Serum and Muscle Creatine Kinase Isoenzymes and Serum Aspartate Aminotransferase Isoenzymes in Progressive Muscular Dystrophy

Enzyme ◽  
1971 ◽  
Vol 12 (1) ◽  
pp. 49-62 ◽  
Author(s):  
A. Cao ◽  
S. de Virgiliis ◽  
C. Lippi ◽  
G. Coppa
Keyword(s):  
Creatine Kinase ◽  
Muscular Dystrophy ◽  
Aspartate Aminotransferase ◽  
Muscle Creatine Kinase ◽  
Progressive Muscular Dystrophy ◽  
Creatine Kinase Isoenzymes ◽  
Serum Aspartate Aminotransferase ◽  
Muscle Creatine

Creatine kinase isoenzymes of mitochondrial origin in human serum.

1979 ◽  
Vol 25 (6) ◽  
pp. 943-947 ◽  
Author(s):  
G P James ◽  
R L Harrison
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Lactate Dehydrogenase ◽  
Serum Samples ◽  
Muscle Creatine Kinase ◽  
Cellulose Acetate Electrophoresis ◽  
University Of Texas ◽  
Creatine Kinase Isoenzymes ◽  
Mitochondrial Origin ◽  
Muscle Creatine

Abstract We measured creatine kinase (EC 2.7.3.2) activity in 1009 serum samples from 538 patients in the intensive-care units of the University of Texas Medical Branch hospitals. Creatine kinase isoenzymes migrating cathodal to skeletal muscle creatine kinase (CK-MM) on cellulose acetate electrophoresis were found in sera from 14 of the 538 patients. Creatine kinase, lactate dehydrogenase (EC 1.1.1.27), aspartate aminotransferase (EC 2.6.1.1), and alanine aminotransferase (EC 2.6.1.2) activities were abnormally increased in these 14 patients. Liver lactate dehydrogenase isoenzyme (LDH5) and cardiac creatine kinase isoenzyme (CK-MB) were abnormally increased in 12 and eight of these patients, respectively. Ten of the 14 patients died during their hospital admission. We believe the creatine kinase isoenzymes that migrated cathodal to skeletal muscle creatine kinase (CK-MM) were of mitochondrial origin.

scholarly journals The Role of Common Carp (Cyprinus carpio) Muscle Creatine Kinase Isoenzymes at Temperature Acclimation

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1033-1036
Author(s):  
Hsi-Wen Sun ◽  
Cheng-Wen Liu ◽  
Chih-Lu Wu ◽  
Cho-Fat Hui ◽  
Jen-Leih Wu
Keyword(s):  
Creatine Kinase ◽  
Common Carp ◽  
Cyprinus Carpio ◽  
Temperature Acclimation ◽  
Muscle Creatine Kinase ◽  
Creatine Kinase Isoenzymes ◽  
Muscle Creatine

scholarly journals Complete cDNA-derived amino acid sequence of chick muscle creatine kinase.

1984 ◽  
Vol 259 (24) ◽  
pp. 15224-15227
Author(s):  
C P Ordahl ◽  
G L Evans ◽  
T A Cooper ◽  
G Kunz ◽  
J C Perriard
Keyword(s):  
Creatine Kinase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Muscle Creatine Kinase ◽  
Muscle Creatine

scholarly journals Molecular docking and density functional theory studies on creatine, guanidinoacetic acid, and their phosphorylated analogues binding to muscle creatine kinase

2020 ◽  
pp. 174751982097858
Author(s):  
M Vraneš ◽  
S Ostojić ◽  
Č Podlipnik ◽  
A Tot
Keyword(s):  
Density Functional Theory ◽  
Creatine Kinase ◽  
Molecular Docking ◽  
Density Functional ◽  
Creatine Phosphate ◽  
Docking Studies ◽  
Muscle Creatine Kinase ◽  
Functional Theory ◽  
Guanidinoacetic Acid ◽  
Muscle Creatine

Comparative molecular docking studies on creatine and guanidinoacetic acid, as well as their phosphorylated analogues, creatine phosphate, and phosphorylated guanidinoacetic acid, are investigated. Docking and density functional theory studies are carried out for muscle creatine kinase. The changes in the geometries of the ligands before and after binding to the enzyme are investigated to explain the better binding of guanidinoacetic acid and phosphorylated guanidinoacetic acid compared to creatine and creatine phosphate.

