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Results for “Creatine Kinase, MM Form”

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PubMed2003

Acute hepatitis E with elevated creatine phosphokinase.

Acute hepatitis E is caused by infection with hepatitis E virus, which is endemic in developing countries. Recently, the number of cases with acute hepatitis E is increasing in Japan due to increased travel to the endemic areas. This paper reports a case of a Japanese man with acute hepatitis E who had a history of traveling to south China. Serum creatine phosphokinase was elevated on admission without symptoms of muscle damage (isoenzyme MM 100%), and normalized in parallel with resolution of hepatitis, raising the possibility of an association between elevation of creatine phosphokinase and acute hepatitis E. However, we need to investigate further the incidence of elevation of serum creatine phosphokinase in many cases with acute viral hepatitis including hepatitis A, B, and C to determine whether muscle disorder is characteristic of acute hepatitis E.

Creatine Kinase↗

PubMed2001

Creatine kinase gene mutation in a patient with muscle creatine kinase deficiency.

BACKGROUND: We describe a 56-year-old woman admitted to the hospital with a diagnosis of acute myocardial infarction without an increase of serum creatine kinase (CK) activity during her clinical course. She died on the 11th hospital day, and the diagnosis was confirmed by autopsy. The patient had had no previous muscular symptoms. METHODS: Expression of the CK-muscle (CK-M) protein in cardiac tissue was examined by immunoblotting and immunochemical staining. CK-M mRNA expression was estimated by semiquantitative reverse transcription-PCR. Gene structure of CK-M was determined by Southern blotting and direct sequencing of 2251 bp. Existence of a point mutation in the CK-M gene was examined by restriction fragment length polymorphism analysis of PCR products (PCR-RFLP) in the patient and in 108 controls. RESULTS: CK-M protein in the myocardial tissue of the patient was substantially lower (103 +/- 7 ng/mg protein) than in control myocardial tissue (35 800 +/- 2860 ng/mg protein). Immunoreactive CK-M in the patient tissue sample was 0.3% of the value for the control sample. CK-M mRNA was 53-fold less in the patient sample compared with the control. This very low expression of CK-M mRNA was considered to be the primary reason for CK-M deficiency. Direct sequencing revealed a point mutation at residue 54 in exon 2, which was specific for the patient. No other abnormalities were found in the CK-M gene of the patient. CONCLUSIONS: This report identifies a molecular abnormality in human CK deficiency and discusses the physiologic relevance of CK-M.

Blotting, Southern↗

PubMedDate not supplied

Serum creatine kinase is not a reliable indicator of ectopic pregnancy.

OBJECTIVE: It has been reported that elevation in creatine kinase may be used as an indicator of ectopic pregnancy as a consequence of trophoblast invasion of the smooth muscle layer of the Fallopian tube. In this study, we attempt to verify this observation and establish the sensitivity and positive predictive value of the test. METHODS: Serum creatine kinase (MM-fraction) was obtained from patients presenting with possible ectopic pregnancy prior to surgical intervention. Ectopic pregnancies were confirmed by laparoscopy. Noted was whether the gestation was ruptured or unruptured, its location in the tube, and estimated cross-sectional tubal distention. Controls consisted of patients with first-trimester pregnancies simulating ectopic pregnancy, i.e., patients having a positive pregnancy test, complicated by vaginal bleeding and/or abdominal pain. RESULTS: The distribution of creatine kinase values for both patients with ectopics versus control are positively skewed, with a mode of 10-19 U/L. The mean creatine kinase for ectopic pregnancies was 62.3 U/L, S.D. = 63.1 U/L. For controls, the mean creatine kinase = 40.8 U/L, S.D. = 30.1 U/L. The difference in these means is significant (p = 0.04), but weakly so. In addition, for ectopic gestations there was no significant difference in creatine kinase values with regard to degree of tubal distention, gestation location, or whether rupture had occurred, thereby limiting the clinical value of this test. CONCLUSIONS: Although the mean value of serum creatine kinase is statistically significantly higher in ectopic pregnancy relative to controls, the distribution curve for creatine kinase values for ectopics is broad, with much overlap with the control curve. Hence, the sensitivity and positive predictive value for this test is poor.

