Role of G protein-coupled estrogen receptor-1 in estradiol 17β-induced alterations in protein synthesis and protein degradation rates in fused bovine satellite cell cultures

E. Kamanga-Sollo, K. J. Thornton, M. E. White, W. R. Dayton

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

In feedlot steers, estradiol-17β (E2) and combined E2 and trenbolone acetate (a testosterone analog) implants enhance rate and efficiency of muscle growth; and, consequently, these compounds are widely used as growth promoters in several countries. Treatment with E2 stimulates protein synthesis rate and suppresses protein degradation rate in fused bovine satellite cell (BSC) cultures; however, the mechanisms involved in these effects are not known with certainty. Although the genomic effects of E2 mediated through the classical estrogen receptors have been characterized, recent studies indicate that binding of E2 to the G protein-coupled estrogen receptor (GPER)-1 mediates nongenomic effects of E2 on cellular function. Our current data show that inhibition of GPER-1, matrix metalloproteinases 2 and 9 (MMP2/9), or heparin binding epidermal growth factor-like growth factor (hbEGF) suppresses E2 stimulate protein synthesis rate in cultured BSCs (P < 0.001) suggesting that all of these are required in order for E2 to stimulate protein synthesis in these cultures. In contrast, inhibition of GPER-1, MMP2/9, or hbEGF has no effect on the ability of E2 to suppress protein degradation rates in fused BSC cultures indicating that these factors are not required in order for E2 to suppress protein degradation rate in these cells. Furthermore, treatment of fused BSC cultures with E2 increased (P < 0.05) pAKT levels indicating that the pAKT pathway may play a role in E2-stimulated effects on cultured BSC. In summary, our current data show that active GPER-1, MMP2/9, and hbEGF are necessary for E2-stimulated protein synthesis but not for E2-simulated suppression of protein degradation in cultured BSC. In addition, E2 treatment increases pAKT levels in cultured BSC.

Original languageEnglish (US)
Pages (from-to)90-96
Number of pages7
JournalDomestic Animal Endocrinology
Volume58
DOIs
StatePublished - Jan 1 2017

Bibliographical note

Funding Information:
This material is based on work that is supported by the National Institute of Food and Agriculture , U.S. Department of Agriculture , under award number 2012-67015-19447 and by the Minnesota Agricultural Experiment Station .

Publisher Copyright:
© 2016 Elsevier Inc.

Keywords

  • Estrogen
  • G protein-coupled estrogen receptor-1
  • Muscle
  • Protein turnover
  • Satellite cell
  • pAKT

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