WASHINGTON UNIVERSITY IN ST. LOUIS SCHOOL OF MEDICINE PEDIATRICS FACULTY CARL H. SMITH, M.D.
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             Picture of Carl H. Smith, M.D.
 
 
 
Carl H. Smith, M.D.    contact information ]

Professor of Pediatrics; Co-director Chemistry Section Core Laboratory; Co-director Core Laboratory

Dr. Smith graduated from Swarthmore College and received his M.D. degree from Yale University in 1959. After training in pathology at Barnes and St. Louis Children's Hospital and in pediatrics at Johns Hopkins Hospital and two years in the Public Health Service, he joined the faculty of Washington University in 1965. Between 1969 and 1972, he went on sabbatical leave to gain experience in clinical laboratory chemistry and fetal and placental physiology. Since 1972, he has been Director of the Clinical Chemistry Laboratory at St. Louis Children's Hospital and in 1986, became overall Laboratory Director.

The major goal of Dr. Smith's research interests continues to be the understanding of the cellular mechanisms of the transfer of amino acids, calcium and other major nutrients by the placenta. These investigations have been pursued using a variety of models: tissue fragments and plasma membranes isolated specifically from the maternal and fetal facing surfaces of human placenta, cultured placental cytotrophoblast and the BeWo choriocarcinoma cell. Membrane functional pathways for transport of neutral, cationic, and anionic amino acids and for the ATP dependent concentrative transport of calcium have been characterized. These investigations have allowed the development of functional cellular models for the fetal supply of calcium and the groups of amino acids and their controls.

At present, this characterization is being extended to the molecular level by cloning the cDNAs for various placental membrane cationic amino acid transport proteins, developing procedures for measuring their mRNAs and the changes in their expression during trophoblast cell differentiation. The relationship of cDNA, mRNA and transport protein with transport function in placental membranes is determined by expression of the cloned cDNAs in Xenopus oocyte and cultured epithelial cell models.

Selected Publications

  1. Smith CH, Moe AJ, Ganapathy V: Nutrient transport pathways across the epithelium of the placenta. Ann Rev Nutr 1992; 12:183-206.

  2. Furesz TC, Smith CH, Moe AJ: ASC system activity is altered by development of cell polarity in trophoblast from human placenta. Am J Physiol 1993; 265:C212-C217.

  3. Furesz TC, Moe AJ, Smith CH: Lysine uptake by human placental microvillous membrane: comparison of system y with basal membrane. Am J Physiol (Cell Physiol), 1995; 37:C755-C761.

  4. Furesz TC, Smith CH: Identification of two leucine sensitive lysine transport activities in human placental basal membranes. Placenta 1997; 18:649-655.

  5. Kamath SG, Furesz TC, Way BA, Smith CH: Identification of three anionic amino acid transporters in placental trophoblast: Cloning, expression and characterization of hCAT-1. J Membrane Biol 1999; 171:55-62.

  6. Cariappa R, Heath-Monnig E, Furesz TC, Kamath SG, Smith CH: Stable polarized expression of hCAT-1 in an epithelial cell line. (Presented at Experimental Biology 2000) 2000; San Diego, Ca., April 15-18.


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