Abstract

Akirin2 plays an important role in skeletal myogenesis. In this study, we found that porcine Akirin2 (pAkirin2) mRNA level was significantly higher in fast extensor digitorum longus (EDL) and longissimus lumborum (LL) muscles than in slow soleus (SOL) muscle of pigs. Overexpression of pAkirin2 increased the number of myosin heavy chain (MHC)-positive cells, indicating that pAkirin2 promoted myoblast differentiation. We also found that overexpression of pAkirin2 increased the mRNA expressions of MHCI and MHCIIa and decreased the mRNA expression of MHCIIb. Myocyte enhancer factor 2 (MEF2) and nuclear factor of activated T cells (NFAT) are the major downstream effectors of calcineurin. Here we also observed that the mRNA expressions of MEF2C and NFATc1 were notably elevated by pAkirin2 overexpression. Together, our data indicate that the role of pAkirin2 in modulating MHCI and MHCIIa expressions may be achieved through calcineurin/NFATc1 signaling pathway.

Highlights

  • Skeletal muscle is comprised of muscle fibers, whose characteristics affect both lean meat production and meat quality [1,2]

  • We found that pAkirin2 mRNA expression was most abundant in the extensor digitorum longus (EDL) muscle, followed by the longissimus lumborum (LL) muscle, and to a lesser extent in the SOL muscle

  • Our results suggest that the role of pAkirin2 in regulating MHCI

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Summary

Introduction

Skeletal muscle is comprised of muscle fibers, whose characteristics affect both lean meat production and meat quality [1,2]. Three main fiber types (slow oxidative type (I), fast oxiditave-glycotic type (IIa), and fast glycotic type (IIb)) can be distinguished according to their myosin ATPase stability after acid or alkali pretreatment [3]. Four MHC isoforms of mammalian skeletal muscles are codified by four genes such as slow-twitch oxidative type I (MHCI), and three fast types, namely oxidative type IIa (MHCIIa), oxido-glycolytic type IIx (MHCIIx), and glycolytic type IIb (MHCIIb) [5,6]. One of the main factors influencing meat quality, directly affects the muscle color, tenderness, and the content of intramuscular fat (IMF) in farm animals [7]

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