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At least 19 recordsLinked to original sources
PubMed2026

Effects of Sacubitril Valsartan Combined With Vericiguat on NT-proBNP and CK-MB Levels in Patients With Chronic Heart Failure.

This study aims to probe the influence of sacubitril valsartan sodium tablets combined with vericiguat on N-terminal pro-B-type natriuretic peptide (NT-proBNP) and creatine kinase isoenzyme (CK-MB) levels in patients with chronic heart failure (CHF). One hundred and twenty CHF patients were enrolled and stratified into a control group (sacubitril valsartan sodium tablets) and a combination group (sacubitril valsartan sodium tablets + vericiguat). Outcome measures included New York Heart Association (NYHA) functional class shifts, echocardiographic indices, cardiac injury markers, 6-min walk distance (6MWD), endothelial function parameters, inflammatory mediator levels, and adverse clinical events. Following a 6-month treatment period, patients in the combination group exhibited superior functional improvement, as reflected by greater advancement in NYHA class. Echocardiographic evaluation revealed more favorable ventricular remodeling in this group, with reduced left ventricular end-diastolic and end-systolic diameters and an elevated ejection fraction. The combination group had a higher 6MWD. Biomarker analysis showed lower NT-proBNP and CK-MB levels in the combination group. Furthermore, improvements in endothelial function were noted, with decreased endothelin and elevated NO, NOS, and CGRP levels in the combination group. Markers of systemic inflammation, including CRP and IL-6, were also attenuated in the combination group. The incidence of adverse reactions and cardiovascular events did not differ significantly between the groups. Co-administration of sacubitril/valsartan and vericiguat enhances cardiac performance, optimizes vascular endothelial responsiveness, modulates heart failure-related biomarkers, and mitigates inflammatory activity in patients with CHF without increasing the risk of adverse events.

Humans↗
PubMed1976

Radioimmunoassay for creatine kinase isoenzymes.

Creatine kinase has three isoenzymes designated MM, MB, and BB, with BB being the grain form and MM the muscle form. Antibodies to BB creatine kinase were obtained by immunization of rabbits with human BB creatine kinase. The antibodies demonstrated specificity for BB and MB creatine kinase (myocardial isoenzyme) but no cross-reactivity with MM creatine kinase. With the use of this antibody, a highly sensitive radioimmunoassay capable of measuring picomolar amounts of MB creatine kinase has been developed. Clinical application of this method should provide a sensitive and specific test for the diagnosis of myocardial infarction.

Brain↗
PubMed1977

Activity of creatine kinase isoenzyme MB in serum and red cell acetylcholinesterase variants in patients with Duchenne muscular dystrophy.

Activity of creatine kinase isoenzyme MB in serum and variants of red cell acetylcholinesterase were determined in patients with Duchenne muscular dystrophy, in other forms of Dystrophy and in family members of Duchenne patients and healthy controls. Creatine kinase isoenzyme MB was observed only in all cases of DMD as well as variants of red cell acetylcholinesterase characterized by so-called inhibitor numbers. Carriers of Duchenne muscular dystrophy can be distinguished from Duchenne patients and healthy controls by estimation of Acetylcholinesterase variants.

Acetylcholinesterase↗
PubMed1977

Brain isoenzyme of creatine kinase. I. Purification of rabbit enzyme and production of specific antibodies.

Creatine kinase (EC 2.7.3.2) of rabbit brain (BB) was purified to hemogeneity as judged by sedimentation velocity analysis in the ultracentrifuge. Nevertheless, the purified enzyme contained as many as seven extraneous protein species when examined by disc electrophoresis in polyacrylamide gel. The purified preparation also showed antigenic heterogeneity when it reacted in agar gel double immunodiffusion analysis with antibodies produced against it in the rooster. At least some of the extraneous proteins appeared to arise from BB during storage. Subsequently BB was purified to hemogeneity by disc electrophoresis in polyacrylamide gel. It was excised from the gel and injected repeatedly with Freund's complete adjuvant into roosters. A single immunoprecipitin line was noted in agar gel double immunodiffusion analysis when partially pure enzyme reacted with the antibodies raised to the electrophoretically pure protein. These antibodies inhibited the enzymatic activity of BB in both soluble and insoluble immune complexes. They did not, however, form immunoprecipitates with or inhibit rabbit muscle (MM) or rabbit hybrid (MB) creatine kinases. The antibodies were therefore specific for BB and did not react with MM or MB.

