Journal of Muscle Research & Cell Motility

, Volume 21, Issue 6, pp 551–563 | Cite as

Myostatin levels in regenerating rat muscles and in myogenic cell cultures

  • Luca Mendler
  • Ernö Zádor
  • Mark Ver Heyen
  • László Dux
  • Frank Wuytack


Myostatin is a newly described member of the TGF-β superfamily acting as a secreted negative regulator of skeletal muscle mass in several species, but whose mode of action remains largely unknown. In the present work, we followed the myostatin mRNA and protein levels in rat soleus and extensor digitorum longus (EDL) muscles regenerating in vivo from notexin-induced necrosis, and the myostatin transcript levels in two different in vitro myogenic differentiation models: i.e. in mouse BC3H1 and C2C12 cultured cells. The in vivo regenerating rat skeletal muscles showed a characteristic time-dependent expression of myostatin mRNA. After notexin injection, the transcript levels dropped below the detection limit on day 1 in soleus and close to the detection limit on day 3 in EDL, then increased to a maximum on day 7 in soleus and after 28 days finally reached the control values in both types of muscles. In contrast, the myostatin protein levels increased dramatically on the first days of regeneration in both muscles, i.e. at the time when its transcript level was low. Later on the myostatin protein level gradually declined to normal in soleus while in EDL it stayed high some days longer and decreased to normal on days 21–28. In vitro proliferating myoblasts produced low level of myostatin mRNA, which increased upon induction of differentiation suggesting that functional innervation is no prerequisite for myostatin expression. Myostatin production in vitro seems not to be dependent on myocyte fusion either, since it is observed in differentiated BC3H1 cells, which are defective in myofiber formation.


Extensor Digitorum Longus Skeletal Muscle Mass Myogenic Differentiation Myogenic Cell Proliferate Myoblast 


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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Luca Mendler
    • 1
  • Ernö Zádor
    • 1
  • Mark Ver Heyen
    • 2
  • László Dux
    • 1
  • Frank Wuytack
    • 2
  1. 1.Institute of Biochemistry, Faculty of MedicineUniversity of SzegedSzegedHungary
  2. 2.Laboratorium voor FysiologieKatholieke Universiteit LeuvenLeuvenBelgium

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