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      Effect of Dietary Creatine on Skeletal Muscle Myosin Heavy Chain Isoform Expression in an Animal Model of Uremia

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          Background: Chronic renal failure is accompanied with muscle dysfunction and myopathy, characterized by muscle weakness and increased fatigue. Myosin heavy chain (MHC) is the principal structural protein that controls the intrinsic contractile properties of striated muscle. Creatine is widely used as an ergogenic nutritional supplement in sportsmen. This study investigates the effect of creatine supplementation on MHC expression in the setting of uremic myopathy. Methods: Male Wistar rats were either sham operated or subtotally nephrectomized and received a control diet or creatine (2% w/w)-supplemented diet. After 4 weeks of treatment, serum creatinine, creatine, urea and creatinine clearances were determined. MHC isoforms were determined electrophoretically in the extensor digitorum longus and soleus muscles. Results: Creatinine clearances were lower in nephrectomized animals, but similar in creatine-supplemented and control diet animals. Nephrectomized animals had significantly higher MHC IIb and lower MHC IIx isoform expression in the extensor digitorum longus muscle compared to sham-operated animals. In the soleus muscle, MHC IIb expression was increased in nephrectomized animals. Creatine supplementation reversed the MHC transitions observed in uremia in the soleus muscle, but not in the extensor digitorum longus muscle. Conclusion: We observed altered expression of MHC isoforms in uremia. In uremic animals, fast MHC IIb isoforms were increased, whereas MHC I and IIx isoforms predominate in control animals. Dietary creatine supplementation reversed the altered MHC expression during uremia in slow-twitch, but not in fast-twitch muscles.

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          Most cited references 5

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          Effects of oral creatine and resistance training on myosin heavy chain expression.

          This study examined 12 wk of creatine (Cr) supplementation and heavy resistance training on muscle strength and myosin heavy chain (MHC) isoform mRNA and protein expression. Twenty-two untrained male subjects were randomly assigned to either a control (CON), placebo (PLC), or Cr (CRT) group in a double-blind fashion. Muscle biopsies were obtained before and after 12 wk of heavy resistance training. PLC and CRT trained thrice weekly using three sets of 6-8 repetitions at 85-90% 1-RM on the leg press, knee extension, and knee curl exercises. CRT ingested 6 g.d-1 of Cr for 12 wk, whereas PLC consumed the equal concentration of placebo. There were no significant differences for percent body fat (P > 0.05). However, for total body mass, fat-free mass, thigh volume, muscle strength, and myofibrillar protein, CRT and PLC exhibited significant increases after training when compared to CON (P < 0.05), whereas CRT was also significantly greater than PLC (P < 0.05). For Type I, IIa, and IIx MHC mRNA expression, CRT was significantly greater than CON and PLC, whereas PLC was greater than CON (P < 0.05). For MHC protein expression, CRT was significantly greater than CON and PLC for Type I and IIx (P < 0.05) but was equal to PLC for IIa. Long-term Cr supplementation increases muscle strength and size, possibly as a result of increased MHC synthesis.
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            Uremic myopathy.

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              ATPase Activity of Myosin Correlated with Speed of Muscle Shortening

              Myosin was isolated from 14 different muscles (mammals, lower vertebrates, and invertebrates) of known maximal speed of shortening. These myosin preparations were homogeneous in the analytical ultracentrifuge or, in a few cases, showed, in addition to the main myosin peak, part of the myosin in aggregated form. Actin- and Ca++-activated ATPase activities of the myosins were generally proportional to the speed of shortening of their respective muscles; i.e. the greater the intrinsic speed, the higher the ATPase activity. This relation was found when the speed of shortening ranged from 0.1 to 24 muscle lengths/sec. The temperature coefficient of the Ca++-activated myosin ATPase was the same as that of the speed of shortening, Q10 about 2. Higher Q10 values were found for the actin-activated myosin ATPase, especially below 10°C. By using myofibrils instead of reconstituted actomyosin, Q10 values close to 2 could be obtained for the Mg++-activated myofibrillar ATPase at ionic strength of 0.014. In another series of experiments, myosin was isolated from 11 different muscles of known isometric twitch contraction time. The ATPase activity of these myosins was inversely proportional to the contraction time of the muscles. These results suggest a role for the ATPase activity of myosin in determining the speed of muscle contraction. In contrast to the ATPase activity of myosin, which varied according to the speed of contraction, the F-actin-binding ability of myosin from various muscles was rather constant.

                Author and article information

                Nephron Exp Nephrol
                Cardiorenal Medicine
                S. Karger AG
                April 2004
                17 November 2004
                : 96
                : 4
                : e103-e110
                aLaboratory of Clinical Chemistry, and bRenal Unit, Department of Internal Medicine, University Hospital Ghent, Ghent, Belgium
                77376 Nephron Exp Nephrol 2004;96:e103–e110
                © 2004 S. Karger AG, Basel

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                Figures: 3, Tables: 1, References: 34, Pages: 1
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