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1.
J Exp Biol ; 214(Pt 23): 3915-23, 2011 Dec 01.
Article in English | MEDLINE | ID: mdl-22071182

ABSTRACT

The purpose of this study was to test the hypothesis that the potentiation of concentric twitch force during work cycles is dependent upon both the speed and direction of length change. Concentric and eccentric forces were elicited by stimulating muscles during the shortening and lengthening phases, respectively, of work cycles. Work cycle frequency was varied in order to vary the speed of muscle shortening and/or lengthening; all forces were measured as the muscle passed though optimal length (L(o)). Both concentric and eccentric force were assessed before (unpotentiated control) and after (potentiated) the application of a tetanic conditioning protocol known to potentiate twitch force output. The influence of the conditioning protocol on relative concentric force was speed dependent, with forces increased to 1.19±0.01, 1.25±0.01 and 1.30±0.01 of controls at 1.5, 3.3 and 6.9 Hz, respectively (all data N=9-10 with P<0.05). In contrast, the conditioning protocol had only a limited effect on eccentric force at these frequencies (range: 1.06±0.01 to 0.96±0.03). The effect of the conditioning protocol on concentric work (force × distance) was also speed dependent, being decreased at 1.5 Hz (0.84±0.01) and increased at 3.3 and 6.9 Hz (1.05±0.01 and 1.39±0.01, respectively). In contrast, eccentric work was not increased at any frequency (range: 0.88±0.02 to 0.99±0.01). Thus, our results reveal a hysteresis-like influence of activity-dependent potentiation such that concentric force and/or work were increased but eccentric force and/or work were not. These outcomes may have implications for skeletal muscle locomotor function in vivo.


Subject(s)
Muscle Fibers, Fast-Twitch/physiology , Animals , Biomechanical Phenomena/physiology , Female , Isometric Contraction/physiology , Mice , Mice, Inbred C57BL , Myosin Light Chains/metabolism , Phosphorylation , Physical Stimulation , Temperature
2.
Pflugers Arch ; 462(2): 349-58, 2011 Aug.
Article in English | MEDLINE | ID: mdl-21499697

ABSTRACT

The intent of this study was to determine if the stimulation-induced increase or "potentiation" of dynamic function of mouse extensor digitorum longus muscle (in vitro 25°C) during work cycles is graded to myosin regulatory light-chain (RLC) phosphorylation. To do this, concentric force and muscle work output during sinusoidal length changes were determined before (unpotentiated) and after (potentiated) the application of conditioning stimuli (CS) producing incremental elevations in RLC phosphorylation from rest. Sine wave excursion was from 1.09 to 0.91 of L (o) with a period of 142 ms; stimulating muscles to twitch and generate force during these cycles produced plots of force × displacement termed work loops. Stimulation at 2.5-, 5.0-, and 100-Hz elevated RLC phosphorylation from 0.16±0.02 (rest) to 0.29±0.03, 0.45±0.02 and 0.56±0.02 mol phos per mole RLC, respectively (n= 6-7, P<0.05). These CS potentiated mean concentric force (at all lengths) to 1.14±0.02, 1.26±0.04 and 1.41±0.06 of pre-stimulus, control levels (all n= 5-7, P<0.05) while work was increased to 1.07±0.02, 1.17±0.02 and 1.34±0.03 of controls, respectively. In a No CS condition that did not elevate RLC phosphorylation, neither mean concentric force nor work was altered. Thus, strong correlations between RLC phosphorylation and mean concentric force and work support the hypothesis that this molecular mechanism modulates muscle power output. No length-dependence for concentric force potentiation was observed in any condition, an outcome suggesting that interactions between instantaneous variations in muscle length and shortening velocity during work cycles modulates the potentiation response.


Subject(s)
Muscle Contraction/physiology , Muscle Fibers, Fast-Twitch/physiology , Muscle, Skeletal/physiology , Myosin Light Chains/physiology , Animals , Female , Isometric Contraction/physiology , Mice , Mice, Inbred C57BL , Muscle Fibers, Fast-Twitch/cytology , Muscle, Skeletal/cytology , Phosphorylation
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