Regenerated soleus muscle shows reduced creatine kinase efflux after contractile activity in vitro (original) (raw)
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Creatine-Kinase- and Exercise-Related Muscle Damage Implications for Muscle Performance and Recovery
Journal of Nutrition and Metabolism, 2012
The appearance of creatine kinase (CK) in blood has been generally considered to be an indirect marker of muscle damage, particularly for diagnosis of medical conditions such as myocardial infarction, muscular dystrophy, and cerebral diseases. However, there is controversy in the literature concerning its validity in reflecting muscle damage as a consequence of level and intensity of physical exercise. Nonmodifiable factors, for example, ethnicity, age, and gender, can also affect enzyme tissue activity and subsequent CK serum levels. The extent of effect suggests that acceptable upper limits of normal CK levels may need to be reset to recognise the impact of these factors. There is a need for standardisation of protocols and stronger guidelines which would facilitate greater scientific integrity. The purpose of this paper is to examine current evidence and opinion relating to the release of CK from skeletal muscle in response to physical activity and examine if elevated concentrations are a health concern.
Activity of creatine kinase in a contracting mammalian muscle of uniform fiber type
Biophysical Journal, 1994
We investigated whether the creatine kinase-catalyzed phosphate exchange between PCr and-yATP in vivo equilibrated with cellular substrates and products as predicted by in vitro kinetic properties of the enzyme, or was a function of ATPase activity as predicted by obligatory "creatine phosphate shuttle" concepts. A transient NMR spin-transfer method was developed, tested, and applied to resting and stimulated ex vivo muscle, the soleus, which is a cellularly homogeneous slowtwitch mammalian muscle, to measure creatine kinase kinetics. The forward and reverse unidirectional CK fluxes were equal, being 1.6 mMs-1 in unstimulated muscle at 220C, and 2.7 mMs-1 at 300C. The CK fluxes did not differ during steady-state stimulation conditions giving a 10-fold range of ATPase rates in which the ATP/PCr ratio increased from approximately 0.3 to 1.6. The observed kinetic behavior of CK activity in the muscle was that expected from the enzyme in vitro in a homogeneous solution only if account was taken of inhibition by an anion-stabilized quaternary dead-end enzyme complex: E-Cr-MgADP-anion. The CK fluxes in soleus were not a function of ATPase activity as predicted by obligatory phosphocreatine shuttle models for cellular energetics.
The creatine kinase response to resistance exercise
Journal of musculoskeletal & neuronal interactions, 2014
Resistance exercise can result in localized damage to muscle tissue. This damage may be observed in sarcolemma, basal lamina, as well as, in the contractile elements and the cytoskeleton. Usually the damage is accompanied by release of enzymes such as creatine kinase (CK) and lactate dehydrogenase, myoglobin and other proteins into the blood. Serum CK has been proposed as one of the best indirect indicators of muscle damage due to its ease of identification and the relatively low cost of assays to quantify it. Thus, CK has been used as an indicator of the training intensity and a diagnostic marker of overtraining. However, some issues complicate CK's use in this manner. There is great interindividual variability in serum CK, which complicates the assignment of reliable reference values for athletes. Furthermore, factors such as training level, muscle groups involved, and gender can influence CK levels to a greater extent than differences in exercise volume completed. This review...
Medicine & Science in Sports & Exercise, 2010
Creatine kinase (CK) primarily serves as an energy buffer assisting in regulating ATP homeostasis through synthesis of ATP from ADP and phosphocreatine (PCr). This enzyme is bound in the sarcomere near sites of ATP consumption via acto-myosin ATPase (A•M•ATPase) and research in cardiac muscle has found that PCr can alter contractile performance (maximal isometric force and Ca 2+ sensitivity). Based on this evidence, CK and A•M•ATPase may be coupled in skeletal muscle. Therefore the purpose of this investigation was to determine the influence of the CK system on contractile performance and energy utilization in skeletal muscle. revisions of this document. There were also numerous others who assisted me in completing this work. Laboratory assistance with HPLC was kindly provided by Janet Rinehart. I am extremely grateful for chemical supplies provided by Carolyn Smith and Dr. Kathy Reynolds. This work would also not have been possible if not for the kind assistance of Dr. Hongwei Si and Dr. Dongmin Liu as well as the technicians at the Laboratory Animal Resources, especially Dave Gemmell. Lastly, I would like to thank the entire HNFE Department, especially Sherry Saville and Sherry Terry as well as my fellow graduate students, Mary
Pflügers Archiv - European Journal of Physiology, 2006
There has been speculation on the origin of the increased endurance of skeletal muscles in creatine kinase (CK)-deficient mice. Important factors that have been raised include the documented increased mitochondrial capacity and alterations in myosin heavy chain (MyHC) isoform composition in CK-deficient muscle. More recently, the absence of inorganic phosphate release from phosphocreatine hydrolysis in exercising CK-deficient muscle has been postulated to contribute to the lower fatigueability in skeletal muscle. In this study, we tested the hypothesis that the reported shift in MyHC composition to slower isoforms in CK-deficient muscle leads to a decrease in oxygen cost of twitch performance. To that aim, extensor digitorum longus (EDL) and soleus (SOL) muscles were isolated from wild-type (WT) and knock-out mice deficient in the cytoplasmic muscle-type and sarcomeric mitochondrial isoenzymes of CK, and oxygen consumption per twitch time-tension-integral (TTI) was measured. The results show that the adaptive response to loss of CK function does not involve any major change to contractile economy of skeletal muscle.
