Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.7.11.1 (protein kinase)
 81,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The total activity and range of the creatine kinase (CK) isozymes have been studied in the homogenate and subcellular fractions (nuclei, mitochondria, cytoplasm) of the rat brain and heart during postnatal ontogenesis. The total activity of CK in the brain and heart of newborn rats was found to be 4 and 2 times less, resp., than in those of adults. The age patterns were established in the activity of cytoplasmic (CK-1, CK-2 and CK-3) and mitochondrial (CK-4) isozymes. During the whole postnatal development the rat brain contains only one cytoplasmic isozyme, CK-1. In the heart of newborn rats, as compared with adults, the content of CK-1 and CK-2 is much higher and that of CK-3 lower. On the 12-15th day of life the range of the CK isozymes approaches that characteristic of adult animals. The activity of CK-4 was found in the brain on the 5-7th day of life and in the heart on 12-15th day. In the range of the CK isozymes in the adult brain the content of mitochondrial CK amounts to 19.3% and in the heart to 16.5%. The data obtained complement the literary ones suggesting the low level of energy-forming processes in the brain and heart cells at the early stages of the rat postnatal development.
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PMID:[Intracellular distribution of creatine kinase isoenzymes in the brains and hearts of rats at different stages of postnatal development]. 121 11

Male Sprague-Dawley rats administered with an acute sublethal dose of carbofuran (1.5 mg/kg, s.c.) developed the signs of peak hypercholinergic activity during 30-60 min. At this time, in hemidiaphragm muscle, a significant decrease in ATP (28%) and phosphocreatine (PC) (29%) occurred without concurrent change in AMP and creatine (CR). A significant decrease in the levels of total adenine nucleotides (ATP + ADP + AMP) (20%) and total creatine compounds (PC + CR) (17%) was evident. The decline in the corresponding ratios of ATP/ADP (26%), ATP/AMP (39%), and PC/CR (20%) was therefore suggestive of greater utilization of ATP and PC in response to their increased demand for high-frequency muscle fasciculations. The energy charge = ATP + 1/2 ADP/(ATP + ADP + AMP), an index of high-energy phosphate adequacy in hemidiaphragm, remained unchanged. A significant (p less than 0.01) increase in serum magnesium with no concurrent change in calcium was also evident. The observed higher activity (152%) of total CK (EC 2.7.3.2) in the serum induced by carbofuran was possibly a reflection of more than a twofold increase in CK-BB isoenzyme (CK-1) and 141% increase in CK-MM isoenzyme (CK-3), which also strengthens our findings of enhanced synthesis of ATP and PC. Increased levels of CK-MM isoenzyme in the brain (253%) and hemidiaphragm (195%); and depletion of CK-BB isoenzyme in the hemidiaphragm (0%), heart (42%), and brain (77%), and of CK-MB isoenzyme (CK-2) in the brain (4%) and hemidiaphragm (14%), appeared to be the major contributory factors leading to enhanced serum CK activity.
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PMID:Carbofuran-induced alterations (in vivo) in high-energy phosphates, creatine kinase (CK) and CK isoenzymes. 195 49

Changes in the proportions of individual isoforms of creatine kinase (CK) in serum promptly reflect both myocardial infarction and coronary reperfusion. A new commercial kit has been introduced for measuring CK-3(1) isoform in serum (ISOFOR-MM, International Immunoassay Labs.). This is an immunochemical assay containing CK-3(1) specific monoclonal antibody, bound to magnetizable particles, used to immunoextract this isoform. The CK activity of the sample is measured before and after immunoextraction and the difference in the two values gives the measure of CK-3(1). Extraction of CK-3(1) was complete at less than or equal to 1200 U/L. Analysis of between-day imprecision gave CV between 2.9-7.9%. The method was not susceptible to interference by CK-3(2) and CK-3(3) isoforms, CK-2 isoenzyme, or mitochondrial CK. Reference interval for CK-3(1) (expressed as percent of total CK-3) was 42-69%. Correlation between percent CK-3(1) by isoform electrophoresis (x) and evaluated procedure (y) was y = 0.83x + 7.6, with r = 0.957 (n = 40). The ISOFOR-MM performed well enough in this evaluation to replace electrophoresis or isoelectric focusing for measurement of CK-3(1) isoform.
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PMID:An immunochemical procedure for determination of creatine kinase 3(1) (serum-specific) isoform in human serum evaluated. 237 36

