Muscular atrophy of caveolin-3–deficient mice is rescued by myostatin inhibition
J. Clin. Invest. Yutaka Ohsawa, et al. 116:2924 doi:10.1172/JCI28520 [Go to this article.]

Figure 5
Myostatin inhibition suppresses hyperphosphorylation of Smad2 and increased p21 expression in caveolin-3–deficient muscle. (A) Prodomain C terminal myostatin complex was immunoprecipitated from mouse crude skeletal muscle homogenates (top panel) or sera (middle panel) with an Ab against the myostatin C terminal peptide (α–C-peptide), then immunoblotted (IB) using a polyclonal Ab against the prodomain (α-prodomain). Recombinant myostatin prodomain is used as a control. Immunoblot analysis of sera (bottom panel) shows an excessive amount of prodomain putatively derived from the transgene in the mutant myostatin–Tg mice as well as the double-Tg mice. (B) Immunoblot analysis of total Smad2 and p-Smad2 in crude skeletal muscle homogenates from mice (left). Quantification of the p-Smad2/Smad2 ratio by densitometric analysis (right). Values are represented as fold increase with respect to wild-type mice. Data are expressed as mean ± SD (n = 5). *P < 0.05. (C) Northern blot analysis in mouse skeletal muscle for p21 and p15, which are myostatin-dependent and -independent CDK inhibitors, respectively (left). Quantification of the p21/GAPDH ratio by densitometric analysis (right). Values are represented as fold increase with respect to wild-type mice. Data are expressed as mean ± SD (n = 5). *P < 0.05.