|Dr. Robert Smith's Research Focus
AStructure-function studies of proteins; interactions between fibronectin
and other extracellular matrix macromolecules.
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.