Journal of Muscle Research & Cell Motility

, Volume 22, Issue 8, pp 627–633

Content and localization of myostatin in mouse skeletal muscles during aging, mechanical unloading and reloading


  • Shigeo Kawada
    • Department of Life Sciences, Graduate School of Arts and SciencesThe University of Tokyo
  • Chikashi Tachi
    • Laboratory of Developmental and Reproductive Biotechnology, Department of Animal Resource Sciences, School of Veterinary Medicine and Life SciencesAzabu University
  • Naokata Ishii
    • Department of Life Sciences, Graduate School of Arts and SciencesThe University of Tokyo

DOI: 10.1023/A:1016366409691

Cite this article as:
Kawada, S., Tachi, C. & Ishii, N. J Muscle Res Cell Motil (2001) 22: 627. doi:10.1023/A:1016366409691


Changes in myostatin content and localization in mouse skeletal muscles were investigated during aging, hindlimb suspension (HS) and reloading after HS. During aging, the content of myostatin among solubilized proteins in gastrocnemius and plantaris muscles (Gast/Plant) was initially low and increased until their wet weight/body weight ratio reached a peak. It remained unchanged with further aging, although gradual atrophy of the muscles was seen to occur. Also, the myostatin content did not change significantly during HS (up to 14 days) in both Gast/Plant and soleus muscles, though the muscles showed morphological signs of atrophy. However, reloading for 2 days after a 14-day HS caused significant decreases in the myostatin content in both of these muscles. Immunohistochemical observations showed the sarcoplasmic existence of myostatin, the amount of which appeared to decrease after reloading. The results suggest that myostatin plays a part in the processes of muscular growth and loading-induced hypertrophy, but is not involved in either aging-related or unloading-induced muscular atrophy.

Copyright information

© Kluwer Academic Publishers 2001