Adaptive responses to creatine loading and exercise in fast-twitch rat skeletal muscle
American Journal of Physiology-regulatory Integrative and Comparative Physiology, 2008
We investigated the effects of chronic creatine (Cr) loading and voluntary running (Run) on muscle fiber types, proteins that regulate intracellular calcium and on the metabolic profile in rat plantaris, in order to ascertain the bases for our previous observations that Cr loading results in a higher proportion of myosin heavy chain (MHC)-IIb, without corresponding changes in contractile properties. Forty Sprague-Dawley rats were assigned to one of four groups: Cr+Sedentary (Cre-Sed); Cr+Run (Cre-Run); control+Sed (Con-Sed); Con+Run (Con-Run). Cre-Run, compared to Con-Run, resulted in 10% and 15% increases in proportion and cross-sectional area of type IIB fibres, and an 11% decrease in IIA fibres (P < 0.03). No differences were observed in content of the fast Ca 2+ ATPase isoform, SERCA1 (P > 0.49). Cr feeding alone induced a 41% increase (P < 0.03) in slow Ca 2+ -ATPase (SERCA2) content, which was further elevated by 33% with running (P < 0.02). Run training alone reduced parvalbumin content by 50% (P < 0.05). By comparison, Cr feeding alone dramatically decreased parvalbumin content by 75% (P < 0.01) but was not further reduced by run training. These adaptive changes indicate that elevating the capacity for high-energy phosphate shuttling, through Cr loading, alleviates the need for intracellular Ca 2+ buffering by parvalbumin, and increases the efficiency of Ca 2+ uptake by SERCA's. Citrate synthase and 3hydroxyacyl-CoA dehydrogenase activities were elevated with run training (P < 0.003) but not when combined with Cr feeding. This indicates that Cr loading during run training supports a faster muscle phenotype that is adequately supported by the existing glycolytic potential, without changes in the capacity for terminal substrate oxidation.
Muscle Recovery After a Session of Resistance Training Monitored Through Serum Creatine Kinase
Medicine & Science in Sports & Exercise, 2011
De Castro APA, Vianna JM, Damasceno VO, Matos DG, Mazini Filho ML, Reis VMM. Muscle Recovery after a Session of Resistance Training Monitored through Serum Creatine Kinase. JEPonline 2011;14 :38-45. The purpose of this study was to monitor the recovery period after a session of resistance training through the levels of serum creatine kinase (CK). Nine healthy subjects who were experienced in resistance training engaged in a training session that consisted of eight exercises with a load of 10 repetitions maximum (10 RM). For the monitoring of CK values, blood tests were performed prior to the training protocol (CKp) and 24 hrs (CK24), 48 hrs (CK48), and 72 hrs (CK72) after training. Significant differences were observed between the mean values of CKp and CK24 and CK48. Thus, the findings support the contention that the CK values at 48 hrs and 72 hrs after a training session with 10 RM are sufficient for the recovery of muscle fibers.
European Journal of Applied Physiology, 2010
The protective effect of short-term creatine supplementation (CrS) upon markers of strenuous contractile activity-induced damage in human and rat skeletal muscles was investigated. Eight Ironman triathletes were randomized into the placebo (Pl; n = 4) and creatine-supplemented (CrS; n = 4) groups. Five days prior to the Ironman competition, the CrS group received creatine monohydrate (20 g day−1) plus maltodextrin (50 g) divided in two equal doses. The Pl group received maltodextrin (50 g day−1) only. The effect of CrS (5 g day−1/kg body weight for 5 days) was also evaluated in a protocol of strenuous contractile activity induced by electrical stimulation in rats. Blood samples were collected before and 36 and 60 h after the competition and were used to determine plasma activities of creatine kinase (CK), lactate dehydrogenase (LDH), aldolase (ALD), glutamic oxaloacetic acid transaminase (GOT), glutamic pyruvic acid transaminase (GPT), and C-reactive protein (CRP) level. In rats, plasma activities of CK and LDH, muscle vascular permeability (MVP) using Evans blue dye, muscle force and fatigue were evaluated. Activities of CK, ALD, LDH, GOT, GTP, and levels of CRP were increased in the Pl group after the competition as compared to basal values. CrS decreased plasma activities of CK, LDH, and ALD, and prevented the rise of GOT and GPT plasma activities. In rats, CrS delayed the fatigue, preserved the force, and prevented the rise of LDH and CK plasma activities and MVP in the gastrocnemius muscle. CrS presented a protective effect on muscle injury induced by strenuous contractile activities.
Functional Equivalence of Creatine Kinase Isoforms in Mouse Skeletal Muscle
Journal of Biological Chemistry, 1997
Creatine kinase (CK) is a highly conserved enzyme abundant in skeletal muscle that has a key role in high energy phosphate metabolism. The localization of the muscle isoenzyme of CK (MM-CK) to the M line and the sarcoplasmic reticulum of myofibrils has been suggested to be important for proper force development in skeletal muscle. The importance of this subcellular compartmentation has not been directly tested in vivo. To test the role of myofibrilar localization of CK, the consequences of a complete CK isoform switch from MM-CK to the brain (BB-CK) isoform, which does not localize to the M line, was studied in transgenic mouse skeletal muscle. In MM-CK knockout mice there are large contractile defects. When MM-CK was replaced by BB-CK, the aberrant contractile phenotypes seen in MM-CK knockout mice were returned to normal despite the lack of myofibrillar localization. These results indicate that CK compartmentation to the myofibril of skeletal muscle is not essential for contractile function and that there is functional equivalence of creatine kinase isoforms in supporting cellular energy metabolism.