| Moremen,
Kelley W. |
E-mail:
moremen@uga.edu |
| Research in the
Moremen lab focuses on the structure, enzymology, regulation,
and localization of enzymes involved in the biosynthesis, recognition,
and catabolism of mammalian glycoproteins. Carbohydrate structures
on glycoproteins contribute to many biological recognition events
between molecules and between cells in an organism. Alterations
in the synthesis and degradation of these structures can also
occur in human genetic disease. Work in the Moremen lab is focused
on (1) the characterization of enzymes involved in mammalian
glycoprotein biosynthesis and catabolism and the functionally
defective forms of these enzymes involved in human genetic disease
and (2) the identification and characterization of carbohydrate-binding
proteins and their roles in vertebrate development and physiology. |
| Keywords: enzymology
and molecular biology of glycosylation enzymes, enzyme structure,
human genetic disease |
|
| Pierce,
J. Michael |
E-mail:
hawkeye@uga.edu |
| Our research focuses
on the function of glycoconjugates in the regulation of cell
adhesion. 1) investigation of the mechanism how glycosyltransferases
and oligosaccharide expression regulate cell adhesion, migration,
and invasiveness; 2) structure and function of the glycosyltransferase
GlcNAc-T V to develop an inhibitor as a cancer therapeutic;
3) identification of glycoprotein glycoforms diagnostic for
carcinomas; 4) function of a novel endothelial cell lectin,
most likely in pathogen surveillance; 5) structural determination
of a new family of animal and fungal lectins, the X-type lectins;
6) functions of lectins in animal development and as ligands
for BT toxins. |
| Keywords: glycosyltransferases;
signal transduction; cell adhesion; pathogen surveillance; protein
structure/function; oligosaccharide structure / function; tumor
markers |
|
| Puett,
J. David |
E-mail:
puett@bmb.uga.edu |
| Dr. Puett's laboratory
is engaged in research on glycoprotein hormones and their cognate
G protein-coupled receptors, with emphasis on molecular and
cellular reproductive biochemical endocrinology and tumor biology.
One of the major goals being addressed is that of the molecular
mechanism of ligand-mediated receptor activation necessary for
intracellular signaling. Techniques employed include protein
engineering, site-directed mutagenesis, protein expression,
cell culture, determination of signaling pathways, characterization
of tumor antigens, and transgenic mice. Using ethnobotanical
information, research is also conducted on natural products
extracted from plants and assayed via high-throughput screening. |
| Keywords: glycoprotein
hormones, G protein-coupled receptors, transgenic mice, cancer,
natural products |
|
| Schmidt,
Walter K. |
E-mail:
wschmidt@bmb.uga.edu |
| Research in our
lab is focused on three proteases: Rce1, Ste24 and Axl1. These
membrane-localized proteases, two of which are zinc-dependent
enzymes, are required for the biogenesis of certain prenylated
signaling molecules. Prenylated proteins contain a covalently
attached lipid at the C-terminus and are exemplified by Ras,
Ras-related proteins, and secreted fungal mating pheromones.
Because prenylated molecules function in a variety of cellular
pathways that are linked to human disease (e.g. Ras and cancer),
understanding the roles of Rce1, Ste24 and Axl1 in the biogenesis
of prenylated molecules may lead to novel therapeutic strategies
for cancer and other diseases. |
| Keywords: cancer, protease,
post-translational modifications, prenylation, signaling, yeast |
|
| Terns,
Michael P. |
E-mail:
mterns@bmb.uga.edu |
| Telomerase, the
ribonucleoprotein enzyme required for the synthesis of telomeres
at the ends of chromosomes, is a key molecule in both aging
and cancer. Telomerase is inactive in nearly all normal human
somatic cells but is active in the vast majority of human cancer
cell lines and malignant tumors. We have found that the RNA
component of the telomerase RNP is retained in the nucleus and
targeted to nucleoli by a snoRNA-like motif. We are continuing
to investigate the biogenesis and intracellular transport of
telomerase RNA in normal and cancer cells. RNA enzymes (ribozymes)
are being developed as promising human gene therapy agents for
the treatment of a variety of human diseases including cancer.
Anti-cancer ribozymes are being designed to prevent the expression
of key proteins (e.g. oncogenes, mutated tumor suppressor genes,
and genes that cause resistance to contemporary anti-cancer
drugs) known to cause or maintain a cancerous state in cells.
However ribozymes that demonstrate good activity in vitro are
often found to be ineffective when introduced into living cells.
We are determining the pathways that are normally traversed
by cellular RNAs and applying our knowledge to engineer RNA
therapeutics that function efficiently within cells. |
| Keywords: nucleic acids-RNA
(biogenesis, transport, and function), biomedical research (telomerase,
gene therapy, ribozymes), hyperthermophilic Archaea (Pyrococcus
furiosus) |
|
| Tiemeyer, Michael |
E-mail: mtiemeyer@ccrc.uga.edu |
Specific cell surface oligosaccharides function as identity tags, allowing cells to appropriately interact with each other and with their environment. We utilize genetic, molecular, and chemical techniques in vertebrate (mouse) and insect (Drosophila) model systems to study two aspects of carbohydrate expression: 1) the influence of cell surface carbohydrates on development of the nervous system, 2) mechanisms that control tissue- and stage-specific oligosaccharide expression. Our results have implications for facilitating regeneration of axon pathways in the nervous system, for understanding innate immunity and tissue surveillance, and for controlling the cellular changes that precede tumor metastasis. |
| Keywords:glycosylation, N-linked oligosaccharides, glycosphingolipid, Drosophila, Toll-like receptor, neural development |
|
| Wells, Lance |
E-mail: lwells@ccrc.uga.edu |
| Our broad research interest is in understanding how post-translational modifications modulate the properties of proteins. Specifically, we study "nutrient sensing" by characterizing the enzymes responsible for post-translational modification of proteins that have been implicated in responding to nutrients and regulating signal transduction cascades. Our lab uses a combination of methodologies including mass spectrometry, protein biochemistry, cell biology, proteomics, and molecular biology. We perform our experiments in vitro, in mammalian cell culture systems, and in the model organism C. elegans. We are currently focusing on the regulatory role of glycosylation in the development of type II diabetes, cancer, and congenital muscular dystrophy. |
| Keywords: glycosylation, phosphorylation, mass spectrometry, proteomics, signal transduction, diabetes, cancer, protein biochemistry |
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