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Thomas M. Beres, Ph.D.

Staff Scientist
Section on Biological Chemistry, DIR

NATIONAL INSTITUTES OF HEALTH/NIDCR
BUILDING 30 ROOM 524
30 CONVENT DR
BETHESDA MD 20892

Phone: 301-496-8904
Fax: 301-480-5353
E-mail: berestm@mail.nih.gov

Research Interests

My goal is to understand the biological role of O-linked glycosylation during eukaryotic development. Mucin-type O-glycosylation is initiated by a family of enzymes, ppGalNAcTs, that catalyzes the transfer of GalNAc to serine or threonine residues of protein substrates. Many of the genes encoding these enzymes are under strong temporal and spatial regulation during early development, suggesting that they have important developmental functions. However, because of the large number of family members (18 in mice; 20 in human) and their overlapping spatial and temporal patterns of expression and redundant functions, specific gene knockouts in mice have only yielded subtle phenotypes. As a basal deuterostome, the sea urchin is a sister to the chordates, the evolutionary precursors to the vertebrates. Analysis of development of all cell types is possible because of the transparency of the embryo and availability of many molecular tools to monitor developmental progress. Importantly, the sea urchin genome is predicted to have significantly fewer genes encoding ppGalNAcTs than mammals, likely making functional analysis of individual family members more feasible. In collaboration with the laboratory of Drs. Lynne and Robert Angerer, we are employing the sea urchin, Strongylocentrotus purpuratus, as a model system in which to study the role of O-glycans during embryonic development. We are using a variety of tools, including antisense morpholinos, to eliminate individual ppGalNAcT enzyme function and analyzing the resulting morphological and molecular abnormalities using a combination of in situ hybridization, antibody staining, and microscopy. In addition to my work in sea urchin, I am exploring the physiological roles of several ppGalNAcTs in lipid metabolism and male fertility, as well as evaluating potential inhibitors of ppGalNAcTs. The combination of these studies will further elucidate the physiological roles for O-glycans in both invertebrate and mammalian systems.

Complete CV [PDF File 26KB]

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This page last updated: February 26, 2014