Use of dantrolene plus multiple pulses to detect stress-susceptible porcine muscle

1986 ◽  
Vol 60 (4) ◽  
pp. 1313-1320 ◽  
Author(s):  
J. G. Quinlan ◽  
P. A. Iaizzo ◽  
G. A. Gronert ◽  
S. R. Taylor
Keyword(s):  
Intravenous Administration ◽  
Tibialis Anterior ◽  
Skeletal Muscles ◽  
Contractile Properties ◽  
Tension Development ◽  
Porcine Muscle ◽  
Multiple Pulses ◽  
Twitch Characteristics

Twitch characteristics of tibialis anterior muscles in situ were examined in stress-susceptible and normal swine. Three groups of pigs were studied: (1) purebred Pietrain stress-susceptible, (2) purebred Yorkshire normal, and (3) a crossbred (Pietrain-Yorkshire) litter containing both stress-susceptible and normal animals. Purebred and crossbred stress-susceptible pigs provided qualitatively similar results, as did purebred and crossbred normal pigs. Single stimuli produced greater than normal peak tensions and faster rates of tension development in stress-susceptible animals. Multiple stimuli (2–6 pulses at 5-ms intervals) increased peak tensions and rates of tension development, but did not augment differences between normal and stress-susceptible pigs. Intravenous administration of dantrolene reduced peak tensions and rates of tension development in all groups for single and multiple stimuli. However, the reduction was significantly less (P less than 0.01) for stress-susceptible pigs. Multiple stimuli (4–6 pulses) plus dantrolene amplified differences (P less than 0.01) in contractile properties between normal and stress-susceptible skeletal muscles, with stress-susceptible muscles obtaining larger peak tensions and faster rates of tension development. Normal and stress-susceptible pigs may, therefore, be distinguished by these procedures.

Phosphorylated beta-guanidinopropionate as a substitute for phosphocreatine in rat muscle

1975 ◽  
Vol 228 (4) ◽  
pp. 1123-1125 ◽  
Author(s):  
CD Fitch ◽  
M Jellinek ◽  
RH Fitts ◽  
KM Baldwin ◽  
JO Holloszy
Keyword(s):  
Muscle Contraction ◽  
Tibialis Anterior ◽  
High Energy ◽  
High Energy Phosphate ◽  
Tension Development ◽  
Rat Muscle ◽  
Peak Value

To evaluate phosphorylated beta-guanidinopropionate (beta-GPAP) as a substitute for phosphocreatine (PC), hypoxic tibialis anterior muscles were stimulated to contract isometrically in situ until twitch tension fell to 25 percent of the peak value. Muscles from rats fed beta-guanidinopropionic acid (beta-GPA) failed to exhibit the staircase phenomenon, and they developed 28 percent less tension than control muscles. In control muscles lactate increased from 0.75 to 20.99, ADP increased from 0.89 to 1.20, ATP decreased from 5.09 to 2.73, and PC decreased from 15.78 to 1.52 mumol/g. In muscles from rats fed beta-GPA, lactate increased from 0.85 to 14.31, ADP increased from 0.86 to 1.05, ATP decreased from 2.69 to 1.71, PC decreased from 0.73 to 0.30, and beta-GPAP decreased from 30.34 to 19.45 mumol/g. From these measurements, the use of high-energy phosphate was calculated to be reduced 32 percent in muscles from rats fed beta-GPA. The relationships between the use of high-energy phosphate was calculated to be reduced 32 percent in muscles from rats fed beta-GPA. The relationships between the use of high-energy phosphate and tension development confirm experimentally the ability of beta-GPAP to substitute for PC as a source of energy to sustain muscle contraction.

scholarly journals Contractile properties of in situ perfused skeletal muscles from rats with congestive heart failure

2002 ◽  
Vol 540 (2) ◽  
pp. 571-580 ◽  
Author(s):  
Per Kristian Lunde ◽  
Esther Verburg ◽  
Morten Eriksen ◽  
Ole M. Sejersted
Keyword(s):  
Heart Failure ◽  
Congestive Heart Failure ◽  
Skeletal Muscles ◽  
Contractile Properties