Sodium barbital is a slow reversible inactivator of rabbit-muscle creatine kinase

2006 ◽  
Vol 84 (2) ◽  
pp. 142-147
Author(s):  
Feng Shi ◽  
Tong-Jin Zhao ◽  
Hua-Wei He ◽  
Jie Li ◽  
Xian-Gang Zeng ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Energy Homeostasis ◽  
Inactivation Kinetics ◽  
Rabbit Muscle ◽  
Muscle Creatine Kinase ◽  
Reversible Inactivation ◽  
Inhibition Effect ◽  
Sodium Barbital ◽  
Muscle Creatine ◽  
Detailed Kinetics

As a depressant of the central nervous system, the clinical effect of sodium barbital has been extensively studied. Here we report on sodium barbital as an inhibitor of rabbit-muscle creatine kinase (CK), which plays a significant role in energy homeostasis in the muscles. Although sodium barbital gradually inhibits the activity of CK with increased concentration, the inhibition effect can be completely reversed by dilution, indicating that the inactivation process is reversible. Detailed kinetics analysis, according to a previously presented theory, indicates that sodium barbital functions as a non complexing inhibitor, and its inhibition effect on CK is a slow reversible inactivation. In this study, a kinetic model of the substrate reaction is presented, and the microscopic rate constants for the reaction of sodium barbital with the free enzyme and the enzyme–substrate complexes are determined. Kinetic analysis reveals that sodium barbital might compete with both creatine and ATP, but mainly with creatine, to inhibit the activity of CK. The results suggest that CK might be a target for sodium barbital in vivo.Key words: creatine kinase; inactivation; kinetics; sodium barbital.

scholarly journals Brain and muscle creatine kinase genes contain common TA-rich recognition protein-binding regulatory elements.

1990 ◽  
Vol 10 (9) ◽  
pp. 4826-4836 ◽  
Author(s):  
R A Horlick ◽  
G M Hobson ◽  
J H Patterson ◽  
M T Mitchell ◽  
P A Benfield
Keyword(s):  
Creatine Kinase ◽  
Binding Site ◽  
Regulatory Element ◽  
Gene Promoter ◽  
Regulatory Elements ◽  
Muscle Creatine Kinase ◽  
Enhancer Activity ◽  
L6 Myotubes ◽  
Recognition Protein ◽  
Muscle Creatine

We have previously reported that the rat brain creatine kinase (ckb) gene promoter contains an AT-rich sequence that is a binding site for a protein called TARP (TA-rich recognition protein). This AT-rich segment is a positively acting regulatory element for the ckb promoter. A similar AT-rich DNA segment is found at the 3' end of the 5' muscle-specific enhancer of the rat muscle creatine kinase (ckm) gene and has been shown to be necessary for full muscle-specific enhancer activity. In this report, we show that TARP binds not only to the ckb promoter but also to the AT-rich segment at the 3' end of the muscle-specific ckm enhancer. A second, weaker TARP-binding site was identified in the ckm enhancer and lies at the 5' end of the minimal enhancer segment. TARP was found in both muscle cells (C2 and L6 myotubes) and nonmuscle (HeLa) cells and appeared to be indistinguishable from both sources, as judged by gel retardation and footprinting assays. The TARP-binding sites in the ckm enhancer and the ckb promoter were found to be functionally interchangeable. We propose that TARP is active in both muscle and nonmuscle cells and that it is one of many potential activators that may interact with muscle-specific regulators to determine the myogenic phenotype.

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