Figure 1
From: Rbm24 displays dynamic functions required for myogenic differentiation during muscle regeneration
Rbm24 expression in mouse adult muscles. (a,b) Analyses by qRT-PCR of Rbm24 (a) and myogenin (b) expression in different skeletal muscle types. Dia diaphragm, VL vastus lateralis, Sol soleus, Gas gastrocnemius, TA tibialis anterior, Mas masseter. The expression level of Rbm24 or myogenin in the diaphragm is set to 1 as a reference. Data are the mean ± s.e.m. from three independent experiments. ANOVA F (df 5.22) = 6.333, p < 0.001 for Rbm24; ANOVA F (df 5.22) = 10.55, p < 0.0001 for myogenin; *p < 0.05 by Tukey’s HSD test. Note the higher levels of Rbm24 and myogenin expression in the slow-twitch soleus muscle compared to the five other muscles enriched in fast-twitch myofibers. (c) Linear correlation between Rbm24 and myogenin expression in different muscles. R2 = 0.6527. (d,e) Double immunostaining on cryosections of soleus (Sol) and gastrocnemius (Gas) muscles shows Rbm24 nuclear localization in type I and type IIa myofibers, as well as in other fiber types devoid of MyHC-I or MyHC-IIa staining in the gastrocnemius. Note that more intense Rbm24 nuclear staining is present in the soleus muscle. (f–h) Immunolocalization of Rbm24 in the myonucleus of tibialis anterior muscle, as visualized by counterstaining with DAPI. (i–n) Double immunofluorescence staining of Rbm24 and dystrophin (Dys) or laminin (Lam) on cryosections of tibialis anterior muscle shows the localization of Rbm24 protein at the periphery of myofibers, inside the dystrophin- and laminin-associated muscle cell membrane (arrows). Note the absence of Rbm24 staining in nuclei outside the sarcolemma. Scale bars: 10 µm.
