Research in our lab focuses on structural biology. We are interested in glycoproteins, particularly those implicated in human disease. Recent structural results on three topics of particular interest are described under Current Research.
Lysosomal storage diseases: In the lysosome, breakdown of glycoproteins and glycolipids occurs via the action of proteases, lipases, and glycosidases. Our lab is interested in the function and trafficking of lysosomal enzymes, required components in the catabolism of macromolecules. Deficiencies in these enzymes result in the accumulation of their substrates, which eventually leads to the symptoms of lysosomal storage diseases (a family containing over 40 members including Gaucher, Tay-Sachs, and Fabry diseases). Malarial surface proteins: Through the course of its life cycle, the malaria parasite Plasmodium expresses scores of receptors on its surface. These receptors function in cell adhesion, entry into host cells, and immune system evasion. Due to their accessibility on the surface of the parasite and their functional importance, many show promise as vaccine candidates. Antibody-receptor interactions: Fc receptors are found on the surface of immune cells, where they couple the exact specificity of antibodies to the specialized effector functions of different immune cells. Fc receptors bind antibodies distal to the antigen binding site on the antibody. In the case of mast cells, the high affinity IgE Fc receptor (FcεRI) binds the IgE antibody, and the appearance of specific antigens (such as allergens) causes crosslinking of the IgE:Fc receptor complexes. This crosslinking initiates a src kinase-mediated signal transduction pathway in the cell, leading minutes later to the degranulation of the mast cell and to the subsequent appearance of allergic symptoms.
Learn more at www.biochem.umass.edu/faculty/scott-c-garman
- PhD Harvard University
- Postdoctoral training: Northwestern University