The CK-2 and CK-3 isoenzymes of human serum creatine kinase (CK) can be further subdivided into five isoforms (subforms derived from the same isoenzyme). Three are derived from CK-3 and two from CK-2. The formation of these isoforms is a postsynthetic phenomenon brought about by a serum carboxypeptidase that acts on the M monomer of the enzyme. Sera from healthy subjects contain CK-3(1) as the dominant isoform with lesser amounts of CK-3(2) and CK-3(3). Following damage of muscle tissue, the serum isoform distribution changes as a result of the increased release of CK enzyme. This provides more diagnostic information concerning acute myocardial infarction and other muscle diseases than is available from routine CK isoenzyme analysis.
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PMID:Serum isoforms of creatine kinase isoenzymes. 304 46

Kinetics of the catalytic activities of creatine kinase (CK;EC 2.7.3.2) for three CK-3 and two CK-2 isoforms in serum were studied in 20 patients with myocardial infarction randomly assigned to receive either intracoronary urokinase (group A) or conventional therapy (group B). The temporal characteristics of isoform changes described were (a) time at which the isoform activities are significantly greater than initial values, (b) maximal rate (Ka) at which isoforms are released into blood, (c) time lag from onset of pain until maximum activity value, (d) peak value of each serum isoform, and (e) rate (Kd) at which each isoform is cleared from serum. Thrombolytic treatment induced earlier peak times in group A: for CK-3(3), 7.4 vs 20.0 h; for CK-3(2), 11.6 vs 24.8; for CK-3(1), 18.6 vs 34.3; for CK-2(2), 9.1 vs 17.8; and for CK-2(1), 11.8 vs 26.8 (numbers given are medians; for all isoforms, P less than 0.05). Ka values were at least twofold greater and the first increase was significantly earlier in the urokinase group. Consequently, the ratio for CK-3(3) to CK-3(1) activities peaked significantly earlier in group A. Isoform peak activities and Kd were not significantly different between the two groups.
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PMID:Isoforms of creatine kinase isoenzymes in serum in acute myocardial infarction after intracoronary thrombolysis. 367 76

We compared the clinical sensitivity, specificity, and diagnostic efficiency of measuring creatine kinase-3 (MM) isoenzyme sub-types (CK, EC 2.7.3.2) with the measurement of CK-2 (MB) isoenzymes for the diagnosis of acute myocardial infarction. Serial blood collections at 3-h intervals from 35 patients with acute myocardial infarction were examined. In attempts to reperfuse their coronary arteries, some of these patients were treated with pharmacological thrombolysis (streptokinase, tissue plasminogen activator), with or without coronary angioplasty. The infarction patients were divided into two groups: patients who were successfully treated with thrombolytic agents (i.e., they achieved coronary reperfusion), and patients who were treated unsuccessfully or who were not treated acutely. We also examined blood from 34 non-infarction patients. We measured CK-3 sub-types by both anion-exchange liquid chromatography and a modified high-voltage electrophoresis method, and CK-2 by immunoprecipitation. Our results show that during the first few critical 3 to 9 h after onset of chest pain, measurement of CK-3 sub-types has the highest diagnostic efficiency; in contrast, CK-2 has the highest efficiency during the 10- to 21-h time intervals. Thus early diagnosis of acute myocardial infarction can be based on rapid assays of CK-3 sub-types.
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PMID:Early diagnosis of acute myocardial infarction by rapid analysis of creatine kinase isoenzyme-3 (CK-MM) sub-types. 381 99

