Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.1.1.27 (lactate dehydrogenase)
29,211 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum samples from patients admitted to a coronary care unit with a history of acute chest pain suggestive of myocardial infarction in the previous 12 h were obtained on admission and at 6 and 12 h, thereafter. Creatine kinase (CK), CK-MB isoenzyme, CK-MM sub-bands, myoglobin, and lactate dehydrogenase (LD) isoenzymes were examined. Changes were evaluated in relation to the diagnosis obtained from clinical examination, serial electrocardiography and 'routine' cardiac enzymes (CK, aspartate transaminase and alpha-hydroxy butyrate dehydrogenase daily for 3 days following admission). The slope of the logarithms of CK, CK-MB activity and CK-MB concentration in the early post infarct period fully distinguished between infarct and non-infarct patients. Measurement of myoglobin and lactate dehydrogenase isoenzymes was less sensitive. Serial estimation of CK-MM sub-band patterns allowed the time from infarction to be estimated. Serial estimation of CK in the 12 h following admission can be substituted for conventional daily enzyme estimations for the diagnosis of acute myocardial infarction in patients with onset of chest pain within the previous 12 h. This could reduce laboratory and in-patient costs.
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PMID:Early diagnosis of myocardial infarction by timed sequential enzyme measurements. 321 18

Oxygen-derived free radicals and intracellular calcium overload have been implicated as mediators of myocardial ischemia/reperfusion injury. We hypothesized that free radical scavengers or calcium channel blockers could enhance the protection afforded the isolated, working rat heart by crystalloid cardioplegia against this type of injury at 37 degrees C. Hearts from 42 male rats in seven groups (n = 6) were studied in an isolated, working heart preparation measuring aortic flow (ml/min/gm dry wt), peak systolic pressure (mm Hg), coronary artery flow (ml/min/gm dry wt), and calculated coronary vascular resistance (dyne.sec.cm-5/gm dry wt). Creatine kinase and lactate dehydrogenase release were measured before ischemia and at various times during the postischemic reperfusion period. Time-matched control hearts (group 1) were perfused for 2 hours. After finding that 30 minutes of ischemia and 10 minutes of reperfusion (group 2) produced significant (p less than 0.01) functional impairment that was completely protected (group 3) by a preischemic bolus of St. Thomas' Hospital cardioplegic solution, we again found significant (p less than 0.01) functional impairment after 40 minutes of ischemia and 10 minutes (group 4) or 20 minutes (group 5) of reperfusion despite a preischemic bolus of St. Thomas' Hospital cardioplegic solution. Diltiazem (10 mg/L) plus St. Thomas' Hospital cardioplegic solution (group 6) did not significantly (p less than 0.01) enhance functional recovery. Addition of superoxide dismutase plus catalase (200 microns/ml) (group 7) produced marked improvement in functional recovery that did not differ significantly (p less than 0.01) from control results (group 1). The creatine kinase and lactate dehydrogenase data strongly supported the preceding functional data. Coronary flow and vascular resistance were not significantly (p less than 0.01) changed from control values in any group. We conclude that the addition of superoxide dismutase and catalase but not diltiazem to St. Thomas' Hospital cardioplegic solution can significantly enhance myocardial protection against normothermic ischemia/reperfusion injury. This implicates oxygen-derived free radicals as mediators of this type of injury.
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PMID:Enhancement of crystalloid cardioplegic protection against global normothermic ischemia by superoxide dismutase plus catalase but not diltiazem in the isolated, working rat heart. 336 28

Creatine kinase (CK) and lactate dehydrogenase (LD) enzyme activities and isoenzymes were determined for synovial fluid, synovial membrane, and articular cartilage from 24 clinically normal equine tarsocrural (tibiotarsal) and femoropatellar joints. All 3 tissues contained LD isoenzymes LD1 to LD5, and CK isoenzymes BB and MM. The CK isoenzyme MB was not found. The similarities in isoenzyme composition of these 3 tissues made differentiation of the source of LD and CK impossible by isoenzyme pattern alone. Reference values for the total enzyme activities of specific joint tissues also had wide variations. The wide variation in activities, as determined by the enzymatic analysis of synovial fluid and a lack of tissue specificity in clinically normal equine joint tissue, indicated that those values were not predictive for the extent and type of tissue damage in equine joint disease. This hypothesis was confirmed when synovial fluids from 22 abnormal joints were analyzed for LD isoenzymes and total enzyme activity. The various causes of the joint problems were not distinguishable.
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PMID:Evaluation of creatine kinase and lactate dehydrogenase activities in clinically normal and abnormal equine joints. 356 3