Biomarkers↗

PubMedDate not supplied

[Rhabdomyolysis].

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Acute Kidney Injury↗

PubMed2004

Hybrid retroviral vector with MCK enhancers inserted in LTR for stable and specific expression of human factor IX in skeletal muscle.

BACKGROUND: Retroviral vectors have been widely used to introduce foreign into various target cells in vitro, thus showing relatively high systemic delivery efficiency of various transgene products. The authors investigated the stability and efficiency of skeletal muscle-specific hybrid retroviral vectors in expression of human factor IX (FIX) in vitro and iv vivo. METHODS: FIX cDNA in LIXSN vector was replaced with a FIX minigene containing splicing donor and splicing acceptor sequence of first intron of human FIX gene. Two copies of muscle creatine kinase enhancer (MCK, Me2) were inserted in forward or reverse orientation at NheI site of 3' long terminal repeat (LTR), resulting in two hybrid vectors, which were designated as LMe2IXm2SN(F) and LMe2IXm2SN(R), respectively. The vectors were tested in vitro and in vivo for stability and muscle-specificity of factor IX expression with SCID mice. RESULTS: Muscle cells carrying vector with Me2 expressed significantly higher levels of FIX (up to 1800 ng/106.24 h) than those without Me2, thus suggesting that Me2 could specifically increase expression level of FIX in muscle cells. Myoblasts transduced with LMe2IXm2SN(R) produced much less FIX in vivo in SCID mice than LMe2IXm2SN(F). One or two copies of Me2 sequence were deleted in myoblasts transduced with LMe2IXm2SN(R) without changing the orientation of Me2. CONCLUSIONS: LTR inserted with MCK enhancers can specifically increase human FIX expression in skeletal muscle cells in vitro and in vivo, and MCK enhancer should be positioned in the same orientation as that of LTR promoter.

Animals↗

PubMed2005

[An A/G polymorphism in muscle-specific creatine kinase gene in Han population in Northern China].

To explore the distribution about genotype and allele frequencies of Nco I polymorphism in the CKMM gene in Han population in Northern China, and investigate what the genotypes were, PCR-RFLP was used to examine the genotype and allele frequencies of 306 unrelated healthy persons. Sequencing was used to analyze all three genotypes. Chi2 test was used to compare the frequencies between Chinese Han population and foreign population. The Nco I polymorphism was A/G. The allele frequencies were as follows: A=86%,G=14% . The genotype frequencies were A/A=74%, A/G=24%, G/G=2% and they were in Hardy-Weinberg equilibrium. The site of Nco I in the CKMM from Chinese Han population had polymorphism. No significant difference was detected in genotype and allele frequencies between men and women. There were significant differences between Chinese Han population and those in Europe and America, but no significant difference was detected between Chinese population and Korean population.

Adolescent↗

PubMedDate not supplied

[Evolutionary comparison of laboratory cardiac and infectious parameters during septic shock: about an original case].

A massive release of troponin Ic and CKMB was described in a patient during septic shock. According to experimental animal models previously described, this release of biological markers by myocardial tissue could be due to an inflammatory process of myocardial tissue during septic shock without myocardial infarction in non cardiac critically ill patients.

Aged↗

PubMed2005

Long-term MRI and clinical follow-up of symptomatic and presymptomatic carriers of dysferlin gene mutations.

We report the results of a longitudinal study involving MRI and clinical follow-up in nine siblings from four families with Miyoshi myopathy (MM). All individuals carried pathogenic dysferlin gene (DYSF) mutations with six of them suffering from symptomatic disease and three being presymptomatic. In presymptomatic subjects, MRI was sensitive to detect alterations in muscle tissue years before disease onset. The first MRI alteration to disclose was evidence for myoedema in dorsal compartment muscles of the legs followed by fatty degeneration. Moreover, MRI changes anticipated the topography of subsequent clinical muscle involvement and progressed from distal to proximal dorsal leg muscles. In symptomatic subjects, MRI changes reflected the pattern and severity of clinical muscle involvement. MRI evidence, however, suggests that muscle involvement is much more prominent in early disease stages than clinically seen. Clinical follow-up up to 8 years made evident that MM onset occurs at a mean age of 18.4 years. The most prominent initial deficit was impaired tiptoe gait due to muscle plantarflexor dysfunction followed by impaired dorsiflexor function. Dorsal compartments were predominantly affected not only in distal but also in proximal leg muscles, and a more rapid progression was noticed during the early phase of the disease. Our data suggest that MRI is a helpful diagnostic tool for an early diagnosis of MM and other distal myopathies since it provides sensitive and topographic information about initial and even preclinical muscle involvement. This is of particular relevance in Miyoshi myopathy because distinct CK elevation is present long before its clinical onset and often misdiagnosed as "idiopathic".

