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PubMed1994

Compartmentation of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in neurons: evidence for a creatine phosphate energy shuttle in adult rat brain.

Multiple isoforms of creatine kinase (CK) are expressed in specific cell types as part of an energy delivery or shuttle system. To test the hypothesis that neurons utilize a creatine phosphate energy shuttle, we examined the pattern of CK isoform expression and localization in adult rat brain. Two isoforms of CK are present in brain extracts, "brain-type," or BCK, and the ubiquitous form of the mitochondrial CK (uMtCK), as detected by enzyme activity following nondenaturing electrophoresis and by Western blotting following denaturing electrophoresis. In formalin-fixed and paraffin-embedded sections of rat brain, uMtCK immunostaining is detected in the somata of all Golgi type I neurons in the cerebellum, pontine reticular formation, red nucleus, hippocampus, and cerebral cortex. Immunostaining for uMtCK appears throughout the cell body but not in nuclei. BCK immunostaining is also present in somata of Golgi type I neurons in the cerebellum, red nucleus, and pons and is distributed throughout the cell body and within nuclei. BCK immunostaining also appears in neuronal processes and is concentrated in the molecular layers of the cerebellum and the hippocampus and in cortical pyramidal cell dendrites. These results demonstrate a coordinate pattern of expression and compartmentation of BCK and uMtCK isoforms in neurons, which provides an anatomic basis for the transfer of metabolic energy via a creatine phosphate energy shuttle.

Animals↗
PubMed1990

Clinical application of subforms of creatine kinase MM and macro creatine kinases.

The subforms of MM isozyme of creatine kinase (ATP:creatine N-phosphotransferase, EC 2.7.3.2, CK) in sera obtained from healthy adults and patients were determined by agarose gel isoelectric focusing (IEF). The patients were classified into six groups according to serum CK-MM activities and IEF patterns. The IEF spectra offered useful information on cell hyperplasia, augmented cell membrane permeability, cell destruction and release time of CK-MM in the circulation from the cells for diagnosis, progress observation and prognosis, especially in the cases of chronic hepatic diseases, acute myocardial infarction and muscular dystrophy. Macro CKs were also determined by IEF. Macro CKs could be completely distinguished from each other, and CK isozymes consisting of macro CK type 1 could be presumed by isoelectric points.

Chromatography, Gel↗
PubMed1994

Hybridization of matrix-bound MM-creatine kinase with BB-creatine kinase and arginine kinase.

Dimeric rabbit muscle creatine kinase (MM-CK) was bound to CNBr-activated Sepharose 4B by one of its subunits (MM-CKA). Treatment of MM-CKA with guanidine hydrochloride released the unbound subunit to yield the matrix-bound monomer (M-CKB). M-CKB recombined with dissociated MM-CK soluble subunits to reconstitute a matrix-bound dimer (MM-CKC). M-CKB also associated with dissociated subunits of BB-CK from crude extracts of rabbit brain and of arginine kinase from sea cucumber muscle (MM-AK) to form the matrix-bound heterohybrids MB-CKC and M-CK/M-AKC, respectively. Guanidine hydrochloride gradient elution studies showed that MM-CKA, MM-CKC and MB-CKC were all dissociated at the same concentration of the denaturant (0.96 M), while the M-CK/M-AKC heterohybrid was less stable, dissociating at 0.5 M. The specific interaction between subunits of echinoderm and mammalian phosphagen kinases to form a hybrid enzyme of dual substrate specificity supports the view that these enzymes had a common evolutionary origin.

Animals↗
PubMed1997

Immunochemical extraction and automated measurement of plasma creatine kinase MB isoenzyme and creatine kinase MB2 isoform.

Measurement of creatine kinase MB (CK-MB) and its isoforms CK-MB2 and CK-MB1 are now applied in the diagnosis of acute myocardial infarction (AMI). The most common approach for analysis includes RIA, IRMA, and electrophoresis, all of which may be time-consuming. This study examines determination of CK-MB and CK-MB2 by a rapid immunochemical extraction method followed by an automated measurement for both analytes. The automated method was sensitive to 2 U/L, linear to 180 U/L, and gave excellent interassay precision (< 10% CV). Interference studies indicated that bilirubin, hemolysis, and lipemia caused analytical problems as did the presence of high activities of other CK isoenzymes, notably CK-MM and CK-BB, requiring dilution of samples prior to analysis. Application of immunochemical extraction gave a reference interval of CK-MB (0-2.5 U/L) and CK-MB2 (0.1-1.4 U/L) for blood donors (20-60 years), peak levels for ruled-out AMI patients of CK-MB (0.5-7.3 U/L) and CK-MB2 (0.3-4.9), peak levels for ruled-in AMI patients of CK-MB (80-174 U/L) and CK-MB2 (80-155 U/L). Coronary artery bypass patients (n = 24) and all trauma patients (n = 14) also demonstrated elevations in CK-MB and CK-MB2, whereas only five of the trauma patients demonstrated increased CK-MB by IRMA. In patients (n = 7) having increased total CK and normal CK-MB by IRMA, the extraction assay for CK-MB and CK-MB2 yielded increased values in all patients. This new approach to CK-MB and CK-MB2 analysis can be performed within 30 minutes of sample receipt.

