The importance of protein glycosylation in human development has been underscored by the emergence of a group of inherited disorders known as the congenital disorders of glycosylation (CDG). Using both cell biological and biochemical approaches, our laboratory seeks to identify and characterize novel forms of these disorders with particular interest in CDGs that arise from defects in proteins that support overall Golgi function (i.e. proteins involved in vesicular trafficking events). Utilizing zebrafish as a vertebrate model organism, we are also interested in studying the craniofacial pathogenesis of lysosomal storage diseases and related genetic disorders. The goal is to delineate the cellular and molecular events that lead to the developmental defects in these patients.
R. Steet, S. Chung, W.S. Lee, C.W. Pine, H. Do, S. Kornfeld. 2007. Selective action of the iminosugar isofagomine, a pharmacological chaperone for mutant forms of acid-beta-glucosidase . Biochem. Pharmacol. 73: 1376-1383. PMID:17217920
R. Steet, S. Kornfeld. 2006. COG-7 deficient human fibroblasts exhibit altered recycling of Golgi proteins. Mol. Biol. Cell 17: 2312-2321. PMID:16510524
R. Steet, S. Chung, B. Wustman, D.A. Powell, S.H. Doares, S. Kornfeld. 2006. The iminosugar isofagomine increases the activity of N370S mutant acid-beta-glucosidase in Gaucher fibroblasts by several mechanisms. Pro. Natl. Acad. Sci. 103: 13813-13818.PMID:16945909