggests that mechanisms not affecting myoglobin release are responsible for the muscular weakness of thyrotoxic patients.
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PMID:Serum myoglobin in thyroid disease. 689 84

1. The non-invasive method of near-infrared spectroscopy was used to measure myocardial oxygenation and haemodynamics in response to left anterior descending coronary artery occlusion in a porcine model. 2. Near-infrared spectroscopy measures changes in haemoglobin (and myoglobin) oxygenation and blood volume to yield information on tissue perfusion and flow. It also measures the redox state of cytochrome aa3, thus providing information about intracellular oxygen utilization. 3. Left anterior descending coronary artery occlusion was induced to produce periods of ischaemia lasting between 24s and 13.5 min (n = 13). The changes in deoxyhaemoglobin, oxyhaemoglobin and cytochrome aa3 measured during occlusion were all highly significant compared with baseline variation. In all occlusions (n = 13) a rapid decrease in oxyhaemoglobin concentration (-75.83 +/- 3.27 mumol/l, mean +/- SEM) with a simultaneous increase in deoxyhaemoglobin of 9.27 +/- 1.69 mumol/l was measured. The total haemoglobin concentration also fell by -71.3 +/- 5.32 mumol/l. Cytochrome aa3 was also reduced during occlusion (-8.35 +/- 1.044) mumol/l. 4. Over the range 24-60s occlusion, the magnitude of the fall in total haemoglobin and oxyhaemoglobin correlated with the duration of occlusion (P < 0.003 and 0.013 respectively). For total haemoglobin only the magnitude of the fall correlated with the increase upon release of occlusion (r = 0.89, P < 0.003). 5. Release of occlusion (n = 8) resulted in an immediate increase in the concentration of deoxyhaemoglobin at 9.88 +/- 1.06s, then total haemoglobin at 13.62 +/- 1.23s and finally oxyhaemoglobin at 29.75 +/- 5.96s. The difference between the timing of the maxima after reperfusion is significant (P < 0.002 and P < 0.007 respectively). Moreover, the time for the deoxyhaemoglobin signal to reach maximum values was found to correlate with the duration of occlusion (P < 0.04). This could be indicative of the PO2 of the ischaemic tissues and an immediate off-loading of oxygen from oxyhaemoglobin. The results are reliable, reproducible and sensitive enough to detect the kinetics of haemoglobin oxygenation from a beating heart in situ.
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PMID:Non-invasive measurement of cardiac oxygenation and haemodynamics during transient episodes of coronary artery occlusion and reperfusion in the pig. 877 60

Despite advances in therapy acute myocardial infarction is associated with a mortality rate of up to 30%. Early and complete reperfusion of the infarct related artery (defined as TIMI flow 3 at 90 minutes following therapy) as obtained with thrombolytic therapy in 50 to 80% of patients improves survival and enhances ventricular function. Failure to achieve recanalization should prompt further intervention (second attempt of thrombolysis or rescue-PTCA). Various cardiac markers known from diagnosing acute myocardial infarction or risk stratification in unstable angina pectoris have been assessed in their ability to predict successful reperfusion/failure of therapy. Following reperfusion creatinkinase (CK) and its isoform CK-MB, troponin and myoglobin show an early and rapid rise to a high maximum value with rapid normalization. For creatinkinase time to peak values of less than 9 hours or rates of increase of > 50 U/h (> or = 10 U/h for CK-MB activity) within the first 2.5 hours following thrombolysis have been suggested as useful indicators of successful reperfusion. The same applies for a troponin (T)slope > 0.5 ng/ml/h within the first hour (Table 5). The major limitation in applying either creatinkinase, troponin or even lactatdehydrogenase (LDH) is their comparatively late release (4 to 6 hours) following myocardial infarction. In that respect myoglobin (though not specific for cardiac injury) seems ideal for guidance of intervention after failed thrombolysis. The I.S.A.M. study included 1,741 patients with acute myocardial infarction of less than 6 hours duration being given either streptokinase or placebo. Serial blood samples for measurement of cardiac enzymes were drawn within the first 50 hours. In the streptokinase group the time to peak concentration of CK-MB activity was significantly lower (mean 10.9 hours vs 16.1 hours following initiation of treatment) as was the area under the CK-MB curve indicating reduction of infarct size (Table 2). A substudy investigating the myoglobin release in 120 patients having received streptokinase or placebo demonstrated higher maximum values in the streptokinase group (mean 3008 vs 2097 ng/ml), a shorter time to peak interval following treatment (3.4 vs 6.5 hours) and a reduction in infarct size as suggested by a smaller area under the myoglobin curve (17,377 vs 23,240 ng/ml x h) (Table 3). For LDH/alpha-HBDH the reduction in time to peak intervals was less impressive (Table 4). In angiographic studies with TIMI flow 3 at 90 minutes in the infarct related artery in 22 patients (Figure 5) the maximum myoglobin value was reached in less than 4.2 hours (mean value plus SEM) following treatment (9.5 hours for CK-MB activity). Therefore, myoglobin seems to be the preferred marker in reperfusion assessment.
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PMID:[Enzymatic markers of reperfusion in acute myocardial infarct. With data from the ISAM study]. 1054 47


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