Genetic basis of creatine kinase isozymes in skeletal muscle of salmonid fishes

1979 ◽  
Vol 17 (11-12) ◽  
pp. 1079-1091 ◽  
Author(s):  
F. M. Utter ◽  
F. W. Allendorf ◽  
B. May
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Genetic Basis ◽  
Salmonid Fishes ◽  
Creatine Kinase Isozymes

Comparative studies on creatine kinase isozymes from skeletal-muscle and stomach of trout

1972 ◽  
Vol 182 (1) ◽  
pp. 119-125 ◽  
Author(s):  
Jean-Claude Perriard ◽  
Adolf Scholl ◽  
Hans M. Eppenberger
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Comparative Studies ◽  
Creatine Kinase Isozymes

scholarly journals Fixation and immunofluorescent analysis of creatine kinase isozymes in embryonic skeletal muscle.

1987 ◽  
Vol 35 (7) ◽  
pp. 717-722 ◽  
Author(s):  
M M Robinson
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Fixation Procedure ◽  
Creatine Kinase B ◽  
Immunofluorescent Analysis ◽  
Embryonic Muscle ◽  
Creatine Kinase Isozymes

Pectoral muscles from chicken embryos of various ages were examined with immunofluorescent and radiolabeled probes for the presence of brain-type creatine kinase (B-CK), muscle-specific creatine kinase (M-CK), muscle-specific myosin heavy chain (MHC), and cycling cells. The diffusible creatine kinase isozymes were not detectable by indirect immunofluorescence after standard histological fixation of embryonic muscle. However, a fixation procedure was devised that permitted immunodetection of the creatine kinase isozymes (particularly B-CK) in embryonic tissue from all stages of development studied. B-CK, M-CK, and MHC were all detected in post-mitotic muscle cells, but only B-CK was detected in cycling cells. Correlations between these findings and in vitro observations of a deterministic muscle lineage are discussed.

Slow skeletal muscle myosin-binding protein-C (MyBPC1) mediates recruitment of muscle-type creatine kinase (CK) to myosin

2011 ◽  
Vol 436 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Zhe Chen ◽  
Tong-Jin Zhao ◽  
Jie Li ◽  
Yan-Song Gao ◽  
Fan-Guo Meng ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Muscle Contraction ◽  
Binding Protein ◽  
High Energy ◽  
Functional Coupling ◽  
Muscle Type ◽  
Myosin Binding Protein ◽  
Slow Skeletal Muscle ◽  
Myosin Binding

Muscle contraction requires high energy fluxes, which are supplied by MM-CK (muscle-type creatine kinase) which couples to the myofibril. However, little is known about the detailed molecular mechanisms of how MM-CK participates in and is regulated during muscle contraction. In the present study, MM-CK is found to physically interact with the slow skeletal muscle-type MyBPC1 (myosin-binding protein C1). The interaction between MyBPC1 and MM-CK depended on the creatine concentration in a dose-dependent manner, but not on ATP, ADP or phosphocreatine. The MyBPC1–CK interaction favoured acidic conditions, and the two molecules dissociated at above pH 7.5. Domain-mapping experiments indicated that MM-CK binds to the C-terminal domains of MyBPC1, which is also the binding site of myosin. The functional coupling of myosin, MyBPC1 and MM-CK is further corroborated using an ATPase activity assay in which ATP expenditure accelerates upon the association of the three proteins, and the apparent Km value of myosin is therefore reduced. The results of the present study suggest that MyBPC1 acts as an adaptor to connect the ATP consumer (myosin) and the regenerator (MM-CK) for efficient energy metabolism and homoeostasis.