Contractile properties of bundles of fiber segments from skeletal muscles

1982 ◽  
Vol 243 (1) ◽  
pp. C66-C73 ◽  
Author(s):  
J. A. Faulkner ◽  
D. R. Claflin ◽  
K. K. McCully ◽  
D. A. Jones
Keyword(s):  
Skeletal Muscle ◽  
Muscle Fiber ◽  
Skeletal Muscles ◽  
Maximum Velocity ◽  
Skeletal Muscle Fiber ◽  
Contractile Properties ◽  
Tension Development ◽  
Velocity Of Shortening ◽  
Lower Maximum ◽  
Fixed End

Our purpose was to determine whether contractile properties of bundles of skeletal muscle fiber segments were significantly different from those of bundles of intact fibers. In frog muscles, the only difference between the contractile properties of fiber segments and intact fibers was a lower maximum velocity of shortening (Vo) for the fiber segments. In mammalian muscles, the contraction time (TPT), relaxation time (RT1/2), and maximum tetanus tension (Po) of bundles of fiber segments were not different from those of intact fibers, but the rate of tension development (dP/dt), twitch-to-tetanus ratio (Pt/Po) and Vo were lower. The lower dP/dt and Pt/Po resulted from increased compliance due to damaged sarcomeres near cut ends. Within 4-9 mm of a cut end, membrane potentials were less than control values, and sarcomeres lengthened during a fixed-end contraction. after the length of fiber segments was corrected for the exact portion that was not shortening, the Vo of fiber segments was not different from that of intact fibers. We conclude that valid estimates of contractile properties can be obtained from bundles of skeletal muscle fiber segments.

Contractile properties of rat soleus muscle: effects of training and fatique

1977 ◽  
Vol 233 (3) ◽  
pp. C86-C91 ◽  
Author(s):  
R. H. Fitts ◽  
J. O. Holloszy
Keyword(s):  
Prolonged Exercise ◽  
Contractile Properties ◽  
Treadmill Running ◽  
Contraction Time ◽  
Shortening Velocity ◽  
Tension Development ◽  
Prolonged Training ◽  
Rat Soleus Muscle ◽  
Tetanic Tension

The effects of exercise training and fatique on the contractile properties of rat soleus muscles have been investigated. Prolonged exercise, consisting of 2 h or daily treadmill running, induced small but significant decrease in contraction time, one-half relaxation time, and maximum tetanic tension (Po), and increase in the peak rate of tension development (dP/dt) during a twitch, and an increase in maximum shortening velocity (Vmax). The 20% increase in Vmax was proportional to the previously reported increase in actomyosin ATPase induced by 2 h of daily running. These results indicate that prolonged training can induce modifications of the neurally determined contractile properties of skeletal muscle. To investigate the effects of fatigue, soleus muscles were stimulated in situ with 250-ms trains of 100 Hz at a rate of 110 trains per minute for 30 min. This resulted in a 32% decrease in Po, a 48% decline in peak tetanic dP/dt, and a 12% decrease in Vmax in muscles of untrained animals. Muscles that had adapted to exercise were significantly protected against the decrease in Po (only an 8% decrease) and Vmax (no significant decrease) but not against the decline in peak dP/dt.

scholarly journals A novel miniature in-line load-cell to measure in-situ tensile forces in the tibialis anterior tendon of rats

PLoS ONE ◽  
2017 ◽  
Vol 12 (9) ◽  
pp. e0185209 ◽  
Author(s):  
Martin Schmoll ◽  
Ewald Unger ◽  
Manfred Bijak ◽  
Martin Stoiber ◽  
Hermann Lanmüller ◽  
...  
Keyword(s):  
Tibialis Anterior ◽  
Load Cell ◽  
Line Load ◽  
Tibialis Anterior Tendon ◽  
Tensile Forces

RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel

2004 ◽  
Vol 287 (1) ◽  
pp. C36-C45 ◽  
Author(s):  
Takashi Murayama ◽  
Yasuo Ogawa
Keyword(s):  
Binding Sites ◽  
Skeletal Muscles ◽  
Specific Activity ◽  
Adenine Nucleotides ◽  
Minor Effect ◽  
Mammalian Skeletal Muscle ◽  
Selective Stabilization ◽  
Underlying Mechanisms ◽  
A Minor

