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Scott Garman

Associate Professor

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.

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 http://www.biochem.umass.edu/faculty/scott-c-garman

Academic Background

  • PhD Harvard University
  • Postdoctoral training: Northwestern University
Clark, NE, Garman, SC. The 1.9 A structure of human alpha-N-acetylgalactosaminidase: The structural basis of Schindler and Kanzaki diseases. Journal of Molecular Biology. 2009, Oct 23;393(2):435-447.
Ishii S, Chang HH, Kawasaki K, Yasuda K, Wu HL, Garman SC, Fan JQ. Mutant alpha-galactosidase A enzymes identified in Fabry disease patients with residual enzyme activity: biochemical characterization and restoration of normal intracellular processing by 1-deoxygalactonojirimycin. Biochem J. 2007 Sep 1;406(2):285-95.
Hebert DN, Garman SC, Molinari M. (2005) "The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags." Trends Cell Biol. Jul;15(7):364-70. Review.
Su HP, Garman SC, Allison TJ, Fogg C, Moss B, Garboczi DN. (2005) "The 1.51-Angstrom structure of the poxvirus L1 protein, a target of potent neutralizing antibodies." Proc Natl Acad Sci U S A. Mar 22;102(12):4240-5. Epub 2005 Mar 10.
Ries M, Gupta S, Moore DF, Sachdev V, Quirk JM, Murray GJ, Rosing DR, Robinson C, Schaefer E, Gal A, Dambrosia JM, Garman SC, Brady RO, Schiffmann R. (2005) "Pediatric Fabry disease." Pediatrics. Mar;115(3):e344-55. Epub 2005 Feb 15.
 
Contact Info

Department of Biochemistry and Molecular Biology
1021K Lederle Graduate Research Tower
710 North Pleasant Street
Amherst, MA 01003-9292

(413) 577-4488
garman@biochem.umass.edu
http://www.biochem.umass.edu/faculty/scott-c-garman