title: Effect of Estradiol-17beta on protein synthesis and degradation rates in fused bovine satellite cell cultures.
abstract: Although androgenic and estrogenic steroids are widely used to enhance muscle growth and increase feed efficiency in feedlot cattle, their mechanism of action is not well understood. Further, in vivo studies indicate that estradiol (E2) affects muscle protein synthesis and/or degradation, but in vitro results are inconsistent. We have examined the effects of E2 treatment on protein synthesis and degradation rates in fused bovine satellite cell (BSC) cultures. Additionally, to learn more about the mechanisms involved in E2-enhanced muscle growth, we have examined the effects of compounds that interfere with binding of E2 or insulin-like growth factor (IGF)-1 to their respective receptors on E2-induced alterations in protein synthesis and degradation rates in BSC cultures. Treatment of fused BSC cultures with E2 results in a concentration-dependent increase (P < 0.05) in protein synthesis rate and a decrease (P < 0.05) in protein degradation rate. The pure estrogen antagonist ICI 182 780 suppresses (P < 0.05) E2-induced alterations in protein synthesis and degradation in fused BSC cultures. The G-protein coupled receptor (GPR)-30 agonist G1 does not affect either synthesis or degradation rate, which establishes that GPR30 does not play a role in E2-induced alterations in protein synthesis or degradation. JB1, a competitive inhibitor of IGF-1 binding to the Type 1 insulin-like growth factor receptor (IGFR-1), suppresses (P < 0.05) E2-induced alterations in protein synthesis and degradation. In summary, our data show that E2 treatment directly alters both protein synthesis and degradation rates in fused BSC cultures via mechanisms involving both the classical estrogen receptor (ER) and IGFR-1.
authors.affiliation: Animal Growth and Development Laboratory, Department of Animal Science, University of Minnesota, St. Paul, MN.
authors.forename: E
authors.initials: E
authors.lastname: Kamanga-Sollo
authors.forename: M E
authors.initials: ME
authors.lastname: White
authors.forename: M R
authors.initials: MR
authors.lastname: Hathaway
authors.forename: W J
authors.initials: WJ
authors.lastname: Weber
authors.forename: W R
authors.initials: WR
authors.lastname: Dayton
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002455:Cell Division / Q000187:drug effects; D002459:Cell Fusion; D002478:Cells, Cultured; D004958:Estradiol / Q000031:analogs & derivatives / Q000494:pharmacology; D004965:Estrogen Antagonists / Q000494:pharmacology; D000077267:Fulvestrant; D007334:Insulin-Like Growth Factor I / Q000037:antagonists & inhibitors / Q000378:metabolism; D009124:Muscle Proteins / Q000096:biosynthesis / Q000187:drug effects* / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects*; D017526:Receptor, IGF Type 1 / Q000187:drug effects / Q000378:metabolism*; D011960:Receptors, Estrogen / Q000187:drug effects / Q000502:physiology; D043562:Receptors, G-Protein-Coupled / Q000819:agonists / Q000502:physiology; D032496:Satellite Cells, Skeletal Muscle / Q000187:drug effects / Q000378:metabolism*
chemical_list: D004965:Estrogen Antagonists; D009124:Muscle Proteins; D011960:Receptors, Estrogen; D043562:Receptors, G-Protein-Coupled; D000077267:Fulvestrant; D004958:Estradiol; D007334:Insulin-Like Growth Factor I; D017526:Receptor, IGF Type 1