We showed that frog α-ryanodine receptor (α-RyR) had a lower gain of Ca2+-induced Ca2+ release (CICR) activity than β-RyR in sarcoplasmic reticulum (SR) vesicles, indicating selective “stabilization” of the former isoform (Murayama T and Ogawa Y. J Biol Chem 276: 2953–2960, 2001). To know whether this is also the case with mammalian RyR1, we determined [3H]ryanodine binding of RyR1 and RyR3 in bovine diaphragm SR vesicles. The value of [3H]ryanodine binding (B) was normalized by the number of maximal binding sites (Bmax), whereby the specific activity of each isoform was expressed. This B/Bmax expression demonstrated that ryanodine binding of individual channels for RyR1 was <15% that for RyR3. Responses to Ca2+, Mg2+, adenine nucleotides, and caffeine were not substantially different between in situ and purified isoforms. These results suggest that the gain of CICR activity of RyR1 is markedly lower than that of RyR3 in mammalian skeletal muscle, indicating selective stabilization of RyR1 as is true of frog α-RyR. The stabilization was partly eliminated by FK506 and partly by solubilization of the vesicles with CHAPS, each of which was additive to the other. In contrast, high salt, which greatly enhances [3H]ryanodine binding, caused only a minor effect on the stabilization of RyR1. None of the T-tubule components, coexisting RyR3, or calmodulin was the cause. The CHAPS-sensitive intra- and intermolecular interactions that are common between mammalian and frog skeletal muscles and the isoform-specific inhibition by FKBP12, which is characteristic of mammals, are likely to be the underlying mechanisms.

Abundance and subcellular distribution of MCT1 and MCT4 in heart and fast-twitch skeletal muscles

2000 ◽  
Vol 278 (6) ◽  
pp. E1067-E1077 ◽  
Author(s):  
Arend Bonen ◽  
Dragana Miskovic ◽  
Mio Tonouchi ◽  
Kathleen Lemieux ◽  
Marieangela C. Wilson ◽  
...  
Keyword(s):  
Subcellular Distribution ◽  
Tibialis Anterior ◽  
Skeletal Muscles ◽  
Inverse Relationship ◽  
Extensor Digitorum Longus ◽  
Plasma Membranes ◽  
Rat Hearts ◽  
T Tubules ◽  
Fast Twitch ◽  
White Gastrocnemius

The expression of two monocarboxylate transporters (MCTs) was examined in muscle and heart. MCT1 and MCT4 proteins are coexpressed in rat skeletal muscles, but only MCT1 is expressed in rat hearts. Among six rat fast-twitch muscles (red and white gastrocnemius, plantaris, extensor digitorum longus, red and white tibialis anterior) there was an inverse relationship between MCT1 and MCT4 ( r = −0.94). MCT1 protein was correlated with MCT1 mRNA ( r = 0.94). There was no relationship between MCT4 mRNA and MCT4 protein. MCT1 ( r = −0.97) and MCT4 ( r = 0.88) protein contents were correlated with percent fast-twitch glycolytic fiber. When normalized for their mRNAs, MCT1 but not MCT4 was still correlated with the percent fast-twitch glycolytic fiber composition of rat muscles ( r = −0.98). MCT1 and MCT4 were also measured in plasma membranes (PM), triads (TR), T tubules (TT), sarcoplasmic reticulum (SR), and intracellular membranes (IM). There was an intracellular pool of MCT4 but not of MCT1. The MCT1 subcellular distribution was as follows: PM (100%) > TR (31.6%) > SR (15%) = TT (14%) > IM (1.7%). The MCT4 subcellular distribution was considerably different [PM (100%) > TR (66.5%) > TT (36%) = SR (43%) > IM (24%)]. These studies have shown that 1) the mechanisms regulating the expression of MCT1 (transcriptional and posttranscriptional) and MCT4 (posttranscriptional) are different and 2) differences in MCT1 and MCT4 expression among muscles, as well as in their subcellular locations, suggest that they may have different roles in muscle.

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