Molecular and functional characterization of glycogen synthase in the porcine satellite cells under insulin treatment.

Glycogen synthase (GS) catalyzes the key step of glycogen synthesis and plays an important role in glycogen metabolism in liver and muscle. In this study, we cloned the cDNA and promoter sequences of porcine glycogen synthesis genes (GYS1 and GYS2). Expression analysis revealed that porcine GYS1 was highly expressed in the skeletal muscle and heart. GYS2 was expressed specifically in liver and subcutaneous adipose tissue. The expression level of GYS1 was up-regulated from proliferation to differentiation in the porcine satellite cells, and insulin did not significantly affect the transcription of GYS1. Insulin stimulated 72-h-differentiated satellite cells as indicated by decrease in phosphorylation of GS, but did not affect GYS1 transcription and total GS protein level, suggesting that the effect of insulin is primarily mediated via posttranscriptional control rather than regulated at the transcriptional level. Four single-nucleotide polymorphisms (SNPs) were detected in the promoter and cDNA sequences of porcine GYS1. Association analyses revealed that the GYS1 Hin6I and MvaI polymorphisms both had significant associations (P < 0.05) with pH of M. longissimus dorsi (pHLD), M. biceps femoris (pHBF) and M. semipinalis capitis (pHSC) at 45 min postmortem. These results provide useful information for further investigation on the function of glycogen synthase in porcine skeletal muscle.