The Effect of Temperature on Glycolysis in Brain and Skeletal Muscle from a Hibernator and a Non-Hibernator

1967 ◽  
Vol 40 (2) ◽  
pp. 201-206 ◽  
Author(s):  
Roy F. Burlington ◽  
Jacob E. Wiebers
Keyword(s):  
Skeletal Muscle ◽  
Effect Of Temperature

Effect of temperature on reactive hyperemia in skeletal muscle

1962 ◽  
Vol 202 (6) ◽  
pp. 1055-1058 ◽  
Author(s):  
Lloyd R. Yonce
Keyword(s):  
Skeletal Muscle ◽  
Blood Flow ◽  
Reactive Hyperemia ◽  
Vascular Occlusion ◽  
Effect Of Temperature ◽  
Temperature Step ◽  
Time Required

Circulatory reactivity to vascular occlusion for periods of 30, 60, and 120 sec was determined on eight isolated canine gracilis muscles under normothermic and hypothermic conditions (approx. 37.5 C, 25 C, 18 C, and 7 C). Control blood flow either increased or decreased when the temperature was lowered but was quite stable at each temperature step. The amount of reactive hyperemia always decreased with hypothermia and was statistically independent of effect from the control blood flow as the temperature was lowered. Recovery from reactive hyperemia required approximately the same time for the three periods of occlusion at each temperature step. The effect of hypothermia on control blood flow appears to determine the time required for recovery from reactive hyperemia.

Effect of temperature on the allosteric transitions of rabbit skeletal muscle phosphorylase b

Biochemistry ◽  
1968 ◽  
Vol 7 (12) ◽  
pp. 4543-4556 ◽  
Author(s):  
Lewis L. Kastenschmidt ◽  
Jeannine. Kastenschmidt ◽  
Ernst. Helmreich
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Effect Of Temperature ◽  
Muscle Phosphorylase ◽  
Allosteric Transitions

scholarly journals A quantitative study of potassium channel kinetics in rat skeletal muscle from 1 to 37 degrees C.

1983 ◽  
Vol 81 (4) ◽  
pp. 485-512 ◽  
Author(s):  
K G Beam ◽  
P L Donaldson
Keyword(s):  
Skeletal Muscle ◽  
Low Temperatures ◽  
Time Course ◽  
Voltage Dependence ◽  
Potassium Currents ◽  
Effect Of Temperature ◽  
Time Axis ◽  
Rat Skeletal Muscle ◽  
Rapid Phase ◽  
Qualitative Effect

Potassium currents were measured using the three-microelectrode voltage-clamp technique in rat omohyoid muscle at temperatures from 1 to 37 degrees C. The currents were fitted according to the Hodgkin-Huxley equations as modified for K currents in frog skeletal muscle (Adrian et al., 1970a). The equations provided an approximate description of the time course of activation, the voltage dependence of the time constant of activation (tau n), and the voltage dependence of gK infinity. At higher temperatures the relationship between gK infinity and voltage was shifted in the hyperpolarizing direction. The effect of temperature on tau n was much greater in the cold than in the warm: tau n had a Q10 of nearly 6 at temperatures below 10 degrees C, but a Q10 of only approximately 2 over the range of 30-38 degrees C. The decreasing dependence of tau n on temperature was gradual and the Arrhenius plot of tau n revealed no obvious break-points. In addition to its quantitative effect on activation kinetics, temperature also had a qualitative effect. Near physiological temperatures (above approximately 25 degrees C), the current was well described by n4 kinetics. At intermediate temperatures (approximately 15-25 degrees C), the current was well described by n4 kinetics, but only if the n4 curve was translated rightward along the time axis (i.e., the current had a greater delay than could be accounted for by simple n4 kinetics). At low temperatures (below approximately 15 degrees C), n4 kinetics provided only an approximate fit whether or not the theoretical curve was translated along the time axis. In particular, currents in the cold displayed an initial rapid phase of activation followed by a much slower one. Thus, low temperatures appear to reveal steps in the gating process which are kinetically "hidden" at higher temperatures. Taken together, the effects of temperature on potassium currents in rat skeletal muscle demonstrate that the behavior of potassium channels at physiological temperatures cannot be extrapolated, either quantitatively or qualitatively, from experiments carried out in the cold.

