| First Author | Baán JA | Year | 2013 |
| Journal | J Histochem Cytochem | Volume | 61 |
| Issue | 12 | Pages | 889-900 |
| PubMed ID | 23979839 | Mgi Jnum | J:214501 |
| Mgi Id | MGI:5603049 | Doi | 10.1369/0022155413503661 |
| Citation | Baan JA, et al. (2013) The compact mutation of myostatin causes a glycolytic shift in the phenotype of fast skeletal muscles. J Histochem Cytochem 61(12):889-900 |
| abstractText | Myostatin is an important negative regulator of skeletal muscle growth. The hypermuscular Compact (Cmpt) mice carry a 12-bp natural mutation in the myostatin propeptide, with additional modifier genes being responsible for the phenotype. Muscle cellularity of the fast-type tibialis anterior (TA) and extensor digitorum longus (EDL) as well as the mixed-type soleus (SOL) muscles of Cmpt and wild-type mice was examined by immunohistochemical staining of the myosin heavy chain (MHC) proteins. In addition, transcript levels of MHC isoforms were quantified by qPCR. Based on our results, all investigated muscles of Cmpt mice were significantly larger compared with that of wild-type mice, as characterized by fiber hyperplasia of different grades. Fiber hypertrophy was not present in TA; however, EDL muscles showed specific IIB fiber hypertrophy while the (I and IIA) fibers of SOL muscles were generally hypertrophied. Both the fast TA and EDL muscles of Cmpt mice contained significantly more glycolytic IIB fibers accompanied by a decreased number of IIX and IIA fibers; however, this was not the case for SOL muscles. In summary, despite the variances found in muscle cellularity between the different myostatin mutant mice, similar glycolytic shifts were observed in Cmpt fast muscles as in muscles from myostatin knockout mice. |
