Leucine, a key essential branched chain amino acid, may have a role in the regulation of protein metabolism. In addition, measurements of leucine kinetics have been used as a model to estimate whole body rates of protein turnover, synthesis, breakdown and oxidation. Currently, there is little information concerning leucine kinetics in the neonatal period, and limited knowledge of fetal leucine metabolism. These studies will determine leucine kinetics in specific human neonatal populations (term normal newborns, small and large for gestational age infants, and premature neonates) in a variety of nutritional states (fasting versus feeding, enteral versus parenteral) using a constant tracer infusion of 1-13C leucine combined with respiratory calorimetry. In addition, similar techniques (using 1-14C leucine) will be employed to quantitate leucine metabolism in the normal and experimental intrauterine growth retarded fetal and neonatal lamb. The performance of these studies will 1) generate new information concerning leucine metabolism in several important neonatal populations, 2) determine how alterations in the intrauterine environment might affect fetal and neonatal leucine (and protein) metabolism, 3) further the understanding of protein accretion in the neonatal period, and 4) provide an objective means to assess different nutritional strategies.

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
Clinical Investigator Award (CIA) (K08)
Project #
7K08HD000840-02
Application #
3081369
Study Section
Maternal and Child Health Research Committee (HDMC)
Project Start
1988-07-01
Project End
1991-06-30
Budget Start
1989-07-01
Budget End
1990-06-30
Support Year
2
Fiscal Year
1989
Total Cost
Indirect Cost
Name
Indiana University-Purdue University at Indianapolis
Department
Type
Schools of Medicine
DUNS #
005436803
City
Indianapolis
State
IN
Country
United States
Zip Code
46202
Huddleston, Heather; Schust, Danny J (2004) Immune interactions at the maternal-fetal interface: a focus on antigen presentation. Am J Reprod Immunol 51:283-9
Bedecarrats, Gregoy Y; O'Neill, Francis H; Norwitz, Errol R et al. (2003) Regulation of gonadotropin gene expression by Mullerian inhibiting substance. Proc Natl Acad Sci U S A 100:9348-53
Patel, Radhika N; Quack, Katharina C; Hill, Joseph A et al. (2003) Expression of membrane-bound HLA-G at the maternal-fetal interface is not associated with pregnancy maintenance among patients with idiopathic recurrent pregnancy loss. Mol Hum Reprod 9:551-7
Norwitz, Errol R; Xu, Shuyun; Xu, Jian et al. (2002) Direct binding of AP-1 (Fos/Jun) proteins to a SMAD binding element facilitates both gonadotropin-releasing hormone (GnRH)- and activin-mediated transcriptional activation of the mouse GnRH receptor gene. J Biol Chem 277:37469-78
Norwitz, Errol R; Xu, Shuyun; Jeong, Kyeong-Hoon et al. (2002) Activin A augments GnRH-mediated transcriptional activation of the mouse GnRH receptor gene. Endocrinology 143:985-97
Gould, D S; Ploegh, H L; Schust, D J (2001) Murine female reproductive tract intraepithelial lymphocytes display selection characteristics distinct from both peripheral and other mucosal T cells. J Reprod Immunol 52:85-99
Norwitz, E R; Schust, D J; Fisher, S J (2001) Implantation and the survival of early pregnancy. N Engl J Med 345:1400-8
Furman, M H; Ploegh, H L; Schust, D J (2000) Can viruses help us to understand and classify the MHC class I molecules at the maternal-fetal interface? Hum Immunol 61:1169-76
Schust, D J; Tortorella, D; Ploegh, H L (1999) HLA-G and HLA-C at the feto-maternal interface: lessons learned from pathogenic viruses. Semin Cancer Biol 9:37-46
Schust, D J; Tortorella, D; Seebach, J et al. (1998) Trophoblast class I major histocompatibility complex (MHC) products are resistant to rapid degradation imposed by the human cytomegalovirus (HCMV) gene products US2 and US11. J Exp Med 188:497-503

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