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

• Published in: Journal of muscle research and cell motility 2001-01, Vol.22 (8), p.627-633
• Main Authors: Kawada, S, Tachi, C, Ishii, N
• Format: Article
• Language: English
• Subjects: Aging - metabolism; Animals; Hindlimb Suspension - physiology; Immunohistochemistry; Male; Mice; Mice, Inbred C57BL; Muscle, Skeletal - chemistry; Muscle, Skeletal - physiology; Muscular Atrophy - physiopathology; Muscular system; Myostatin; Proteins; Space life sciences; Transforming Growth Factor beta - analysis; Transforming Growth Factor beta - metabolism; Weight-Bearing - physiology
• ISSN: 0142-4319; 1573-2657
• 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.