Isoenzymes and isoforms of creatine kinase (CK, EC 2.7.3.2) were measured to assess reperfusion after acute myocardial infarction (AMI). In streptokinase-treated and in spontaneously reperfused AMI patients, total CK, CK-2 activity and concentration, and CK-3(3) isoform activity peaked significantly (p less than 0.05) earlier than conventionally treated, non-reperfused patients. The ratio for CK-3(3) to CK-3(1) activities peaked significantly (p less than 0.05) earlier in both the streptokinase-treated and spontaneously reperfused groups, and indicated a greater release of enzyme (higher ratio) than in the conventionally treated patients. The ratio of CK-3(3)/3(1) also peaked significantly (p less than 0.05) earlier in all three groups than did total CK, CK-2, and CK-3(3) activities or concentrations. The clearance rates of total CK, CK-2, and CK-3(3) were not significantly different in all three groups. Thus, the ratio CK-3(3)/3(1) was the earliest indicator of infarction in both reperfused and non-reperfused patients.
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PMID:Analyses of creatine kinase isoenzymes and isoforms in serum to detect reperfusion after acute myocardial infarction. 382 81

The thermal stability at 37 degrees C of several clinically relevant enzymes and isoenzymes was assessed by measuring changes in enzyme activity as a function of time under incubation and reaction conditions. Selwyn plots were used in the reaction-condition assessments. Except for CK-1 (BB), all the enzymes investigated are stable enough at 37 degrees C to permit assay. These enzymes were LDH-1, LDH-5, s-AspAT, m-AspAT, apo-s-AspAT, apo-m-AspAT, ALP-liver, ALP-bone, ALP-intestine, ALT, apo-ALT, CK-2, and CK-3. CK-1 is stable at 37 degrees C under assay conditions but not under incubation conditions. We specifically avoided using Arrhenius plots to evaluate thermal stability and point out pitfalls inherent in their indiscriminate use.
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PMID:Evaluation of the thermal stability of clinically relevant enzymes at 37 degrees C. 647 18

We report the effect of serum pH and of the presence or absence of mercaptoethanol, N-acetyl-L-cysteine, monothioglycerol, ethylenediaminetetraacetate, and ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetate on the activation of the human creatine kinase isoenzymes. At the serum pH giving maximal enzyme stability and minimal assay lag phase (Nealon et al., Clin. Chem. 26: 1165-1169, 1980) thiol activation of CK-1 and CK-3 is nearly maximal with monothioglycerol in an optimized creatine kinase assay (Szasz et al., Clin. Chem. 22: 650-656, 1976). However, CK-2 is maximally activated at pH 8.5, a pH at which this isoenzyme is least stable on storage and its assay lag phase is prolonged. These findings suggest irreconcilable problems in the storage, activation, and assay of CK-2.
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PMID:Activation of human creatine kinase isoenzymes by pH and various sulfhydryl and chelating agents. 678 91

Serum creatine kinase (CK) and lactic dehydrogenase (LD) isoenzyme activities were measured in blood serum of pigs having myocardial damage and skeletal muscular lesions. Myocardial and muscular damage was induced by restraint stress provoked by intravenous infusion of a pharmacological restraint (succinylcholine-chloride) during 12 minutes. Pigs of Swedish Landrace and Swedish Landrace X Yorkshire breed, stress-susceptible (halothane-sensitive) and nonreacting pigs were studied. Severe myocardial damage and slight to moderate skeletal muscle necrosis were found 24 hours after restraint stress in the stress-susceptible pigs whereas in nonreacting pigs generally only myocardial lesions of moderate extent were registered. No significant increase was detected in the serum CK-BB (CK-1) or CK-MB (CK-2) activity whereas a pronounced elevation of the CK-MM (CK-3) activity was found, particularly in the stress-sensitive animals. In the myocardial tissue of pigs only a low CK-MD activity was found (about 4-5% CK-MD in addition to CK-MM) and this may explain the low CK-MB activity in serum of pigs subjected to severe myocardial damage. This is further supported by the pronounced increase in the anodal serum fractions LD 1-2 in animals free from skeletal muscular lesions. In the halothane-sensitive pigs skeletal muscle necrosis besides the myocardial lesions contributed to the high levels of CK-MM activity in serum.
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PMID:Creatine kinase isoenzymes in serum of pigs having myocardial and skeletal muscle necrosis. 688 87


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