Dr. Robert Smith's Research Focus

Major Research Interests:
AStructure-function studies of proteins; interactions between fibronectin and other extracellular matrix macromolecules.

The high molecular weight glycoprotein, fibronectin, is present in many animal tissue fluids and on the surfaces of numerous cell types. It has been implicated cell adhesion and migration in embryogenesis, connective tissue formation, hemostasis, wound healing, reticuloendothelial system function, pathogen invasion, and cancer malignancy. The interaction of fibronectin with collagen is thought to be crucial to its function. We study the nature and regulation of the specific structural elements that participate in fibronectin-collagen binding. Using chemical modification, we have identified amino acids in fibronectin that contribute to this binding. We hypothesize that fibronectin serves as a molecular chaparone that regulates the biosynthesis of collagen. We have shown that exposure of fibronectin to ultraviolet light (280 nm) results in the photochemical reduction of disulfide bonds and other structural changes that are accompanied by loss of binding to collagen. This phenomenon may be involved in acute skin damage as well as other adverse effects of solar UV radiation. Another current research project is a collaborative study of how the pathogenic yeast Candida albicans establishes and maintains infections by attaching to fibronectin and other extracellular matrix proteins of the host.