Hyperthermia stimulates energy-proteasome-dependent protein degradation in cultured myotubes

2000 ◽  
Vol 278 (3) ◽  
pp. R749-R756 ◽  
Author(s):  
Guang-Ju Luo ◽  
Xiaoyan Sun ◽  
Per-Olof Hasselgren
Keyword(s):  
Skeletal Muscle ◽  
High Temperature ◽  
Elevated Temperature ◽  
Protein Degradation ◽  
Severe Infection ◽  
Effect Of Temperature ◽  
Maximal Effect ◽  
Mrna Levels ◽  
L6 Myotubes ◽  
Proteolytic Pathways

Previous studies suggest that elevated temperature stimulates protein degradation in skeletal muscle, but the intracellular mechanisms are not fully understood. We tested the role of different proteolytic pathways in temperature-dependent degradation of long- and short-lived proteins in cultured L6 myotubes. When cells were cultured at different temperatures from 37 to 43°C, the degradation of both classes of proteins increased, with a maximal effect noted at 41°C. The effect of high temperature was more pronounced on long-lived than on short-lived protein degradation. By using blockers of individual proteolytic pathways, we found evidence that the increased degradation of both long-lived and short-lived proteins at high temperature was independent of lysosomal and calcium-mediated mechanisms but reflected energy-proteasome-dependent degradation. mRNA levels for enzymes and other components of different proteolytic pathways were not influenced by high temperature. The results suggest that hyperthermia stimulates the degradation of muscle proteins and that this effect of temperature is regulated by similar mechanisms for short- and long-lived proteins. Elevated temperature may contribute to the catabolic response in skeletal muscle typically seen in sepsis and severe infection.

scholarly journals Products of lipid peroxidation, but not membrane susceptibility to oxidative damage, are conserved in skeletal muscle following temperature acclimation

2015 ◽  
Vol 308 (5) ◽  
pp. R439-R448 ◽  
Author(s):  
Jeffrey M. Grim ◽  
Molly C. Semones ◽  
Donald E. Kuhn ◽  
Tamas Kriska ◽  
Agnes Keszler ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Lipid Peroxidation ◽  
Thermal Effects ◽  
Total Phospholipid ◽  
Acyl Chain ◽  
Morone Saxatilis ◽  
Redox Status ◽  
Temperature Acclimation ◽  
Effect Of Temperature ◽  
Phospholipid Content

Changes in oxidative capacities and phospholipid remodeling accompany temperature acclimation in ectothermic animals. Both responses may alter redox status and membrane susceptibility to lipid peroxidation (LPO). We tested the hypothesis that phospholipid remodeling is sufficient to offset temperature-driven rates of LPO and, thus, membrane susceptibility to LPO is conserved. We also predicted that the content of LPO products is maintained over a range of physiological temperatures. To assess LPO susceptibility, rates of LPO were quantified with the fluorescent probe C11-BODIPY in mitochondria and sarcoplasmic reticulum from oxidative and glycolytic muscle of striped bass ( Morone saxatilis) acclimated to 7°C and 25°C. We also measured phospholipid compositions, contents of LPO products [i.e., individual classes of phospholipid hydroperoxides (PLOOH)], and two membrane antioxidants. Despite phospholipid headgroup and acyl chain remodeling, these alterations do not counter the effect of temperature on LPO rates (i.e., LPO rates are generally not different among acclimation groups when normalized to phospholipid content and compared at a common temperature). Although absolute levels of PLOOH are higher in muscles from cold- than warm-acclimated fish, this difference is lost when PLOOH levels are normalized to total phospholipid. Contents of vitamin E and two homologs of ubiquinone are more than four times higher in mitochondria prepared from oxidative muscle of warm- than cold-acclimated fish. Collectively, our data demonstrate that although phospholipid remodeling does not provide a means for offsetting thermal effects on rates of LPO, differences in phospholipid quantity ensure a constant proportion of LPO products with temperature variation.

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