Animals↗
PubMed1976

Biochemical differences between the MB and MM isoenzymes of creatine kinase.

The biochemical properties of partially purified preparations of human myocardial MB and MM iosenzymes of creatine kinase have been compared with one another. Differences in substrate affinity, behaviour with inhibitors, and heat denaturation have been demonstrated. It is doubtful if the differences we have shown are sufficiently great to form the basis of a practical routine procedure for measuring serum levels of the MB isoenzyme.

Adenosine Triphosphate↗
PubMed1979

Serum creatine kinase BB linked to immunoglobulin G.

We describe an atypical form of creatine kinase in the serum of a woman after myocardial infarction. Electrophoresis on agarose gel showed a single fraction between CK-MM and CK-MB isoenzymes. After ion-exchange chromatography on DEAE-Sephadex A-50 we isolated the atypical CK and CK-BB as detected by electrophoresis of the eluted fractions. Results of our immunological investigations and exclusion chromatography clearly demonstrate that the atypical CK consists of complexes with high molecular masses formed by CK-BB isoenzyme and immunoglobulin G. The clinical significance, if any, of this Macro CK has yet to be determined.

Brain↗
PubMed1990

Mass concentration and activity concentration of creatine kinase isoenzyme MB compared in serum after acute myocardial infarction.

We compared three current methods (immunoinhibition, "Isomune-CK" immunoprecipitation, and the Tandem-E CKMB II immunoenzymometric assay) for determination of creatine kinase (CK; EC 2.7.3.2) isoenzyme MB in serum. Although results inter-correlated well, the immunoinhibition assay gave higher activity values. Atypical CK forms did not interfere with the immunoprecipitation and immunoenzymometric methods. In acute myocardial infarction the catalytic properties of CK decreased with the enzyme's age, as reflected by a steady increase in activation energy of the catalyzed reaction. In septicemia patients with very low CK and CK-MB catalytic activity, mean CK-MB mass concentration exceeded the upper reference limit, suggesting an increased rate of loss of activity concentration in these patients' sera. Because of the assay's lesser susceptibility to conformational changes at the active site of the enzyme, we suggest that measurement of CK-MB mass concentration is better suited for infarct sizing than measurement of catalytic activity.

Acute Disease↗
PubMed1978

Post-synthetic changes in creatine kinase isozymes (EC 2.7.3.2).

1. An in vivo change from creatine kinase MM3 into MM2 and finally into MM1 was described earlier in sera of patients during a post-myocardial infarction period. The same change takes place in vitro. 2. Parallel to this change, a turn-over from the MB2 isozyme into the MB1 form can be detected in vitro. 3. Immediately after the mixing of various extracts from heart tissue and other muscles with a serum with low creatine kinase activity, only MM3 and MB2 can be detected. MM1, MM2 and MB1 are not present in muscle cells. From these three observations it can be concluded that the phenomenon of the three MM and two MB isozymes is postsynthetic (i.e. epigenetic). Furthermore evidence is presented that the change from MM3 into MM1 is brought about by a thermolabile substance. This factor transforms one of the two M2 chains, present in the MM3 form, into a M1 chain. This results in the MM2 isozyme. Later on the second M2 chain is also transformed, resulting in the MM1 isozyme. The same mechanism is proposed for the observed change in MB pattern.

Creatine Kinase↗
PubMed1992

Apparent elevation of serum CK-MB not due to acute myocardial infarction.

An increased serum level of the MB isoenzyme of creatine kinase (CK-MB) is a useful marker for acute myocardial infarction. Although described extensively in clinical chemistry literature, there is little information in standard medical references about false positives for this test. We report two cases where high levels of measured CK-MB activity were in fact due to another form of CK, associated with internal malignancy.

Aged↗
PubMed1979

Creatine kinase forms in human skeletal and cardiac muscle.

