title: Initiation and elongation steps of mRNA translation are involved in the increase in milk protein yield caused by growth hormone administration during lactation.
abstract: The underlying molecular mechanisms that control milk yield and milk protein yield in domestic animals are not completely understood. In this study, the galactopoietic response to exogenous growth hormone (GH) was used as an experimental model to investigate the role of translation initiation and elongation in the regulation of milk protein synthesis in the mammary gland. A slow-release formula of commercially available GH was administered via a single subcutaneous injection to 4 lactating cows (GH group). A further 4 cows were given a single subcutaneous injection of saline (control group). Changes in mRNA transcript level and protein phosphorylation status of key members of the mammalian target of rapamycin (mTOR) pathway were assessed in mammary gland tissues of these animals using quantitative real-time PCR and Western blotting. The GH treatment enhanced the phosphorylation of ribosomal protein S6 and increased the protein abundance of eukaryotic initiation factor 4E (eIF4E) and eukaryotic elongation factor 2 (eEF2) proteins in the mammary gland of GH-treated animals. These results indicate a link between milk protein synthesis and the regulation of mRNA translation. The GH treatment did not change mRNA abundance of ribosomal protein S6, eIF4E, and eEF2, nor did it change the mRNA (mTOR, eEF2 kinase) or protein abundance of eEF2 kinase. These results demonstrate that GH administration changes mRNA translation initiation and elongation possibly via the mTOR pathway (suggested by the increased levels of ribosomal protein S6 phosphorylation), indicating that the mTOR pathway might be a potential control point in the regulation of milk protein synthesis in the mammary gland.
authors.affiliation: Food, Metabolism and Microbiology Section, Food and Textiles Group, AgResearch Grasslands, Tennent Drive, Palmerston North 4442, New Zealand.
authors.forename: A A
authors.initials: AA
authors.lastname: Hayashi
authors.forename: K
authors.initials: K
authors.lastname: Nones
authors.forename: N C
authors.initials: NC
authors.lastname: Roy
authors.forename: W C
authors.initials: WC
authors.lastname: McNabb
authors.forename: D S
authors.initials: DS
authors.lastname: Mackenzie
authors.forename: D
authors.initials: D
authors.lastname: Pacheco
authors.forename: S
authors.initials: S
authors.lastname: McCoard
mesh_terms: D000818:Animals; D002417:Cattle / Q000378:metabolism / Q000502:physiology*; D054736:Elongation Factor 2 Kinase / Q000378:metabolism; D015852:Eukaryotic Initiation Factor-2 / Q000378:metabolism; D005260:Female; D013006:Growth Hormone / Q000008:administration & dosage / Q000494:pharmacology*; D007774:Lactation / Q000187:drug effects*; D008321:Mammary Glands, Animal / Q000187:drug effects / Q000378:metabolism; D008892:Milk / Q000737:chemistry / Q000378:metabolism; D008894:Milk Proteins / Q000032:analysis*; D010445:Peptide Elongation Factors / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D014176:Protein Biosynthesis / Q000187:drug effects*; D011494:Protein Kinases / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D038601:Ribosomal Protein S6 / Q000378:metabolism; D058570:TOR Serine-Threonine Kinases
chemical_list: D015852:Eukaryotic Initiation Factor-2; D008894:Milk Proteins; D010445:Peptide Elongation Factors; D012333:RNA, Messenger; D038601:Ribosomal Protein S6; D013006:Growth Hormone; D011494:Protein Kinases; D058570:TOR Serine-Threonine Kinases; D054736:Elongation Factor 2 Kinase