| Adang,
Michael J. |
E-mail:
adang@uga.edu |
| Bacillus
thuringiensis (Bt) is a bacterium the produces protein crystals
that are toxic to insects. The greatest usage of Bt has come
from the engineering of Bt genes into crop plants. In the Adang
laboratory, we combine mutational analyses of Bt toxins with
molecular characterization of glycoprotein receptors in the
insect midgut to elucidate the steps in Bt toxin action. We
also are using a proteomic approach to identify proteins in
the brush border epithelium of pest insects of agricultural
and medical importance. The goal is to understand, at the molecular
level, how insects adapt to Bt toxins and pathogens. |
| Keywords:
Bacillus thuringiensis, toxins, insects, glycoproteins, biopesticides,
Bt, membrane proteins |
|
| Mohnen,
Debra |
E-mail:
dmohnen@ccrc.uga.edu |
| Tendons
are connective tissues that transmit the force created in the
muscle to the bone, and thereby make movement possible. The
basic functional units in tendons are collagen fibers that are
crosslinked by proteoglycans. The proteoglycans are believed
to influence the ability of the tendons to respond to strains
and stresses. In collaboration with other researchers in The
Soft Tissue Center we are using chicken as a model system to
study the role of proteoglycans in tendon structure, function,
and repair. Current emphasis involves characterizing the proteoglycans
in chicken gastrocnemius tendons and studying how the proteoglycans
change in tendons under stress. |
| Keywords:
pectin, cell wall, polysaccharide, homogalacturonan, glycosyltransferase,
galacturonosyltransferase, methyltransferase, epimerase, oligosaccharide,
oligogalacturonide, Golgi, membrane, tendon, proteoglycan, glycosaminoglycan
|
|
| 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 |
|
| 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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