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Edie C. Goldsmith

Edie C. Goldsmith

Edie C. Goldsmith
Associate Professor
Dept.of Cell Biology and Anatomy
University of South Carolina
USA

University of South Carolina

Biography

present  Assistant Professor, University of South Carolina School of Medicine,2002  Research Assistant Professor, University of South Carolina School of Medicine,1998-1999  Postdoctoral Fellow, University of South Carolina School of Medicine,1996-1998   Postdoctoral Fellow, University of South Carolina Department of Biology and 1990-1996   Graduate Student, University of North Carolina  Chapel Hill

Research Interest

Interactions between cells and the surrounding extracellular matrix (ECM) are important in a variety of cellular processes including adhesion, migration, proliferation, differentiation and apoptosis. Elucidating the factors that regulate and mediate these interactions represents a fundamental step in understanding how the dynamic reciprocity between cells and the ECM is mediated. The interaction of cells with the ECM is mediated by cell surface receptors that are capable of binding a variety of ECM components. The Discoidin Domain Receptors (DDR1 and DDR2) represent an additional pathway for communicating information about the extracellular environment to the cell. DDRs represent a novel group of receptor tyrosine kinases whose ligand is the ECM protein collagen. The focus of my research is to understand the functional role of this new class of ECM receptors, particularly DDR2, in cardiac development. The main focus currently is exploring the role of DDR2 in mediating ECM remodeling during atrioventricular cushion formation during early valve development. Questions we are interested in include how DDR2 interacts with the ECM, what effect this interaction has on the organization/structure of the ECM along with potential changes in DDR2 expression and distribution, and what information these receptors are capable of providing to the cell. We are also interested in examining the potential interactive role that DDR2 may have with integrins in regulating cardiac fibroblast response to the ECM.

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