Skip to main content
ARS Home » Plains Area » Houston, Texas » Children's Nutrition Research Center » Research » Publications at this Location » Publication #139007

Title: REGULATION OF PROTEIN SYNTHESIS IN MUSCLE AND LIVER OF FASTED AND FED SOMATOTROPIN-TREATED PIGS

Author
item BUSH, JILL - BAYLOR COLLEGE OF MED
item KIMBALL, SCOT - PENN STATE COL OF MED
item NGUYEN, HANH - BAYLOR COLLEGE OF MED
item SURYAWAN, AGUS - BAYLOR COLLEGE OF MED
item O'CONNOR, PAMELA - BAYLOR COLLEGE OF MED
item REEDS, PETER - UNIV OF ILLINOIS
item Davis, Teresa

Submitted to: Federation of American Societies for Experimental Biology Conference
Publication Type: Abstract Only
Publication Acceptance Date: 4/20/2002
Publication Date: 4/20/2002
Citation: Bush, J.A., Kimball, S.R., Nguyen, H.V., Suryawan, A., O'Connor, P.M.J., Reeds, P.J., Davis, T.A. 2002. Regulation of protein synthesis in muscle and liver of fasted and fed somatotropin-treated pigs [abstract]. Federation of American Societies for Experimental Biology Conference. Part I, 16(4):A236

Interpretive Summary: Not Necessary for an Abstract

Technical Abstract: Somatotropin (ST) minimizes protein loss during fasting and maximizes protein gain during meal absorption in pigs. Feeding increases translation initiation in growing pigs. The effect of ST on the activity of specific translation initiation factors (eIF) in the fasted and fed state has not been studied in vivo. Thus, fractional protein synthesis rates and the activation of initiation factors were determined in muscle and liver of fasted and fed growing pigs treated for 7d with ST (150 micro g/kg/d). Fed and fasted pigs (n=20) were infused for 6h with 13C-leucine. Feeding increased (p<0.05) liver and muscle protein synthesis in control and ST-treated pigs. ST increased protein synthesis in liver of fasted and fed pigs. In muscle and liver, feeding increased 4EBP1 phosphorylation, decreased association of 4EBP1 (repressor protein) with eIF4E, and increased association of eIF4E with eIF4G. ST increased 4EBP1 phosphorylation in muscle. The results suggest that modulation of the availability of eIF4E for 48S ribosomal complex formation does not account entirely for the effects of feeding and ST treatment on liver and muscle protein synthesis.