Adolescent↗

PubMed2007

Muscle creatine kinase/SV40 hybrid promoter for muscle-targeted long-term transgene expression.

Gene therapy for congenital protein deficiencies requires lifelong expression of a deficient protein. Current gene therapy approaches preferentially employ the strong cytomegalovirus (CMV) promoter/enhancer or its derivative CAG promoter; however, these promoters provide only temporary transgene expression. To create a promoter that enables long-lasting expression in muscle, hybrid promoters were constructed by coupling the muscle creatine kinase (MCK) enhancer to various strong promoters for enhancement of tissue specificity and improved transcriptional activity. A hybrid promoter containing the MCK enhancer and the simian virus 40 promoter (MCK/SV40 promoter) yielded long-term (>6 months) expression of a human secretory alkaline phosphatase (huSEAP) reporter gene following electrotransfer of the plasmid into mice, whereas expression using a conventional CMV or CAG promoter faded away within a few weeks. To explore the mechanism behind the sustained expression obtained with the MCK/SV40 promoter, mice were immunized with a LacZ expression plasmid driven by MCK/SV40 or a conventional promoter. Minimal cellular and humoral responses to LacZ were observed in MCK/SV40 promoter-treated animals, and mouse SEAP gene expression in vivo was successfully maintained by both the MCK/SV40 and conventional promoters. These results suggest that the lower immunogenicity of the MCK/SV40 promoter contributed to long-lasting gene expression in mice. Therefore, the MCK/SV40 promoter may provide the basis for development of an effective transgene expression cassette for treatment of congenital protein deficiencies in which therapeutic proteins are recognized as foreign by the host immune system.

Animals↗

PubMed1985

The nature of post-translational formation of MM creatine kinase isoforms.

Isoforms (derived from the same isoenzyme but distinguished by differences in isoelectric point) of MM creatine kinase appear in plasma after myocardial infarction. They are formed by conversion of the tissue form of creatine kinase (MM-A, pI 7.80) to progressively more acidic species (MM-B, pI 7.50) and MM-C (pI 7.20) after release into the circulation. To define the changes responsible for myocardial MM creatine kinase isoform formation in humans and dogs, purified isoforms were treated with trypsin or cyanogen bromide. The digests were fractionated by reverse-phase high pressure liquid chromatography. Comparison of proteolytic maps showed that MM-A and MM-C were each characterized by a single, unique peptide peak. Maps of MM-B creatine kinase contained both of these peaks. Sequence analysis and comparison with the complete amino acid sequence of MM creatine kinase showed that the peptide unique to MM-A corresponded to the COOH-terminal tryptic or CNBr peptide. The peptide unique to MM-C was shown to have the same amino acid composition except for lysine (the COOH-terminal amino acid). Thus, isoform formation is characterized by the successive removal of the COOH-terminal lysine residue from one M subunit at a time resulting in the conversion of MM-A to isoforms MM-B and MM-C.

Amino Acid Sequence↗

PubMed1986

Highly sensitive enzyme immunoassay for human creatine kinase MM and MB isozymes.

