Alterations in the expression and activity of creatine kinase-M and mitochondrial creatine kinase subunits in skeletal muscle following prolonged intense exercise in rats

2000 ◽  
Vol 81 (1-2) ◽  
pp. 114-119 ◽  
Author(s):  
YingJie Chen ◽  
Robert C. Serfass ◽  
Fred S. Apple
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Intense Exercise ◽  
Mitochondrial Creatine Kinase ◽  
Expression And Activity

scholarly journals Maturation of Mitochondrial and other Isoenzymes of Creatine Kinase in Skeletal Muscle of Preterm Born Infants

1992 ◽  
Vol 29 (3) ◽  
pp. 302-306 ◽  
Author(s):  
J Smeitink ◽  
W Ruitenbeek ◽  
T v Lith ◽  
R Sengers ◽  
F Trijbels ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Protein Content ◽  
Human Skeletal Muscle ◽  
Specific Activity ◽  
Prenatal Development ◽  
Quadriceps Muscle ◽  
Mitochondrial Creatine Kinase ◽  
Total Creatine ◽  
Preterm Born

We studied pre- and postnatal changes in total creatine kinase (CK) activity, mitochondrial creatine kinase (Mi-CK) activity and immunochemical reactivity with anti-Mi-CK antibodies in skeletal muscle specimens from 12 infants, 10 of them preterm born, after a pregnancy varying between 28 and 40 weeks. Our results demonstrate that Mi-CK is present in fetal human quadriceps muscle and that the specific activity of Mi-CK increases during prenatal development from week 28 to 40 by a factor about two. Generally, adult levels have not been reached at birth, indicating a further postnatal increase of the activity of the enzyme. The Mi-CK protein content also increases during prenatal development. These results suggest that in human skeletal muscle the expression and accumulation of Mi-CK starts at mid-gestation, later than is known to occur for cytosolic CK.

scholarly journals Mitochondrial creatine kinase activity and phosphate shuttling are acutely regulated by exercise in human skeletal muscle

2012 ◽  
Vol 590 (21) ◽  
pp. 5475-5486 ◽  
Author(s):  
Christopher G. R. Perry ◽  
Daniel A. Kane ◽  
Eric A. F. Herbst ◽  
Kazutaka Mukai ◽  
Daniel S. Lark ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Human Skeletal Muscle ◽  
Kinase Activity ◽  
Creatine Kinase Activity ◽  
Mitochondrial Creatine Kinase

scholarly journals Chronic Hypoxia Enhances Expression and Activity of Mitochondrial Creatine Kinase and Hexokinase in the Rat Ventricular Myocardium

2014 ◽  
Vol 33 (2) ◽  
pp. 310-320 ◽  
Author(s):  
Petra Waskova-Arnostova ◽  
Dita Kasparova ◽  
Barbara Elsnicova ◽  
Jiri Novotny ◽  
Jan Neckar ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Chronic Hypoxia ◽  
Ventricular Myocardium ◽  
Mitochondrial Creatine Kinase ◽  
Expression And Activity

A Method for Quantitative Measurement of Mitochondrial Creatine Kinase in Human Skeletal Muscle

1992 ◽  
Vol 29 (2) ◽  
pp. 196-201 ◽  
Author(s):  
J Smeitink ◽  
R Wevers ◽  
J Hulshof ◽  
W Ruitenbeek ◽  
T v Lith ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Human Skeletal Muscle ◽  
Quantitative Measurement ◽  
Mitochondrial Creatine Kinase ◽  
Biopsy Material ◽  
Skeletal Muscle Biopsy ◽  
Wet Weight ◽  
Enzyme Complexes ◽  
Generating System

Defects in the mitochondrial energy generating system in patients with a mitochondrial myopathy are known to be localized in various enzyme complexes involved in energy production. Such a defect may exist at the level of mitochondrial creatine kinase (Mi-CK). On that account we have developed a method for measurement of the enzyme activity in human skeletal muscle biopsy material (> 10 mg). Interfering creatine kinase isoenzymes are removed by anion exchange and affinity chromatography. The activity of Mi-CK in reference skeletal muscle homogenates amounts to 240±88 mU/mg protein (30±8·0 mU/mg wet weight).

Myofibrillar or mitochondrial creatine kinase deficiency alone does not impair mouse diaphragm isotonic function

2000 ◽  
Vol 88 (3) ◽  
pp. 973-980 ◽  
Author(s):  
Jon F. Watchko ◽  
Monica J. Daood ◽  
Bé Wieringa ◽  
Alan P. Koretsky
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Subcellular Localization ◽  
Maximum Power ◽  
Work Output ◽  
Null Mutant ◽  
Force Load ◽  
Mitochondrial Creatine Kinase ◽  
Tetanic Force ◽  
Isotonic Function

Creatine kinase (CK) provides ATP buffering in skeletal muscle and is expressed as 1) cytosolic myofibrillar CK (M-CK) and 2) sarcomeric mitochondrial CK (ScCKmit) isoforms that differ in their subcellular localization. The diaphragm (Dia) expresses both M-CK and ScCKmit in abundance. We compared the power and work output of 1) control CK-sufficient (Ctl), 2) M-CK-deficient [M-CK(−/−)], 3) ScCKmit-deficient [ScCKmit(−/−)], and 4) combined M-CK/ScCKmit-deficient null mutant [CK(−/−)] Dia during repetitive isotonic activations to determine the effect of CK phenotype on Dia function. Maximum power was obtained at ∼0.4 tetanic force in all groups. M-CK(−/−) and ScCKmit(−/−) Dia were able to sustain power and work output at Ctl levels during repetitive isotonic activation (75 Hz, 330-ms duration repeated each second at 0.4 tetanic force load), and the duration of sustained Dia shortening was 67 ± 4 s in M-CK(−/−), 60 ± 4 s in ScCKmit(−/−), and 62 ± 5 s in Ctl Dia. In contrast, CK(−/−) Dia power and work declined acutely and failed to sustain shortening altogether by 40 ± 6 s. We conclude that Dia power and work output are not absolutely dependent on the presence of either M-CK or ScCKmit, whereas the complete absence of CK acutely impairs Dia shortening capacity during repetitive activation.

Mitochondrial creatine kinase activity alterations in skeletal muscle during long-distance running

1986 ◽  
Vol 61 (2) ◽  
pp. 482-485 ◽  
Author(s):  
F. S. Apple ◽  
M. A. Rogers
Keyword(s):  
Skeletal Muscle ◽  
Creatine Kinase ◽  
Intracellular Transport ◽  
Gastrocnemius Muscle ◽  
Creatine Kinase Activity ◽  
Percentage Increase ◽  
Distance Running ◽  
Mitochondrial Creatine Kinase ◽  
Long Distance ◽  
Long Distance Running

In human gastrocnemius muscle obtained from long-distance runners, mitochondrial creatine kinase (CK) activities were significantly greater than nonrunning control skeletal muscle and significantly increased during training for and after a marathon race. Thus skeletal muscle tended to become similar to heart muscle in its mitochondrial CK composition. Total muscle CK activity was significantly different in males and females, was unaffected by marathon training and racing, and was similar to gastrocnemius muscle obtained from nonrunning controls. There was an inverse correlation between the maximum O2 uptake and the percentage increase in mitochondrial CK activity after training. These studies suggest that mitochondrial CK may play a key role in the intracellular transport of energy from mitochondrial to myofibrils in skeletal muscle during endurance exercise such as long-distance running.

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
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