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High‐Energy Phosphates in Smooth Muscle

Thomas M. Butler, Robert E. Davies

10.1002/cphy.cp020210

Source: Supplement 7: Handbook of Physiology, The Cardiovascular System, Vascular Smooth Muscle

Originally published: 1980

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 High‐Energy Phosphate Contents
1.1 Variability in Reported Results
1.2 Comparison to Skeletal Muscle
1.3 ADP and Actin Contents
2 Energy Input During Muscle Contraction
2.1 ATP as the Immediate Energy Source
2.2 Recovery Reactions
3 High‐Energy Phosphates and Contraction
3.1 Validity of Energetics Experiments
3.2 Historical Review of Smooth Muscle Energetics
4 Chemical Energetics Studies on a Well‐Defined Smooth Muscle Preparation
4.1 Chemical Contents of Resting Muscle
4.2 Treatment to Stop Glycolysis and Oxidative Phosphorylation
4.3 ATP and Phosphocreatine Changes During an Isometric Tetanus
4.4 Absence of a Creatine Kinase Equilibrium
4.5 Average Rate of Energy Usage During Isometric Tetani
4.6 Energetics of Isometric Force Development and Force Maintenance
4.7 Energy Usage During Relaxation
5 Rigor
5.1 Rigor in Skeletal Muscle
5.2 Rigor in Smooth Muscle
Figure 1. Figure 1.

Phosphocreatine: total creatine contents of unstimulated rabbit taenia coli as a function of time after rewarming to 18°C. Muscles were initially treated for 30 min at 5°C in an iodoacetate (0.5 mM), fluoroacetate (5.0 mM), glucose‐free Krebs solution gassed with 95% N2 and 5% CO2. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23
Figure 2. Figure 2.

Adenosine triphosphate and phosphocreatine breakdown during isometric tetani of different durations in the rabbit taenia coli at 18°C. Muscle length is 83% of muscle length at which maximum active isometric tension is observed. (•) ΔPCr; (○), ΔATP. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23
Figure 3. Figure 3.

Comparison of observed changes in PCr and ATP as a function of total high‐energy phosphate usage and those changes expected if the myokinase and creatine kinase reactions remain near equilibrium. Solid lines show expected changes in ATP and PCr and are calculated using the constants given by McGilvery and Murray 73, which assume that the creatine kinase and myokinase were in equilibrium, that all PCr and ATP measured was free, and that 98% of initial ADP present was bound. Total high‐energy phosphate usage was calculated as ΔPCr/Crtot + ΔATP/Crtot ‐ ΔAMP/Crtot. (•), ΔPCr; (○), ΔATP. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23
Figure 4. Figure 4.

Comparison of rates of force development and associated energy usage in the frog sartorius muscle at 0°C and rabbit taenia coli at 18°C. Note differences in time scales. (X), total high‐energy phosphate utilization for rabbit taenia coli at 18°C; (•), total high‐energy phosphate utilization for frog sartorius muscle at 0°C. Mean ± SE.

From Butler, Davies, et al. 22


Figure 1.

Phosphocreatine: total creatine contents of unstimulated rabbit taenia coli as a function of time after rewarming to 18°C. Muscles were initially treated for 30 min at 5°C in an iodoacetate (0.5 mM), fluoroacetate (5.0 mM), glucose‐free Krebs solution gassed with 95% N2 and 5% CO2. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23


Figure 2.

Adenosine triphosphate and phosphocreatine breakdown during isometric tetani of different durations in the rabbit taenia coli at 18°C. Muscle length is 83% of muscle length at which maximum active isometric tension is observed. (•) ΔPCr; (○), ΔATP. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23


Figure 3.

Comparison of observed changes in PCr and ATP as a function of total high‐energy phosphate usage and those changes expected if the myokinase and creatine kinase reactions remain near equilibrium. Solid lines show expected changes in ATP and PCr and are calculated using the constants given by McGilvery and Murray 73, which assume that the creatine kinase and myokinase were in equilibrium, that all PCr and ATP measured was free, and that 98% of initial ADP present was bound. Total high‐energy phosphate usage was calculated as ΔPCr/Crtot + ΔATP/Crtot ‐ ΔAMP/Crtot. (•), ΔPCr; (○), ΔATP. Ct, total creatine. Mean ± SE.

From Butler, Davies, et al. 23


Figure 4.

Comparison of rates of force development and associated energy usage in the frog sartorius muscle at 0°C and rabbit taenia coli at 18°C. Note differences in time scales. (X), total high‐energy phosphate utilization for rabbit taenia coli at 18°C; (•), total high‐energy phosphate utilization for frog sartorius muscle at 0°C. Mean ± SE.

From Butler, Davies, et al. 22
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Article Title: High‐Energy Phosphates in Smooth Muscle
 

How to Cite

Thomas M. Butler, Robert E. Davies. High‐Energy Phosphates in Smooth Muscle. Compr Physiol 2011, Supplement 7: Handbook of Physiology, The Cardiovascular System, Vascular Smooth Muscle: 237-252. First published in print 1980. doi: 10.1002/cphy.cp020210