The creatine kinase (CK) activity in human skeletal and cardiac muscle submitted to QAE-Sephadex chromatography was found to distribute into three peaks (m and h I, II, III fractions). Characterization according to electrophoretic behaviour, approximate molecular weight, thermal stability and immunological properties unambiguously demonstrated the coincidence of fractions I and III with reference MM-CK and MB-CK isoenzymes, while both cardiac and muscular forms II proved to escape any assignment within the dimeric (M, B) model. A higher molecular weight than for reference CK and the absence of interaction with BB-antiserum resulted for both forms II, which on the contrary were found to diverge as for reactivity to MM-antiserum and stability characteristics. Quantitation of the CK forms, attempted on a limited number of samples, confirmed the expected relative levels of MM-CK and BB-CK and gave evidence for the presence of hII- or mII-CK amounting up to 30% of the total activity in cardiac and skeletal muscle, respectively. The results of the study both confirm a complexity greater than supposed for the CK system and point to the inadequacy of several of the commonly used analytical approaches to derive correct information.

Chromatography, Ion Exchange↗
PubMed1976

Sarcolemmal membrane changes related to enzyme release in the imipramine/serotonin experimental animal model.

We report specific findings in the imipramine/serotonin animal model that are consistent with sarcolemmal membrane alterations. Among these findings are cytoplasmic enzyme release, diminished uptake of alpha-aminoisobutyrate (an amino acid analog), decreased oxygen consumption in isolated rat diaphragm, and ribosuria. Furthermore, we describe for the first time the release of the MB isoenzyme of creatine kinase from a source other than cardiac tissue; that is, isolated diaphragms from imipramine/serotonin-treated animals release increased amounts of MB isoenzyme as compared to diaphragms from control animals. We believe the similarities between this animal model and the human disease (Duchenne muscular dystrophy) support a genetically determined generalized membrane abnormality in the pathogenesis of this form of muscular dystrophy.

Adenosine Triphosphatases↗
PubMed1990

Non-M CK--a practical measure of creatine kinase isoenzymes in cancer patients.

The individual creatinine kinase (CK) isoenzymes CK-BB and CK-Macro II have previously been investigated as potential tumour markers. We believe there is a need for a system to measure those CK forms not usually present in serum. We have studied a CK-MB immunoinhibition kit which measures all residual CK activity following inactivation of M-subunit activity. In 162 patients with cancer we found no difference in grading (+ or -) between detailed isoenzyme studies and the simple non-M assay. In 33 samples with elevated non-M CK, detailed analysis showed BB alone (45%), Macro II alone (9%), or both (36%). Raised activities were mainly found in patients with small cell lung cancer (SCLC) (17/40; 43%) and GI Tumours (6/11; 55%). In patients with SCLC, elevated activities were associated with disseminated disease. Preliminary evidence indicates that Non-M CK may also be a simple means of monitoring initial treatment response.

Biomarkers, Tumor↗
PubMed1978

An investigation into creatine kinase and other plasma enzymes in thyroid disorders.

The relationship between plasma protein bound iodine (PBI) level and creatine kinase (CK) activity was investigated in 143 males and 528 females suspected of various thyroid disorders; there was significant negative correlation between low PBI level and raised CK activity. CK, aldolase, lactate dehydrogenase (LD), aspartate transaminase (AST), and alanine transaminase (ALT) activities were determined in plasma from patients with reduced PBI levels; apart from CK, LD was the only enzyme increased in an appreciable number of cases. A further series of specimens was collected from 66 patients with low PBI levels and the CK isoenzymes investigated. In all of these MM was the main form present; a trace of MB was found in 6. These findings do not explain the elevation of CK in hypothyroidism which may be a non-specific effect.

Adolescent↗
PubMed1991

Identification of creatine kinase isoenzymes in the guinea-pig. Presence of mitochondrial creatine kinase in smooth muscle.