To determine the adaption of myocardial metabolism in mitral regurgitation and mitral stenosis, human papillary muscles obtained during open heart surgery were analysed to measure selective enzyme activities in energy metabolism. All enzyme activities were expressed per unit dry weight muscle, per unit alkali soluble protein, and per unit total creatine and the different results compared. The activities of enzymes concerned with mitochondrial energy production and energy transfer (namely, citrate synthase and mitochondrial creatine kinase) tended to be higher in papillary muscles from hearts with mitral regurgitation than in those with mitral stenosis. The activities of enzymes concerned with cytoplasmic energy production (creatine kinase MM, lactate dehydrogenase, and phosphofructokinase) did not show statistically significant differences between mitral regurgitation and mitral stenosis. The ratio of creatine kinase MB activity to total creatine content showed the greatest difference when papillary muscles from patients with mitral regurgitation and mitral stenosis were compared (31% higher in mitral regurgitation; p less than 0.001). The specific function of creatine kinase MB, which is located in cytoplasm, is not well defined. Creatine kinase MB activity increases with extreme endurance training of human skeletal muscle. Thus the higher creatine kinase MB activity in papillary muscle of mitral regurgitation may represent an adaptation to increased physical demand.
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PMID:Myocardial enzyme activities in patients with mitral regurgitation or mitral stenosis. 365 86

We undertook a retrospective study of 36 victims of high-voltage electrical contact injuries to determine the incidence and possible source of elevated creatine kinase (CK)-MB enzyme in their serum. Only two sustained myocardial infarctions (one late) according to history, electrocardiographic findings, and clinical course. Serum lactate dehydrogenase isoenzyme levels were abnormal but revealed no myocardial infarction patterns. Creatine kinase total activity, however, reached 1.5 to 1,140 times normal in 92% and the CK-MB level was abnormal in 50% despite the low incidence of myocardial damage. Skeletal muscle CK and CK-MB levels in four nonelectrically injured patients were comparable to those in normal muscle while CK and CK-MB activity was elevated in six such electrical injuries. There was a gradient in CK-MB activity with greatest CK-MB activity in "normal" muscle near the injury site, lesser amounts in border tissue, and least in the worst-injured site. We conclude that myocardial injury is uncommon in high-voltage electrical injury and skeletal muscle injured by high electrical voltage is stimulated to produce, as well as release, CK-MB.
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PMID:Is serum creatine kinase-MB in electrically injured patients predictive of myocardial injury? 394 78

Creatine kinase (CK), brain CK (CKBB), lactate dehydrogenase (LD), and aspartate aminotransferase (ASAT) levels were determined in cerebrospinal fluid (CSF) obtained from 35 patients with acute stroke. In patients with transient, minor neurological disturbances, only LD levels increased; in those who remained comatose and died, the levels of all the enzymes, except ASAT, increased. Patients who remained with focal motor defects had increased CK and LD levels, while CKBB and ASAT levels were variable. In most of the CSF samples, muscle CK activity was also detectable, suggestive of a leakage from blood to CSF. The pattern of the enzyme increase could be related to the causative mechanisms for the strokes. The study suggests that CSF enzyme determinations may provide supplementary information as to the extent and severity of brain damage and the recovery potentials of selected patient groups with strokes.
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PMID:Enzyme level changes in the cerebrospinal fluid of patients with acute stroke. 395 19

Enzyme activities of energy metabolism were determined in both homogenates and single fibers of immature-normal (IN), adult-normal (AN), and adult-dystrophic (AD) tibialis anterior (TA) muscle of BL6 mice. Mitochondrial enzyme activities were similar in AN and AD, whereas lower activities were found in IN. Creatine kinase, glycogenolytic, and glycolytic enzyme activities were reduced but glucose 6-phosphate dehydrogenase was elevated in AD and IN as compared to AN. IN and AD both showed an increase in the H-subunit of lactate dehydrogenase. Microphotometric measurements of succinate dehydrogenase (SDH) revealed large fiber differences in AN whereas smaller scattering was observed both in IN and AD. Although similarities exist between enzyme and isozyme patterns of anaerobic metabolism in AD and IN, this does not hold for mitochondrial enzymes.
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PMID:Enzyme activities and activity profiles in muscle fibers of dystrophic, immature-normal, and adult-normal BL6 mice. 671 87

