Distribution Of Creatine Kinase Isoenzymes Research Articles

Creatine Kinase Activity in Human Spermatozoa and Seminal Plasma Lacks Predictive Value for Male Fertility in In Vitro Fertilization

Objective: To examine the predictive value of creatine kinase in human spermatozoa and seminal plasma from patients treated in an IVF program. Design: Prospective, blind clinical study. Setting: Male infertility clinic. Patient(s): Seventy-three patients and 32 fathers (age, <45 years). Intervention(s): Determination of creatine kinase activity in seminal plasma, washed spermatozoa, and swim-up purified spermatozoa from patients treated in an IVF program. Main Outcome Measure(s): Creatine kinase activity in seminal plasma, washed spermatozoa, and swim-up purified spermatozoa. Result(s): Creatine kinase activity in washed spermatozoa correlated significantly with normal sperm morphology. No significant correlations were found between creatine kinase activity or creatine kinase isoenzyme ratio in seminal plasma, washed spermatozoa, or swim-up purified spermatozoa and success in the IVF program. The percentage of spermatozoa with normal morphology was significantly lower in patients whose sperm did not fertilize than in patients whose sperm did fertilize oocytes and in the control group of proven fathers. Conclusion(s): Total creatine kinase activity and creatine kinase isoenzyme distribution are not sperm function markers for prediction of male fertility in IVF treatment.

Metabolic and diagnostic significance of creatine kinase isoenzymes

Creatine kinase isoenzyme content is frequently used to assess the state of differentiation of muscle and neural tissue and following release into plasma as diagnostic markers for acute myocardial infarction, skeletal muscle disease, and neurologic injury. The establishment of thrombolytic therapy as the standard of care for acute myocardial infarction and new information on the tissue distribution of creatine kinase isoenzymes has necessitated the development of more rapid assays for the diagnosis of infarction and expanded the potential use of these isoenzymes as markers for other disease states.

Compartmentation of adenine nucleotides and phosphocreatine shuttle in cardiac cells: some new evidence.

The concept of the phosphocreatine shuttle for intracellular energy channelling in muscle cells (1 — 6) assumes compartmentation of adenine nucleotides in mitochondrial and myofibrillar compartments and around membranes. The link between these compartments is considered to be performed by phosphocreatine molecules due to heterogeneous distribution of creatine kinase isoenzymes functioning in mitochondria in direction of creatine phosphorylation and in myofibrils in direction of phosphocreatine dephosphorylation. While different isoenzymes of creatine kinase are well characterized, adenine nucleotide compartmentation still remains to be an unsolved question. In our recent studies described below a competitive enzyme method was used to show the existence of rather closed functional cycles of adenine nucleotides in mitochondria and in myofibrils due to titivation of creatine kinase in those structures. Also, 31P-NMR saturation transfer method was used to show the role of those coupled creatine kinases inside mitochondrial and myofibrillar compartments in the integrated intracellular energy fluxes in isolated perfused rat hearts at different workloads.KeywordsCreatine KinaseOxidative PhosphorylationPyruvate KinaseAdenine NucleotideCreatine Kinase IsoenzymeThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Localization of the B and M polypeptide subunits of creatine kinase in normal and neoplastic human tissues by an immunoperoxidase technic.

Measurements of the BB isoenzyme of creatine kinase in serum may be useful in the diagnosis or monitoring of patients who have some types of cancer, and the distribution of creatine kinase isoenzymes in homogenates of certain sarcomas has been evaluated as an aid in the morphologic diagnosis of these neoplasms. The cellular distribution of the B and M polypeptide subunits of creatine kinase in normal and neoplastic tissues were evaluated by an immunoperoxidase technic to determine whether the BB isoenzyme is present in neoplastic epithelial cells and whether immunoperoxidase stains for these polypeptides are useful in microscopic diagnosis. The results indicated that the B polypeptide is distributed very widely in epithelial cells and that normal and neoplastic ductal epithelia from many tissues contain the BB isoenzyme. Normal and neoplastic acinar epithelia contained varying amounts of the B polypeptide, but usually less than ductal epithelia of the same tissues. Large amounts of the B polypeptide were found in tissue sections from malignant fibrous histiocytomas, and of the M polypeptide in sections from an alveolar rhabdomyosarcoma.

Isoenzymes of creatine kinase in extracts of various parts and regions of the human central nervous system.