A sensitive enzyme immunoassay system for measurement of MM and MB forms of human creatine kinase (CK) was developed using purified monospecific antibodies to the M subunit and to the B subunit of CK. The CK-MM assay system consisted of polystyrene balls with immobilized F(ab')2 fragments of anti-M and the same antibody Fab' fragments labeled with beta-D-galactosidase from Escherichia coli. The CK-MB was assayed with the polystyrene balls with either antibody (anti-M or anti-B) F(ab')2 fragments and the other antibody (anti-B and anti-M, respectively) Fab' fragments labeled with galactosidase. The assays were highly sensitive and 3 pg of CK-MM and CK-MB were measurable. The CK-MM assay was specific to the M subunit of creatine kinase, and it cross-reacted about 15% with CK-MB, but not with CK-BB. The CK-MB assay did not cross-react with CK-MM nor CK-BB. Therefore, concentrations of CK-MM could be estimated by subtracting the cross-reacting values of CK-MB. Coefficients of variation in within-run and between-run precision studies for serum CK-MM and CK-MB were less than 9%. Serum levels in healthy adults of various ages (16-59 yr old) were ranged from 35.2-132 ng/ml for CK-MM and from 0.40-1.77 ng/ml for CK-MB. There was apparently no statistical significance among the sex- and age-related differences. Concentrations of CK-MM and CK-MB in various human tissues were also determined. The CK-MM was present abundantly in the heart and the tissues composed of striated muscles (skeletal muscle, diaphragm and proximal esophagus). The CK-MB was distributed not only in the heart but also in the striated muscle tissues at a relatively high level.

Adolescent↗

PubMed2002

Complexities in ETS-domain transcription factor function and regulation: lessons from the TCF (ternary complex factor) subfamily. The Colworth Medal Lecture.

The ETS-domain transcription factor family can be divided into a series of subfamilies. Elk-1 represents the founding member of the ternary complex factor (TCF) subfamily. By focusing on the TCF subfamily, we can demonstrate the complexities that exist in the function and regulation of ETS-domain transcription factors. This article focuses on Elk-1 in detail and summarizes the functions of other TCFs. The key themes covered include the domain structure of the TCFs, the mechanisms of complex formation with serum response factor, regulation of TCFs by mitogen-activated protein kinase cascades, and transcriptional regulatory properties of the TCFs. Finally, the emerging role of the TCFs in vivo is discussed. A picture is developing indicating that, while these proteins exhibit significant sequence and functional conservation, key differences in their structure and regulation are being identified which may relate to unique functions of these proteins in vivo.

Amino Acid Sequence↗

PubMed1989

[Octameric mitochondrial and dimeric cytoplasmic creatine kinase. The number of subunits, participating in catalysis].

It was found that in the octameric form of mitochondrial creatine kinase (Mr = 340 kD), only 52% of active centers bind Mg-ADP into a E-Mg-ADP-creatine complex with the dissociation constant, K(Cr)ADP, of 0.105 mM, which is close to the Km value for the enzyme (0.072 mM). In the dimeric form of cytoplasmic creatine kinase (Mr = 82 kD), 100% of active centers bind Mg--ADP; the K(Cr)ADP value (0.11 mM) is close to the Km value for the given enzyme preparation (0.083 mM). All active centers of rabbit muscle cytoplasmic creatine kinase were shown to form an analog of the transition state complex (ATSC) - E-Mg-ADP-NO3- -creatine. The constant for Mg-ADP dissociation from ATSC is identical for all centers of cytoplasmic creatine kinase and equals to 6.0 microM. The curves for ATSC saturation with Mg-ADP in the presence of iodacetamide for mitochondrial creatine kinase were constructed and computer analyzed. It was shown that in the octameric form of the enzyme only 54 +/- 13% of subunits can form ATSC. The constant for Mg-ADP dissociation from ATSC, KATSCADP is equal to 1.9 +/- 0.8 microM. It was concluded that 50% of subunits of the octameric form of mitochondrial creatine kinase are not involved in the catalytic act due to masking of their active centres and their inability to form transition state complexes. A model of regulation of cell supply with high energy compounds, e.g., ATP, creatine phosphate, via association-dissociation of mitochondrial creatine kinase oligomers is proposed.

Adenosine Diphosphate↗

PubMed1983

Novel staining pattern of skeletal muscle M-lines upon incubation with antibodies against MM-creatine kinase.