Adult↗
PubMed1994

Creatine kinase isoenzymes in chicken cerebellum: specific localization of brain-type creatine kinase in Bergmann glial cells and muscle-type creatine kinase in Purkinje neurons.

Creatine kinase isoenzymes were localized in the chicken cerebellum by the use of isoenzyme-specific anti-chicken creatine kinase antibodies. Brain-type creatine kinase was found in high amounts in the molecular layer, particularly in Bergmann glial cells but also in other cells of the cerebellar cortex, e.g. in astrocytes and in the glomerular structures, as well as in cells of the deeper nuclei. A mitochondrial creatine kinase isoform was primarily localized to the glomerular structures in the granule cell layer and was also identified in Purkinje neurons. Surprisingly, a small amount of the muscle-type creatine kinase isoform was identified in cerebellar extracts by immunoprecipitation, immunoblotting and native enzyme electrophoresis, and was shown to be localized exclusively in Purkinje neurons. Cell type-specific expression of brain- and muscle-type creatine kinase in Bergmann glial cells and Purkinje neurons, respectively, may serve to adapt cellular ATP regeneration to the different energy requirements in these specialized cell types. The presence of brain-type creatine kinase in Bergmann glial cells and astrocytes is discussed within the context of the energy requirements for ion homeostasis (K+ resorption), as well as for metabolite and neurotransmitter trafficking. In addition, the presence of muscle-type creatine kinase in Purkinje neurons, which also express other muscle-specific proteins, is discussed with respect to the unique calcium metabolism of these neurons and their role in cerebellar motor learning.

Animals↗
PubMed1997

Troponin T, creatine kinase MB mass, and creatine kinase MB isoform ratio in the detection of myocardial damage during non-surgical coronary revascularization.

The presence of myocardial injury during non-surgical coronary revascularization has been evaluated by means of highly specific and sensitive biochemical markers. Troponin T, creatine kinase-MB isoenzyme mass concentration, and creatine kinase MB2/MB1 isoform ratio have been determined in 80 patients who underwent coronary revascularization with percutaneous transluminal coronary angioplasty (PTCA). Forty-five patients underwent balloon angioplasty, 15 rotational atherectomy, 10 directional atherectomy, and 10 elective coronary stenting. Serum concentration of the evaluated markers did not increase significantly after 57 uncomplicated revascularization procedures, including 15 rotablation procedures, nor after 8 PTCAs complicated by localized coronary type B and C dissections. Significant elevation of all markers above the upper limits of the reference interval (P < 0.05) was detected after occlusion of small side branches (< 0.5 mm diameter) in 5 patients. Creatine kinase MB2/MB1 isoform ratio was the earliest marker to increase. After recanalization of occluded vessels in 8/10 patients with 6-60 days old myocardial infarction only troponin T concentrations increased from a baseline of 0.28 microgram/l to a median peak of 0.80 microgram/l. This increase was statistically not significant (P = 0.12). In conclusion, myocardial damage was not detected following uncomplicated non-surgical revascularization obtained with different techniques. Markers of myocardial injury provide high sensitivity after small side branch occlusion.

Aged↗
PubMed1978

[Creatine kinase isoenzymes: idiopathic occurrence of creatine kinase BB activities in patient serum (author's transl)].

By differentiation of creatine kinase isoenzyme activities in sera using immunological methods the published data about occurrence of creatine kinase BB activities in patients with different diseases or after surgical treatment, respectively, cannot be verified in general. With a frequency in the order of magnitude of 1 : 1000 in the serum of old patients (age 57 to 85 years with one exception), however, creatine kinase BB activities can be measured. The range of activities is 15 to 234 U/1, or 19 to 94% of total creatine kinase activities, respectively. At the present time there is no possibility to correlate this phenomenon to any specific disease. These cases are detected by abnormally high results of CK-MB activity measurements with the immunoinhibition test (range 60 to 202% of total creatine kinase activities) which lead to a repeated analysis using immunoprecipitation. The results of all CK-BB patients investigated till now are presented and discussed.

