The slow sarco/endoplasmic reticulum Ca2+ -ATPase declines independently of slow myosin in soleus muscle of diabetic rats

Acta Biochim Pol. 2009;56(3):487-93. Epub 2009 Sep 7.

Abstract

The sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) isoforms are normally expressed in coordination with the corresponding myosin heavy chain (MyHC) isoforms in the fibers of skeletal muscle but this coordination is often disrupted in pathological conditions. In the streptozotocin-induced diabetes of rats (stz-rats), the soleus muscle showed peripheral neuropathy and the SERCA2a level decreased in type I (slow-oxidative) fibers compared to the control muscles, whereas the expression of the corresponding slow MyHC1 did not change. No difference was found at the mRNA and protein levels of SERCA and MyHC isoforms in the whole soleus, except that the level of the SERCA2a protein specifically declined in stz-rats compared to the controls. This shows that the coordinated expression of SERCA2a and MyHC1 is disrupted at the SERCA2a protein level in the diabetic soleus. The results are in line with previous observations that regulators of the Ca-homeostasis may adapt faster to type I diabetes than the contractile elements.

MeSH terms

  • Animals
  • Diabetes Mellitus, Experimental / metabolism*
  • Immunoblotting
  • Immunohistochemistry
  • Male
  • Muscle, Skeletal / enzymology*
  • Muscle, Skeletal / metabolism*
  • Myosin Heavy Chains / genetics
  • Myosin Heavy Chains / metabolism*
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Rats
  • Rats, Wistar
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sarcoplasmic Reticulum Calcium-Transporting ATPases / genetics
  • Sarcoplasmic Reticulum Calcium-Transporting ATPases / metabolism*

Substances

  • Protein Isoforms
  • Sarcoplasmic Reticulum Calcium-Transporting ATPases
  • Myosin Heavy Chains