Isoenzymes of creatine kinase (CK, EC 2.7.3.2) in guinea-pig smooth, cardiac and skeletal muscles as well as in brain were analyzed by cellulose acetate electrophoresis and FPLC gel permeation chromatography. In crude tissue extracts of smooth muscles brain type BB-CK and the hybrid form MB-CK were detected, but in enriched mitochondrial fractions from different guinea-pig smooth muscles, mitochondrial type Mi-CK was unambiguously identified. Smooth muscle Mi-CK displayed the same electrophoretic mobility as Mi-CK from brain, which migrates slower than cardiac Mi-CK. Identical to parallel experiments with Mi-CK from cardiac muscle and brain, smooth muscle Mi-CK could be resolved into dimeric and octameric species, the latter being remarkably stable. In contrast to guinea-pig smooth muscles, Mi-CK was not detected in chicken gizzard tissue extracts nor in enriched mitochondrial fractions thereof. The presence of Mi-CK, predominantly in octameric form, in guinea-pig smooth muscles, but not in chicken gizzard, may represent a clue for the different physiological properties of these muscles and may provide the molecular basis for the dependence of the PCr production on oxidative metabolism observed in the guinea-pig taenia caeci.

Animals↗
PubMed1979

Further observations on the incidence and nature of atypical creatine kinase activity.

The interference of atypical creatine kinase (CK; EC 2.7.3.2) with anion-exchange methods for the measurement of the CK-MB isoenzyme is now firmly established. False-positive results from this source are much more common than interferences caused by the BB isoenzyme. Atypical CK, at least in some patients, does not appear to be a genetic variant, nor could we relate it to a specific clinical diagnosis, to hypoxia, or to administration of a particular drug. Its behavior in an immuno-inhibition test for CK-B subunit indicates an immunological difference from the normal M subunit. Thus the change in immunological properties is associated with the altered electrophoretic properties. The variability of electrophoretic patterns suggests that atypical CK may represent multiple forms of creatine kinase rather than a unique entity.

Aged↗
PubMed1977

Subcellular compartmentation of creatine kinase isoenzymes in guinea pig heart.

In an attempt to determine whether a subcellular compartmentation of creatine kinase exists and if so, whether there is a different distribution of the 3 isoenzymes of CK in the cell, studies were carried out with the guinea pig heart which had been subfractionated by either isopycnic density gradient centrifugation or differential pelleting. Isoenzyme analysis of CK in the isolated subcellular fractions by electrophoresis on agarose gels, revealed that the MM isoenzyme occurred in the cytosol, myofibrils, and the microsomes while the MB isoenzyme (which is cardio-specific) was only found in the cytosol. Trace amounts of the BB isoenzyme were detected in the cytosol. Considerable CK activity was associated with the mitochondria, this did not represent the MM, the MB, or the BB isoenzymes but was a distinct and additional mitochondrial-specific form of CK. PH optima and kinetic studies were carried out to characterise and distinguish the mitochondrial isoenzyme from other CK isoenzyme activity. The evidence for a differential compartmentation of MM, MB, BB, and mitochondrial CK is discussed in relation to their possible cellular roles.

Animals↗
PubMed1990

S-100ao protein in serum during acute myocardial infarction.

Concentrations in serum of S100ao protein (alpha alpha form of S-100 protein, which is present at high concentrations in heart muscle) were successively measured by enzyme immunoassay in 21 patients with acute myocardial infarction (AMI) and six with angina pectoris (ANP). Results were compared with measurements of creatine kinase isoenzyme MB (CK-MB) concentrations in the same specimens. Mean S100ao concentrations in sera from 100 healthy adults were 0.12 (SD 0.08) microgram/L. In patients with AMI, S100ao concentrations were 4.74 +/- 5.27 micrograms/L at admission, peaked 8 h after admission (23.5 +/- 27.7 micrograms/L), then decreased gradually. Among nine AMI patients who were admitted within an hour after their attack, eight showed abnormally high concentrations of S100ao in serum (greater than 0.5 microgram/L), whereas only four showed abnormally high CK-MB concentrations (greater than 5 micrograms/L) in sera at the time of admission. Serum S100ao concentrations remained within the normal range in all six patients with ANP; however, serum CK-MB concentrations were increased in two of them. Therefore, serum S100ao is useful not only for detection of AMI but also for differentiating AMI from ANP.

Acute Disease↗