Adult↗
PubMed1980

Metastable creatine kinase MM and complexes of creatine kinase BB and immunoglobulin G, "atypical" isoenzymes with similar electrophoretic mobility.

Metastable creatine kinase MM isoenzyme was isolated and partially purified from homogenates of myocardium and skeletal muscle by gradient elution on carboxymethyl cellulose. This variant isoenzyme migrated between the MM and MB isoenzymes on agarose electrophoresis, accounted for 3.5% of the total creatine kinase activity in each tissue, was not a macromolecule, and had stable electrophoretic mobility only in borate buffer (0.02 mol/L). By comparison, the creatine kinase isoenzymes with similar "atypical" electrophoretic mobility in serum specimens were complexes of the BB isoenzyme and immunoglobulin G. These complexes were measured by a radioimmunoassay specific for the creatine kinase B-subunit and eluted predominantly with the MB isoenzyme in a commercial anion-exchange reagent system.

Creatine Kinase↗
PubMed1993

Diagnostic evaluation of creatine kinase-2 mass and creatine kinase-3 and -2 isoform ratios in early diagnosis of acute myocardial infarction.

The diagnostic efficacy of creatine kinase (CK) isoforms (CK-3 and CK-2) was compared with measurement of CK-2 mass concentrations for the early diagnosis of myocardial infarction (MI). Serial serum samples drawn from 76 patients with confirmed MI and 55 non-MI patients were used for determining CK-2 mass concentrations and the MM3/MM1 (CK-3 isoforms) and MB2/MB1 (CK-2 isoforms) ratios. We compared the diagnostic utility of each by receiver-operating-characteristic (ROC) curve and likelihood ratio analyses. Our results indicate that all three tests were ineffective within the first 4 h after the onset of chest pain. All three were most effective at 4-18 h after onset, but both CK-3 and CK-2 isoform ratios were less effective than CK-2 mass concentrations in the next 6-h period (18-24 h). In the critical time between 3 and 6 h, the diagnostic performance of all three was comparable.

Adult↗
PubMed1983

Changes in serum myoglobin, total creatine kinase, lactate dehydrogenase and creatine kinase MB levels in runners.

A comparison was made between pre- and post-run serum levels of total creatine kinase (CK), CK-MB isoenzyme, lactate dehydrogenase (LD) and myoglobin (MG) levels in 84 runners in each of three groups; male 5-10 mile run; female 5-10 mile run; and male 15-55 mile run. Levels of CK-MB and MG were quantified using radioimmunoassay, while total CK and LD were measured using spectrophotometric procedures. Post-run levels of all four markers were significantly higher than the pre-run levels (p less than 0.001). Although levels of enzymes and MG correlated with the sex and distance run, the post-run changes did not correlate with age nor with the smoking status of the runners. Elevation of these markers as a result of vigorous exercise in the absence of myocardial infarction requires cautious interpretation of serum enzyme changes in runners.

Adult↗
PubMed1995

Expression of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in the fetal rat brain: evidence for a nuclear energy shuttle.

To test the hypothesis that embryonic brain cells utilize a creatine phosphate energy shuttle, we examined the pattern of creatine kinase (CK) isoform expression and localization in the fetal rat brain. Moderate levels of CK activity are present at embryonic day 14 (7 U/mg protein) and decrease slightly until 3 days postpartum followed by a rapid, fourfold up-regulation to adult levels by 1 month (18 U/mg protein). In parallel with changes in enzyme activity, there is a biphasic and coordinate pattern of expression of brain-type CK (BCK) and ubiquitous mitochondrial CK (uMtCK) determined by nondenaturing electrophoresis and immunoblot analysis. The localization of CK isoforms was examined by immunocytochemistry, and, during the fetal period, BCK and uMtCK immunoreactivity was detected throughout the central and peripheral nervous system, especially in neuroepithelial regions of the cerebral vesicles and spinal cord. In large cells within the olfactory neuroepithelium and ventral spinal cord, differential compartmentation of CK isoforms was evident, with BCK localized primarily in cell nuclei, whereas uMtCK immunoreactivity was present in the cell body (but not within nuclei). In olfactory bulb neuroepithelium, both isoforms were expressed in the middle zone of the germinal layer associated with DNA synthesis. In embryonic skeletal and cardiac muscle, which also express BCK, the same compartmentation of BCK was seen, with BCK localized primarily in the cell nucleus of cardiac and skeletal myoblasts. These results demonstrate a coordinate pattern of expression and compartmentation of BCK and uMtCK isoforms in the fetal brain that, in some cells, provides the anatomic basis for a nuclear energy shuttle.

Animals↗