The VICC.ORG Directory of Doctors, Healthcare Providers & Researchers

David E. Ong, Ph.D.

Professor of Biochemistry
VICC Member

Contact Information:

Vanderbilt University Medical Center
610 Robinson Research Building
Nashville, TN 37232-0146

Research Specialty

Vitamin A (Retinoid) binding proteins; Retinoid metabolism and function; Retinoid regulated gene expression.

Research Description

Vitamin A is an essential micronutrient that provides not only the signaling molecule essential for vision (11-cis-retinal) but also other retinoids. For example, retinoic acid activates a family of nuclear proteins (the Retinoic Acid Receptors a, b, and g) that direct transcription of genes important for morphological development, proper cellular differentiation and growth control. One member of the RAR group is found in virtually every cell type examined, indicating the essential role that retinoids play in proper bodily function. Remarkably, we still know little about how, where, and when the retinoic acid that activates these receptors is produced. This is currently the major interest of this laboratory. Central to retinoic acid production are a family of carrier proteins, found within certain cells (the cellular retinoid binding proteins), and the plasma carrier protein for the parent retinoid, retinol (retinol binding protein). We have demonstrated that these carrier proteins are directly recognized by other cellular components (enzymes and membrane transporters) to allow the proper delivery and metabolism of retinoids. Our work focuses on defining these interactions at the molecular level as well as using such interactions to find previously unknown enzymes essential for the functions of vitamin A. Techniques used range from site-directed mutagenesis of these proteins to study their interaction with both ligand and enzymes, classical work in enzymology, molecular biological approaches for the study of regulation, as well as immunolocalization at both the light and electron microscopic level of these players to define sites of retinoid action.



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