The distribution of isoenzymes of creatine kinase (EC 2.7.3.2.) was investigated by agarose gel electrophoresis of extracts of selected parts and regions of the human central nervous system. Besides the major brain isoenzyme BB, we demonstrated the presence of three other creatine kinase isoenzyme forms. The distribution of creatine kinase isoenzymes depending strongly on the region from which the biopsy was taken. We found substantial amounts of the MB isoenzyme in extracts of the dura from the cauda equina of the two adults examined.

Isoenzymes of creatine kinase in extracts of various parts and regions of the human central nervous system.

Abstract The distribution of isoenzymes of creatine kinase (EC 2.7.3.2.) was investigated by agarose gel electrophoresis of extracts of selected parts and regions of the human central nervous system. Besides the major brain isoenzyme BB, we demonstrated the presence of three other creatine kinase isoenzyme forms. The distribution of creatine kinase isoenzymes depending strongly on the region from which the biopsy was taken. We found substantial amounts of the MB isoenzyme in extracts of the dura from the cauda equina of the two adults examined.

Creatine Kinase in the Digestive Tract

While studing the distribution of creatine kinase isoenzymes in the mucosa of the rat digestive tract, we found two predominant patterns, namely the esophagic pattern with predominant MM isoenzyme, and the gastrointestinal pattem with predominant BB isoenzyme. The quantitative distribution of the enzyme was higher in the esophagus, although its role is not clear at present.

Isoenzyme distribution of creatine kinase and lactate dehydrogenase in serum and skeletal muscle in Duchenne muscular dystrophy, collagen disease, and other muscular disorders.

We determined the total activity and isoenzyme distribution of lactate dehydrogenase and creatine kinase in serum and biopsy specimens from skeletal muscle of nine normal individuals and nine patients with Duchenne muscular dystrophy (I), five with collagen disease (II), and four with non-progressive unclassified myopathy (III). Mean total serum creatine kinase in patients with Duchenne muscular dystrophy (867 U/liter, SD = 197) was 31-fold that in the control group (28 U/liter, SD = 14). There was also a small (3.3-fold) increase in the mean total serum creatine kinase of patients with III, but none in the serum from patients with II. Changes in the creatine kinase isoenzyme distribution of skeletal muscle were primarily in the MB isoenzyme. The mean percentage of creatine kinase-MB activity in muscle from patients with I (2.81, SD = 1.15) and patients with III (1.69, SD = 1.07) significantly (P less than 0.005) exceeded that of the control group (0.43, SD = 0.18). Muscle from patients with II showed little change. The most striking changes in lactate dehydrogenase were also observed in patients with I, in whom the mean total serum activity (356 U/liter, SD = 115) was 3.4-fold that of serum from the control group (105 U/liter, SD = 19). Skeletal muscle from these patients also showed a significant decrease in mean percent isoenzyme 5 activity (from 50 to 23) and an increase in that of isoenzymes 1 and 2 (from 1 to 9 and 8 to 20, respectively). These changes in the distribution of these two sets of isoenzymes in muscle were reflected in the serum.

Creatine kinase isoenzyme patterns in human tissue obtained at surgery.

Chromatography on DEAE-Sephadex A-50 was applied to study the quantitative distribution of creatine kinase isoenzymes in extracts of human tissue obtained during surgery. The results are compared with those determined by an immunological method [Clin. Chim. Acta 58, 223 (1975)]. Conflicting results for some organs as reported by the two methods are probably attributable to postmortem autolysis.

Quantitation of creatine kinase isoenzymes in human tissues and sera by an immunological method

Antisera against the crystallized creatine kinase isoenzymes from human skeletal muscle (MM) and from human brain (BB) were produced in rabbits. Both the MM and BB isoenzymes were precipitated quantitatively by their homologous antisera. No cross-reaction was observed. The hybrid MB from human heart muscle could not be precipitated completely by either of the two antisera. In artifical mixtures the concentrations of individual creatine kinase isoenzymes were determined from the percentage of non-precipitable activity in the supernatant after reaction with each of the antisera. This immunotitration assay was applied to study the quantitative distribution of creatine kinase isoenzymes in extracts of human tissues. The isoenzyme patterns obtained were compared with those determined by electrophoretic analysis. In sera of patients with myocardial infarction, the immunotitration assay allowed the sensitive and rapid quantitation of creatine kinase isoenzymes, especially of the “infarct-specific” hybrid MB, even in sera with low total activity. This indicates that the method is of diagnostic value.