ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2013
The compact mutation of myostatin causes a glycolytic shift in the phenotype of fast skeletal muscles.
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Two-Way Communication Between Skeletal Muscle and Myokines.Cell biochemistry and function · 2026Review
- A reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice.Glycobiology · 2025Article
- Esophageal striated muscle hypertrophy and muscle fiber type transformation in MSTN knockout pigs.Transgenic research · 2022Article
- Beyond the Big Five: Investigating Myostatin Structure, Polymorphism and Expression inFrontiers in genetics · 2019Article
- SOCE Is Important for Maintaining Sarcoplasmic Calcium Content and Release in Skeletal Muscle Fibers.Biophysical journal · 2017Article
- Skeletal muscle cellularity and glycogen distribution in the hypermuscular Compact mice.European journal of histochemistry : EJH · 2014Article
- Hypermuscular mice with mutation in the myostatin gene display altered calcium signalling.The Journal of physiology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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