scholarly journals Dual role of thyroid hormones in rat soleus muscle MyHC isoform expression

2007 ◽  
pp. 833-836
Author(s):  
A Vadászová-Soukup ◽  
T Soukup
Keyword(s):  
Thyroid Hormones ◽  
Soleus Muscle ◽  
Mrna Level ◽  
Protein Isoforms ◽  
Opposite Pattern ◽  
Mrna Transcripts ◽  
Speed Up ◽  
Rat Soleus Muscle ◽  
Slow Myhc ◽  
Altered Thyroid

We have analyzed the influence of altered thyroid hormone levels on changes of MyHC protein isoforms and their mRNA transcripts in the soleus muscle of 2-, 4- and 7-month-old euthyroid (EU), hypothyroid (HY) and hyperthyroid (TH) female inbred Lewis strain rats (methimazole and T3 treatment started 3 to 4 weeks after birth). We have found that the content of the dominant MyHC 1 isoform gradually increased in the EU rats and that this increase was more progressive in the HY rats at all three stages. On the other hand, in the TH rats the content of MyHC 1 isoform was the highest in the 2-month-old rats and it decreased with an increasing length of T3 treatment. The content of the minor 2a MyHC isoform followed the opposite pattern. In contrast to the protein isoforms, the MyHC mRNA transcripts remained at similar levels. Nevertheless, in general, the MyHC 1 mRNA level was decreased and MyHC 2a transcript increased in the TH rats, while the opposite changes occurred in the HY rats. Our results thus suggest that in the rat soleus muscle, both increased and decreased levels of thyroid hormones speed up the formation of an adult slow phenotype which is demonstrated by the precocious appearance of the slow MyHC 1 isoform, but opposite to the hypothyroid status, a longer T3 application promotes the expression of the faster MyHC 2a isoform.

scholarly journals Changes in myosin heavy chain mRNA and protein isoforms in single fibers of unloaded rat soleus muscle

FEBS Letters ◽  
1999 ◽  
Vol 463 (1-2) ◽  
pp. 15-18 ◽  
Author(s):  
Laurence Stevens ◽  
Bärbel Gohlsch ◽  
Yvonne Mounier ◽  
Dirk Pette
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Protein Isoforms ◽  
Single Fibers ◽  
Rat Soleus Muscle

Time course of the T3- and T4-induced increase in rat soleus muscle mitochondria

1979 ◽  
Vol 236 (3) ◽  
pp. C132-C138 ◽  
Author(s):  
W. W. Winder
Keyword(s):  
Cytochrome C ◽  
Thyroid Hormones ◽  
Soleus Muscle ◽  
Time Course ◽  
Citrate Synthase ◽  
Creatine Phosphate ◽  
Simultaneous Treatment ◽  
Muscle Mitochondria ◽  
Rat Soleus Muscle ◽  
Motor Nerves

Citrate synthase and cytochrome c increase in soleus muscle of rats in response to excess thyroid hormones. The half times of the increase in the levels of citrate synthase and cytochrome c in soleus muscle during induction are greater than the half times of the decline in enzyme levels after cessation of treatment (15 days vs. 7 days for citrate synthase). Denervation of the soleus does not prevent the increase in citrate synthase in response to thyrotoxicosis. This provides evidence that thyroid hormones affect the muscle directly and not via the motor nerves. ATP concentration is reduced in liver, but not in soleus muscle in response to thyrotoxicosis. Creatine phosphate is not significantly altered in soleus muscle. Cyclic AMP is slightly lower in thyrotoxic soleus muscle. Simultaneous treatment with thyroid hormones and propranolol does not affect the increase in citrate synthase in response to excess thyroid hormones. It is concluded that the increase in muscle mitochondria associated with thyrotoxicosis is not mediated via the nervous system or by a cAMP-regulated process.