Elevation of Creatine Kinase From Skeletal Muscle Associated with Inhaled Albuterol

1996 ◽  
Vol 77 (6) ◽  
pp. 488-490 ◽  
Author(s):  
Timothy J Craig ◽  
William Smits ◽  
V Soontornniyomkiu
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase

Modifications in the Concentrations of Circulating Myoglobin after Treatment with Low Doses of Adriamycin

1985 ◽  
Vol 71 (5) ◽  
pp. 463-468 ◽  
Author(s):  
Giovanni Carulli ◽  
Aldo Clerico ◽  
Alessandra Marini ◽  
Maria Grazia Del Chicca ◽  
Renato Vanacore ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Cancer Patients ◽  
Muscle Damage ◽  
Low Doses ◽  
Skeletal Muscle Damage ◽  
Creatine Kinase Mb

The modifications in the concentration of circulating myoglobin have been studied by means of a radioimmunoassay in 15 cancer patients undergoing polychemotherapy including adriamycin. In 8 patients significant increases in myoglobin levels were found after injection of low doses of the drug (25-50 mg/m2). Moreover, a disturbance of the normal biorhythm of the protein was evident in 12 patients. Creatine kinase-MB was evaluated by means of a radioimmunoassay, but there was no relation between an increase in the isoenzyme and an increase in myoglobin. No ECG modifications were detected. These data indicate that the measurement of myoglobin may offer an indication of myocardial or skeletal muscle damage caused by adriamycin.

Creatine kinase activity of urinary bladder and skeletal muscle from control and streptozotocin-diabetic rats

1990 ◽  
Vol 97 (2) ◽  
Author(s):  
RobertM. Levin ◽  
PenelopeA. Longhurst ◽  
SheilaS. Levin ◽  
Niels Haugaard ◽  
AlanJ. Wein
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Urinary Bladder ◽  
Kinase Activity ◽  
Diabetic Rats ◽  
Creatine Kinase Activity ◽  
Streptozotocin Diabetic Rats

scholarly journals Influence of rapid changes in cytosolic pH on oxidative phosphorylation in skeletal muscle: theoretical studies

2002 ◽  
Vol 365 (1) ◽  
pp. 249-258 ◽  
Author(s):  
Bernard KORZENIEWSKI ◽  
Jerzy A. ZOLADZ
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Oxidative Phosphorylation ◽  
Kinetic Properties ◽  
Main Role ◽  
Anaerobic Glycolysis ◽  
Cytosolic Ph ◽  
Intensive Exercise ◽  
Proton Production ◽  
The Stability

Cytosolic pH in skeletal muscle may vary significantly because of proton production/consumption by creatine kinase and/or proton production by anaerobic glycolysis. A computer model of oxidative phosphorylation in intact skeletal muscle developed previously was used to study the kinetic effect of these variations on the oxidative phosphorylation system. Two kinds of influence were analysed: (i) via the change in pH across the inner mitochondrial membrane and (ii) via the shift in the equilibrium of the creatine kinase-catalysed reaction. Our simulations suggest that cytosolic pH has essentially no impact on the steady-state fluxes and most metabolite concentrations. On the other hand, rapid acidification/alkalization of cytosol causes a transient decrease/increase in the respiration rate. Furthermore, changes in pH seem to affect significantly the kinetic properties of transition between resting state and active state. An increase in pH brought about by proton consumption by creatine kinase at the onset of exercise lengthens the transition time. At intensive exercise levels this pH increase could lead to loss of the stability of the system, if not compensated by glycolytic H+ production. Thus our theoretical results stress the importance of processes/mechanisms that buffer/compensate for changes in cytosolic proton concentration. In particular, we suggest that the second main role of anaerobic glycolysis, apart from additional ATP supply, may be maintaining the stability of the system at intensive exercise.

Geographic distribution of xanthine oxidase, free radical scavengers, creatine kinase, and lactate dehydrogenase enzyme systems in rat heart and skeletal muscle

1991 ◽  
Vol 192 (3) ◽  
pp. 319-323 ◽  
Author(s):  
Fred S. Apple ◽  
John E. Hyde ◽  
Ann Marie Ingersoll-Stroubos ◽  
Athanasios Theologides
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Free Radical ◽  
Lactate Dehydrogenase ◽  
Xanthine Oxidase ◽  
Rat Heart ◽  
Free Radical Scavengers ◽  
Radical Scavengers ◽  
Enzyme Systems ◽  
Dehydrogenase Enzyme
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