During a long-term study in the rat some enzyme activities were determined in plasma, lung, spleen and skeletal muscle. Twelve rats of each sex were investigated every 49 days from 35 until 1115 days of life. Lactate dehydrogenase in lung and spleen decreases; in muscle and plasma, however, the activity varies considerably. Malate dehydrogenase in the tissues remains nearly unchanged apart from distinct peaks in the first year of life; in plasma the activity takes an M-shaped course. In contrast to the changes of glutamate dehydrogenase in the tissues with a tendency to diminish, this enzyme increases in plasma during the lifetime. Aspartate aminotransferase activity in the tissues, except muscle, varies with a rhythmical behaviour, and in plasma shows a gradual increase. Alanine aminotransferase in lung and spleen has two activity peaks. In muscle this enzyme varies only slightly after a steep initial decrease. In plasma the activity has a tendency to rise. Creatine kinase in the tissues reveals several activity peaks. In plasma the activity course is U-shaped. Adenylate kinase in spleen and lung rises, whereas in muscle the activity varies considerably. The nearly identical decrease of alkaline phosphatase activity in the tissues during ageing is also reflected by a concomitant behaviour in plasma. Leucine arylamidase in lung and muscle both have a U-shaped characteristic, whereas in spleen the activity changes in a shorter period. In plasma, a rhythmical behaviour is apparent. Aldolase in plasma tripled during the observation period. Except for lactate dehydrogenase and aldolase, distinct sex-differences are observed in plasma. With progressive age the animals suffer increasingly from characteristic diseases, which beside experimental components have influenced the enzyme pattern. Enzyme activities in plasma and tissues show a complex pattern and are only of limited importance in understanding the ageing process.
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PMID:Long-term observation of plasma and tissue enzyme activities in the rat. 720 25

In order to compare the time-course of disappearance of macromolecules and electrolytes from ischaemic myocardium, measurements of creatine kinase and lactate dehydrogenase activity and myoglobin, K+ and Na+ concentration were made on myocardial extracts from dogs which had left anterior descending coronary artery ligation for 3, 6, 12 and 24 h (4 groups of 6 dogs each). Intensity of ischaemia was assessed by myocardial blood flow measured with 15+/- 5 micrometers microspheres at 15 min after ligation. Creatine kinase and lactate dehydrogenase activities and K+/Na+ concentration ratios were at all times correlated with the magnitude of collateral blood flow in the ischaemic myocardium, while myoglobin concentration was correlated with blood flow only at 12 and 24h. Comparisons of the intensity of depletion at the various times after ligation showed that K+, K+/Na+ and creatine kinase had all reached a steady state at 12 h after ligation while lactate dehydrogenase and myoglobin had still to reach a steady state at 24 h. We conclude that these indices are mutually supportive markers of the intensity of ischaemia of 24 h duration, but K+ or K+/Na+ may be the most reliable indices for shorter periods of ischaemia of 3 to 6 h duration.
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PMID:Depletion of myocardial creatine kinase, lactate dehydrogenase, myoglobin and K+ after coronary artery ligation in dogs. 731 13

Creatine kinase (CK) is normally found at high levels in muscle and brain and catalyzes the reaction phosphocreatine (PCr) + MgADP + H+<==>creatine (Cr) + MgATP. CK is not normally found at high levels in liver. A line of transgenic mice that express high levels of the BB-dimer of CK (CKB) in liver has allowed us to assess the role of CKB during periods of low oxygen stress. During 40 min of ischemia of normal perfused livers at 25 degrees C, ATP levels are depleted, and pH decreases to 6.6. pH recovers to a preischemic level after 30 min of reperfusion of normal livers; however, P(i) levels are significantly higher and ATP levels significantly lower than preischemic values. In transgenic liver with an initial PCr-to-ATP ratio of 4.5, ATP levels are maintained until PCr is markedly depleted. pH remains at preischemic levels for 16 min of ischemia of transgenic livers. During this length of ischemia in normal livers, pH has dropped to 6.9. pH, P(i), and ATP levels return to preischemic values within 30 min of reperfusion in transgenic livers containing PCr and CK. During 90 min of hypoxia of normal perfused livers at 37 degrees C, ATP is depleted. After 15 min of hypoxia of normal livers, there is a significant increase in the release of lactate dehydrogenase (LDH). In transgenic livers, ATP is maintained, and no increase in LDH release is observed for up to 90 min, depending on the level of PCr before hypoxia. These results demonstrate the role of CKB in buffering ATP levels and regulating intracellular pH during periods of low oxygen stress.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Phosphocreatine protects transgenic mouse liver expressing creatine kinase from hypoxia and ischemia. 827 16


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