Skip to main content
ARS Home » Plains Area » Houston, Texas » Children's Nutrition Research Center » Research » Publications at this Location » Publication #152891

Title: GLUCOSE CONTRIBUTES TO THE REGULATION OF POSTPRANDIAL PROTEIN SYNTHESIS IN NEONATES

Author
item O'CONNOR, PAMELA - BAYLOR COLLEGE MED
item KIMBALL, SCOT - PENN STATE COLLEGE MED
item ORELLANA, RENAN - BAYLOR COLLEGE MED
item BUSH, JILL - BAYLOR COLLEGE MED
item SURYAWAN, AGUS - BAYLOR COLLEGE MED
item NGUYEN, HANH - BAYLOR COLLEGE MED
item JEFFERSON, LEONARD - PENN STATE COLLEGE MED
item Davis, Teresa

Submitted to: Pediatric Academic Society
Publication Type: Abstract Only
Publication Acceptance Date: 3/1/2003
Publication Date: 3/1/2003
Citation: O'Connor, P.M., Kimball, S.R., Orellana, R.A., Bush, J.A., Suryawan, A., Nguyen, H.V., Jefferson, L.S., Davis, T.A. 2003. Glucose contributes to the regulation of postprandial protein synthesis in neonates [abstract]. Pediatric Academic Society. Part II, 53(4):167A.

Interpretive Summary: Not necessary for an Abstract

Technical Abstract: BACKGROUND: The high growth rate of neonates and their high efficiency of dietary protein utilization is driven by high protein synthesis rates which are maximally stimulated after feeding. We have previously delineated the regulatory roles of insulin and amino acids (AA) in the feeding-induced stimulation of neonatal muscle and liver protein synthesis. OBJECTIVE: To determine whether glucose plays a role in the postprandial regulation of protein synthesis in neonates, we performed pancreatic-substrate clamps in fasted, 7-day-old pigs. DESIGN/METHODS: We infused pigs (n=4/grp) with somatostatin to block insulin secretion, glucose to achieve fasting or fed levels (80 or 220mg/dl), insulin to achieve fasting or fed levels (3 or 10 uU/ml), while AA concentrations were maintained at fasting or fed levels. Fractional protein synthesis rates and translation initiation factor activation were determined. RESULTS: Fed glucose levels in combination with fasting insulin and amino acid levels increased muscle protein synthesis by 34%, but had no stimulatory effect on liver protein synthesis. When glucose, insulin, and AA were all increased to fed levels, muscle protein synthesis was stimulated by 109% and liver protein synthesis by 25%. Fed glucose levels in combination with fasting insulin and amino acid levels increased 4E-BP1 phosphorylation by 101% in muscle. Combined fed levels of glucose, insulin and amino acids increased phosphorylation of 4E-BP1 and S6K1 by 515% and 81% in muscle, and in liver by 28% and 13%, respectively. There was no effect of glucose on eIF2B activity in either tissue. CONCLUSIONS: The results suggest that the postprandial rise in glucose contributes to the feeding-induced stimulation of muscle, but not liver, protein synthesis in the neonate by enhancing translation initiation. Furthermore, this postprandial enhancement of translation initiation by glucose in muscle involves 4E-BP1 phosphorylation.