Expression of the sarco/endoplasmic reticulum Ca2+-transport ATPase protein isoforms during regeneration from notexin-induced necrosis of rat soleus muscle

1998 ◽  
Vol 100 (4) ◽  
pp. 355-369 ◽  
Author(s):  
Ernô Zádor ◽  
Gerda Szakonyi ◽  
Gábor Rácz ◽  
Luca Mendler ◽  
Mark Ver Heyen ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Soleus Muscle ◽  
Protein Isoforms ◽  
Transport Atpase ◽  
Rat Soleus Muscle

scholarly journals HDAC4 Is Indispensable for Reduced Slow Myosin Expression at the Early Stage of Hindlimb Unloading in Rat Soleus Muscle

2021 ◽  
Vol 14 (11) ◽  
pp. 1167
Author(s):  
Inna I. Paramonova ◽  
Natalia A. Vilchinskaya ◽  
Boris S. Shenkman
Keyword(s):  
Mrna Expression ◽  
Soleus Muscle ◽  
Early Stage ◽  
Contractile Activity ◽  
Hindlimb Unloading ◽  
Hindlimb Suspension ◽  
Nuclear Accumulation ◽  
Myhc Isoforms ◽  
Rat Soleus Muscle ◽  
Slow Myhc

It is well known that reduced contractile activity of the main postural soleus muscle during long-term bedrest, immobilization, hindlimb unloading, and space flight leads to increased expression of fast isoforms and decreased expression of the slow isoform of myosin heavy chain (MyHC). The signaling cascade such as HDAC4/MEF2-D pathway is well-known to take part in regulating MyHC I gene expression. Earlier, we found a significant increase of HDAC4 in myonuclei due to AMPK dephosphorylation during 24 h of hindlimb unloading via hindlimb suspension (HU) and it had a significant impact on the expression of MyHC isoforms in rat soleus causing a decrease in MyHC I(β) pre-mRNA and mRNA expression as well as MyHC IIa mRNA expression. We hypothesized that dephosphorylated HDAC4 translocates into the nuclei and can lead to a reduced expression of slow MyHC. To test this hypothesis, Wistar rats were treated with HDAC4 inhibitor (Tasquinimod) for 7 days before HU as well as during 24 h of HU. We discovered that Tasquinimod treatment prevented a decrease in pre-mRNA expression of MyHC I. Furthermore, 24 h of hindlimb suspension resulted in HDAC4 nuclear accumulation of rat soleus but Tasquinimod pretreatment prevented this accumulation. The results of the study indicate that HDAC4 after 24 h of HU had a significant impact on the precursor MyHC I mRNA expression in rat soleus.

Time-dependent changes in myosin heavy chain mRNA and protein isoforms in unloaded soleus muscle of rat

1999 ◽  
Vol 277 (6) ◽  
pp. C1044-C1049 ◽  
Author(s):  
Laurence Stevens ◽  
Karim R. Sultan ◽  
Heidemarie Peuker ◽  
Bärbel Gohlsch ◽  
Yvonne Mounier ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Soleus Muscle ◽  
Heavy Chain ◽  
Time Course ◽  
Mrna Level ◽  
Protein Isoforms ◽  
Time Dependent ◽  
Hindlimb Suspension ◽  
Intermediate Step ◽  
Whole Muscle

Time-dependent changes in myosin heavy chain (MHC) isoform expression were investigated in rat soleus muscle unloaded by hindlimb suspension. Changes at the mRNA level were measured by RT-PCR and correlated with changes in the pattern of MHC protein isoforms. Protein analyses of whole muscle revealed that MHCI decreased after 7 days, when MHCIIa had increased, reaching a transient maximum by 15 days. Longer periods led to inductions and progressive increases of MHCIId(x) and MHCIIb. mRNA analyses of whole muscle showed that MHCIId(x) displayed the steepest increase after 4 days and continued to rise until 28 days, the longest time period investigated. MHCIIb mRNA followed a similar time course, although at lower levels. MHCIα mRNA, present at extremely low levels in control soleus, peaked after 4 days, stayed elevated until 15 days, and then decayed. Immunohistochemistry of 15-day unloaded muscles revealed that MHCIα was present in muscle spindles but at low amounts also in extrafusal fibers. The slow-to-fast transitions thus seem to proceed in the order MHCIβ → MHCIIa → MHCIId(x) → MHCIIb. Our findings indicate that MHCIα is transiently upregulated in some fibers as an intermediate step during the transition from MHCIβ to MHCIIa.

In vitro autoregulation of glucose utilization in rat soleus muscle

Diabetes ◽  
1987 ◽  
Vol 36 (9) ◽  
pp. 1041-1046 ◽  
Author(s):  
S. Sasson ◽  
D. Edelson ◽  
E. Cerasi
Keyword(s):  
Soleus Muscle ◽  
Glucose Utilization ◽  
Rat Soleus Muscle
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