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Ex Vivo Assessment of Contractility, Fatigability and Alternans in Isolated Skeletal Muscles
Published on: November 1, 2012
Difference in activation by Tris(hydroxymethyl)aminomethane of Ca,Mg-ATPase activity between young and old rat
Abstract:
Fresh weight of rat skeletal muscles (M. tibialis anterior) was decreased with age. Specific activity of myosin-ATPase in the homogenate was decreased significantly at later stages of age, but not Ca,Mg-ATPase activity. The activity of Ca,Mg-ATPase was activated by high concentration (more than 75 mM) of Tris(hydroxymethyl)aminomethane. The degree of the activation was observed to be an age-related change; the activation of Ca,Mg-ATPase activity in old rats was lower than that of young rats.
Insights
Aging reduces rat skeletal muscle weight and myosin-ATPase activity. While Ca,Mg-ATPase activity is preserved, its activation by Tris buffer decreases with age, indicating age-related functional changes.
Area of Science:
- Gerontology
- Skeletal Muscle Physiology
- Biochemistry
Background:
- Skeletal muscle mass and function decline with aging.
- Age-related changes in muscle enzyme activity, specifically ATPases, are not fully understood.
- Myosin-ATPase and Ca,Mg-ATPase are key enzymes in muscle contraction and calcium handling.
Purpose of the Study:
- To investigate age-related changes in the fresh weight of rat skeletal muscles.
- To determine the specific activity of myosin-ATPase and Ca,Mg-ATPase in aging rat skeletal muscles.
- To examine the effect of Tris(hydroxymethyl)aminomethane concentration on Ca,Mg-ATPase activity in different age groups.
Main Methods:
- Measurement of fresh weight of M. tibialis anterior in rats of varying ages.
- Assay of specific activity for myosin-ATPase and Ca,Mg-ATPase in muscle homogenates.
- Analysis of Ca,Mg-ATPase activation by high concentrations of Tris(hydroxymethyl)aminomethane.
Main Results:
- Rat skeletal muscle fresh weight significantly decreased with age.
- Specific activity of myosin-ATPase decreased significantly in older rats.
- Ca,Mg-ATPase activity remained unchanged with age, but its activation by high Tris concentrations was reduced in older rats compared to younger rats.
Conclusions:
- Aging leads to a reduction in skeletal muscle mass and myosin-ATPase activity.
- While Ca,Mg-ATPase itself is not diminished, its functional response to buffer conditions is impaired in aged rats.
- These findings suggest an age-related alteration in the regulatory mechanisms of Ca,Mg-ATPase in skeletal muscle.
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