Time course of soleus muscle myosin expression during hindlimb suspension and recovery

Donald Thomason, R. E. Herrick, D. Surdyka, K. M. Baldwin

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Abstract

This study examined the time course of adult rodent soleus muscle myofibril and myosin isoform protein expression after 4, 8, 16, 28, and 56 days of hindlimb unweighting by tail suspension (S). The time course of soleus muscle recovery (R) was also examined after 28 days of hindlimb unweighting with an additional 4, 8, 16, and 28 days of unrestricted cage activity. During suspension, soleus muscle myofibril protein rapidly decreased from 34.3 ± 3.1 (1.96SE) mg/pair in the control (C) group to 6.9 ± 1.4 (1.96SE) mg/pair in S (t = 56 days). The calculated first-order degradation rate constant for this loss was k(d) = 0.17 days-1 [half time (t( 1/2 )) = 4.1 days]. The estimated slow myosin (SM) isoform content decreased from 13.4 ± 2.0 (1.96SE) mg/pair in C to 2.1 ± 0.2 (1.96SE) mg/pair in S (k(d) = 0.19 days-1, t( 1/2 ) = 3.6 days). The relative proportion of other myosin isoforms was increased at 28 and 56 days of suspension, reflecting an apparent de novo synthesis and the loss of SM. Recovery of contractile protein after 28 days of suspension was slower for both the myofibril protein and the SM isoform (k(d) = 0.07 days-1, t( 1/2 ) = 10 days). These data suggest that loss of weight bearing specifically affected the mechanisms of contractile protein expression reflected in soleus muscle protein degradation processes. In addition, the expression of the myosin isoforms were apparently differentially affected by the loss of weight-bearing activity.

Original languageEnglish (US)
Pages (from-to)130-137
Number of pages8
JournalJournal of applied physiology
Volume63
Issue number1
StatePublished - Jan 1 1987

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Hindlimb Suspension
Myosins
Skeletal Muscle
Protein Isoforms
Myofibrils
Contractile Proteins
Suspensions
Muscle Proteins
Weight-Bearing
Hindlimb
Proteolysis
Rodentia
Control Groups
Proteins

All Science Journal Classification (ASJC) codes

  • Physiology
  • Physiology (medical)

Cite this

Time course of soleus muscle myosin expression during hindlimb suspension and recovery. / Thomason, Donald; Herrick, R. E.; Surdyka, D.; Baldwin, K. M.

In: Journal of applied physiology, Vol. 63, No. 1, 01.01.1987, p. 130-137.

Research output: Contribution to journalArticle

Thomason, Donald ; Herrick, R. E. ; Surdyka, D. ; Baldwin, K. M. / Time course of soleus muscle myosin expression during hindlimb suspension and recovery. In: Journal of applied physiology. 1987 ; Vol. 63, No. 1. pp. 130-137.
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abstract = "This study examined the time course of adult rodent soleus muscle myofibril and myosin isoform protein expression after 4, 8, 16, 28, and 56 days of hindlimb unweighting by tail suspension (S). The time course of soleus muscle recovery (R) was also examined after 28 days of hindlimb unweighting with an additional 4, 8, 16, and 28 days of unrestricted cage activity. During suspension, soleus muscle myofibril protein rapidly decreased from 34.3 ± 3.1 (1.96SE) mg/pair in the control (C) group to 6.9 ± 1.4 (1.96SE) mg/pair in S (t = 56 days). The calculated first-order degradation rate constant for this loss was k(d) = 0.17 days-1 [half time (t( 1/2 )) = 4.1 days]. The estimated slow myosin (SM) isoform content decreased from 13.4 ± 2.0 (1.96SE) mg/pair in C to 2.1 ± 0.2 (1.96SE) mg/pair in S (k(d) = 0.19 days-1, t( 1/2 ) = 3.6 days). The relative proportion of other myosin isoforms was increased at 28 and 56 days of suspension, reflecting an apparent de novo synthesis and the loss of SM. Recovery of contractile protein after 28 days of suspension was slower for both the myofibril protein and the SM isoform (k(d) = 0.07 days-1, t( 1/2 ) = 10 days). These data suggest that loss of weight bearing specifically affected the mechanisms of contractile protein expression reflected in soleus muscle protein degradation processes. In addition, the expression of the myosin isoforms were apparently differentially affected by the loss of weight-bearing activity.",
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