ArticleMolecular and cellular biochemistry2012
Molecular and functional characterization of glycogen synthase in the porcine satellite cells under insulin treatment.
Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 16 citations in OpenAlex.
- GSK3β inhibition attenuates LPS-induced IL-6 expression in porcine adipocytes.Scientific reports · 2018Article
- Transcriptional regulation of pig GYS1 gene by glycogen synthase kinase 3β (GSK3β).Molecular and cellular biochemistry · 2017Article
- Identification of candidate genes associated with porcine meat color traits by genome-wide transcriptome analysis.Scientific reports · 2016Article
- Identification of porcine glycogen synthase kinase 3α (GSK-3α) gene and its association with carcass traits.Molecular and cellular biochemistry · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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.
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