Document Detail


Prolonged infusion of amino acids increases leucine oxidation in fetal sheep.
MedLine Citation:
PMID:  22454287     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Maternal high-protein supplements designed to increase birth weight have not been successful. We recently showed that maternal amino acid infusion into pregnant sheep resulted in competitive inhibition of amino acid transport across the placenta and did not increase fetal protein accretion rates. To bypass placental transport, singleton fetal sheep were intravenously infused with an amino acid mixture (AA, n = 8) or saline [control (Con), n = 10] for ∼12 days during late gestation. Fetal leucine oxidation rate increased in the AA group (3.1 ± 0.5 vs. 1.4 ± 0.6 μmol·min(-1)·kg(-1), P < 0.05). Fetal protein accretion (2.6 ± 0.5 and 2.2 ± 0.6 μmol·min(-1)·kg(-1) in AA and Con, respectively), synthesis (6.2 ± 0.8 and 7.0 ± 0.9 μmol·min(-1)·kg(-1) in AA and Con, respectively), and degradation (3.6 ± 0.6 and 4.5 ± 1.0 μmol·min(-1)·kg(-1) in AA and Con, respectively) rates were similar between groups. Net fetal glucose uptake decreased in the AA group (2.8 ± 0.4 vs. 3.9 ± 0.1 mg·kg(-1)·min(-1), P < 0.05). The glucose-O(2) quotient also decreased over time in the AA group (P < 0.05). Fetal insulin and IGF-I concentrations did not change. Fetal glucagon increased in the AA group (119 ± 24 vs. 59 ± 9 pg/ml, P < 0.05), and norepinephrine (NE) also tended to increase in the AA group (785 ± 181 vs. 419 ± 76 pg/ml, P = 0.06). Net fetal glucose uptake rates were inversely proportional to fetal glucagon (r(2) = 0.38, P < 0.05), cortisol (r(2) = 0.31, P < 0.05), and NE (r(2) = 0.59, P < 0.05) concentrations. Expressions of components in the mammalian target of rapamycin signaling pathway in fetal skeletal muscle were similar between groups. In summary, prolonged infusion of amino acids directly into normally growing fetal sheep increased leucine oxidation. Amino acid-stimulated increases in fetal glucagon, cortisol, and NE may contribute to a shift in substrate oxidation by the fetus from glucose to amino acids.
Authors:
Anne M Maliszewski; Monika M Gadhia; Meghan C O'Meara; Stephanie R Thorn; Paul J Rozance; Laura D Brown
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-03-27
Journal Detail:
Title:  American journal of physiology. Endocrinology and metabolism     Volume:  302     ISSN:  1522-1555     ISO Abbreviation:  Am. J. Physiol. Endocrinol. Metab.     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-06-18     Completed Date:  2012-08-27     Revised Date:  2013-07-03    
Medline Journal Info:
Nlm Unique ID:  100901226     Medline TA:  Am J Physiol Endocrinol Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  E1483-92     Citation Subset:  IM    
Affiliation:
Perinatal Research Center, Department of Pediatrics, University of Colorado School of Medicine, Aurora, USA.
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MeSH Terms
Descriptor/Qualifier:
Acid-Base Equilibrium / physiology
Amino Acids / blood,  pharmacology*
Animals
Blood Gas Analysis
Blotting, Western
Carbon Dioxide / blood
Female
Fetus / metabolism*
Glucose / metabolism
Glucose-6-Phosphatase / metabolism
Hormones / blood
Infusions, Intravenous
Kinetics
Lactic Acid / metabolism
Leucine / metabolism*
Organ Size / physiology
Oxidation-Reduction
Phosphoenolpyruvate Carboxykinase (ATP) / genetics
Pregnancy
Pulmonary Gas Exchange
Real-Time Polymerase Chain Reaction
Sheep / metabolism*
Tissue Distribution
Grant Support
ID/Acronym/Agency:
K01 DK090199/DK/NIDDK NIH HHS; K01-DK-090199/DK/NIDDK NIH HHS; K08 HD060688/HD/NICHD NIH HHS; K08-HD-060688/HD/NICHD NIH HHS; K12-HD-057022/HD/NICHD NIH HHS; P30-DK-57516/DK/NIDDK NIH HHS; R01 DK088139/DK/NIDDK NIH HHS; R01-DK-088139/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Hormones; 124-38-9/Carbon Dioxide; 50-21-5/Lactic Acid; 50-99-7/Glucose; 61-90-5/Leucine; EC 3.1.3.9/Glucose-6-Phosphatase; EC 4.1.1.49/Phosphoenolpyruvate Carboxykinase (ATP)
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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