Fiber-specific regulation of Ca(2+)-ATPase isoform expression by thyroid hormone in rat skeletal muscle

1996 ◽  
Vol 271 (6) ◽  
pp. C1908-C1919 ◽  
Author(s):  
C. G. van der Linden ◽  
W. S. Simonides ◽  
A. Muller ◽  
W. J. van der Laarse ◽  
J. L. Vermeulen ◽  
...  

We studied the effect of thyroid hormone (3,5,3'-triiodo-L-thyronine, T3) on the expression of sarcoplasmic reticulum (SR) fast- and slow-type Ca(2+)-ATPase isoforms, SERCA1 and SERCA2a, respectively, and total SR Ca(2+)-ATPase activity in rat skeletal muscle. Cross sections and homogenates of soleus and extensor digitorum longus muscles from hypo-, eu-, and hyperthyroid rats were examined, and expression of Ca(2+)-ATPase isoforms in individual fibers was compared with expression of fast (MHC II) and slow (MHC I) myosin heavy chain isoforms. In both muscles, T3 induced a coordinated and full conversion to a fast-twitch phenotype in one-half of the fibers that were slow twitch in the absence of T3. The conversion was partial in the other one-half of the fibers, giving rise to a mixed phenotype. The stimulation by T3 of total SERCA expression in all fibers was reflected by increased SR Ca(2+)-ATPase activity. The time course of the T3-induced changes of SERCA isoform expression was examined 1-14 days after the start of daily T3 treatment of euthyroid rats. SERCA1 expression was stimulated by T3 at a pretranslational level in all fibers. SERCA2a mRNA expression was transiently stimulated and disappeared in a subset of fibers. In these fibers SR Ca(2+)-ATPase activity was high because of high SERCA1 protein levels. These data suggest that the ultimate downregulation of SERCA2a expression, which is always associated with high SR Ca(2+)-ATPase activities, occurs at a pretranslational level.


1987 ◽  
Vol 63 (5) ◽  
pp. 2111-2121 ◽  
Author(s):  
R. W. Tsika ◽  
R. E. Herrick ◽  
K. M. Baldwin

The purpose of this study was to ascertain the time course of change during both compensatory growth (hypertrophy) and subsequent growth regression on myosin isoform expression in rodent fast-twitch plantaris muscle in response to functional overload (induced by removal of synergists). Peak hypertrophy of the plantaris muscle (92%) occurred after 9 wk of overload. After 7 wk of overload regression (induced by a model of hindlimb unweighting), muscle weight returned to within 30% of control values. Myofibril protein content (mg/g muscle) remained relatively constant throughout the overload period but became significantly depressed relative to control values after 7 wk of regression. However, when expressed on a per muscle basis (mg/muscle) no differences existed at this time point (t = 7 wk regression). The distribution of native myosin isoforms in the myofibril protein pool of the overloaded plantaris muscle reflected a progressive increase (23% at t = 9 wk; P less than 0.001) in the relative proportion of slow myosin (Sm). This change was also accompanied by increases in intermediate myosin (Im) as well as the repression of the fast myosin one (Fm1) isoform (P less than 0.001). These shifts in Sm and Fm1 isoform expression were gradually reversed during the regression period, whereas Im remained elevated relative to control values. These adaptive changes in myosin isoform expression during both hypertrophy and regression were further supported by concomitant shifts in both myosin adenosinetriphosphatase (ATPase) activity (decreased during overload) and slow myosin light chain (SLC) expression. However, during regression the changes in myosin isoform expression and myosin ATPase were not as synchronous as they were during overload. Estimation of the mixed myosin heavy chain (MHC) half-life (t 1/2), using a linear model that assumes zero-order synthesis and first-order degradation kinetics, revealed t 1/2 values of approximately 19 and 10 days for the overload and regression periods, respectively. Collectively these data suggest that 1) skeletal muscle myosin isoforms and corresponding ATPase activity are in a dynamic state of change, although not completely synchronous, in response to altered muscle stress, and 2) the kinetics of change in the mixed MHC protein pool are slower during compensatory growth compared with regression of growth.



1993 ◽  
Vol 1153 (2) ◽  
pp. 184-190 ◽  
Author(s):  
Pamela R. Warnick ◽  
Paul J. Davis ◽  
Faith B. Davis ◽  
Vivian Cody ◽  
Galindo Jose ◽  
...  


Endocrinology ◽  
1991 ◽  
Vol 129 (1) ◽  
pp. 455-464 ◽  
Author(s):  
STEVEN P. WEINSTEIN ◽  
JULIE WATTS ◽  
RICHARD S. HABER


2016 ◽  
Vol 63 (8) ◽  
pp. 727-738 ◽  
Author(s):  
Ronny Lesmana ◽  
Toshiharu Iwasaki ◽  
Yuki Iizuka ◽  
Izuki Amano ◽  
Noriaki Shimokawa ◽  
...  


2010 ◽  
Vol 59 (4) ◽  
pp. 337-348 ◽  
Author(s):  
KEITA KANZAKI ◽  
MAI KURATANI ◽  
SATOSHI MATSUNAGA ◽  
TAKAAKI MISHIMA ◽  
SACHIO USUI ◽  
...  


2003 ◽  
Vol 35 (Supplement 1) ◽  
pp. S95
Author(s):  
S L. Lo Giudice ◽  
S F. Fraser ◽  
J A. Hawley




1998 ◽  
Vol 8 (2) ◽  
pp. 105-112 ◽  
Author(s):  
Jon N. Swift ◽  
James P. Kehrer ◽  
K. Stephen Seiler ◽  
Joseph W. Starnes

The purpose of this study was to determine whether submaximal exercise significantly changes the concentration of vitamin E (αToc) in rat liver and skeletal muscle and to establish a time course for the return to basal levels. Male Sprague-Dawley rats, age 8 to 10 weeks, were randomly divided into sedentary control (Con) (n = 7) and exercise n = 17) groups. Exercised animals ran 100 min on a motorized treadmill at approximately 70% VO2max for 3 consecutive days. They were then sacrificed immediately postexercise (0Post), 24 hr post (24Post), or 72 hr post (72Post). The gastrocnemius, red vastus lateralis (RV), white vastus lateralis (WV), and liver were excised and analyzed for αToc concentration by high-performance liquid chromolography utilizing electrochemical detection. We found that after 3 consecutive days of exercise, αToc was reduced in RV and WV at 0Post and 24Post but returned to control values by 72Post. Liver αToc content was not changed at OPost but was significantly reduced at 24 Post and 72 Post. No significant changes in αToc were observed in the gastrocnemius in response to exercise. The data indicate that following an exercise-related decrease, skeletal muscle vitamin E concentration requires more than 24 hr to return to the preexercise concentration, and that the replenishment process may involve redistribution of vitamin E from liver to muscle.



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