Incubation of chicken skeletal muscle fibers with an excess of anti-M-creatine kinase (CK) immunoglobulin G and an excess of anti-M-CK Fab fragments leads to heavy decoration of the M-line (Wallimann, T., D.C. Turner, and H.M. Eppenberger, 1977, J. Cell Biol. 75:297-317) and to removal of the electron-dense M-line structure (Walliman, T., G. W. Pelloni, D.C. Turner, and H.M. Eppenberger, 1978, Proc. Natl. Acad. Sci. USA., 75:4296-4300), respectively. On the other hand, incubation with low concentrations of monovalent anti-M-CK Fab did not extract but rather decorated the M-line, giving rise to a distinct two-line staining pattern. A similar double-line staining pattern, although less pronounced, was also observed within the M-line of paraformaldehyde-prefixed myogenic cells, which after permeabilization were incubated with low concentrations of divalent anti-M-CK antibody. In both cases, the two decorated lines appearing in the middle of the A-band were spaced axially 42-44 nm apart and correspond most likely to the two M4 and M4' m-bridge rows described by Sjöström and Squire (1977, J. Mol. Biol., 109:49-68; 1977, J. Microscopy., 111:239-278). It is concluded that the muscle-specific form of creatine kinase, MM-CK, contributes mainly to the electron density of these M4 and M4' m-bridges within the M-line structure. This specific labeling pattern is a further demonstration that CK is an integral part of the M-line.

Animals↗

PubMed1989

[The change of creatine kinase bb isozyme in patients undergoing mitral value replacement--comparison with creatine kinase MB and MM isozymes].

By using highly sensitive enzyme immunoassay method recently developed, concentrations of the three forms of cytoplasmic creatine kinases (CK-BB, CK-MB and CK-MM) were determined in blood plasma samples serially taken from 18 patients, who received mitral valve replacement. Plasma CK-BB levels, that were 0.64 +/- 0.32 ng/ml at the beginning of anesthesia, increased sharply after reperfusion reaching peak levels (23.3 +/- 7.56 ng/ml) at 2 hours after reperfusion, and then decreased rapidly. The response of CK-BB in plasma was more rapid and sensitive than that of CK-BB or CK-MM. The CK-BB concentrations were significantly higher in coronary sinus samples than in arterial samples. These results suggest that the major portion of elevated plasma CK-BB levels at early phase after reperfusion were considered to be derived from the heart muscle.

Creatine Kinase↗

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↗

PubMed1989

Creatine kinase BB isozyme in the blood during open heart surgery--comparison with creatine kinase MB and MM isozymes.

By using a recently developed highly sensitive enzyme immunoassay method, concentrations of the 3 forms of cytoplasmic creatine kinases (CK-BB, CK-MB and CK-MM) were determined in blood samples serially taken from 18 patients who received mitral valve replacement. Blood CK-BB levels, 0.64 +/- 0.32 ng/ml at the beginning of anesthesia, rose sharply after reperfusion reaching the peak level (23.3 +/- 7.56 ng/ml) 2 hours after reperfusion, and then fell rapidly. The response of CK-BB in blood was rapider and more sensitive than that of CK-MB or CK-MM. The CK-BB concentrations were significantly higher in coronary sinus samples than in arterial samples. These results suggest that the major portion of elevated blood CK-BB level in the early phase after reperfusion are derived from the heart muscle.

Cardiopulmonary Bypass↗

PubMed1977

Measurement of creatine kinase Z in human sera using a DEAE-cellulose mini-column method.

A DEAE-cellulose mini-column method has been developed which allows for the quantitation in human serum of creatine kinase Z, a sub-band of creatine kinase first described by Lim ((1975) Clin. Chem. 21, 975, Abstract 181) and Sax et al. (Sax, S.M., Moore, J.J., Giegel, J.L. and Welsh, M. (1976) Clin. Chem. 22, 87). We have shown that creatine kinase Z is rather unstable in nature, and converts to a form which electrophoreses with creatine kinase MM on agarose gel electrophoresis. CK-Z is not present in normal human serum. CK-Z is present in human heart extracts, in patients with myocardial infarcts and in patients with skeletal muscle trauma. In infarct patients CK-Z levels paralleled changes in the CK-MB levels. CK-Z ranged in activity from 8.8-67.2 I.U. whereas CK-MB ranged from 29.6-121.6 I.U. in infarct patients. CK-Z and CK-MB activity were measured at or close to the peak rise in total CK activity.

Brain↗