| Mendicino,
Joseph F. |
E-mail:
mendicin@bmb.uga.edu |
| Cystic
fibrosis is a genetic disorder which results in the secretion
of very viscous mucus from cells in the trachea. This effect
ultimately leads to infection of the lungs and death. Studies
of the composition of tracheobronchial mucous glycoproteins
from patients with cystic fibrosis have shown that they exhibit
increased sulfation of longer carbohydrate chains. The metabolic
basis for the formation of these altered chains is unknown.
The primary disorder in cystic fibrosis is caused by an alteration
in membrane chloride ion transport. However increased levels
of intracellular sulfate may be a secondary consequence of electrolyte
abnormalities in this disease and may lead to increased sulfation
of longer oligosaccharide chains. Our studies are concerned
with the regulation of sulfation of these chains. |
| Keywords:
Cystic Fibrosis, sulfation, regulation, mucus, glycoproteins,
genetic defects |
|
| Mohnen,
Debra |
E-mail:
dmohnen@ccrc.uga.edu |
| Pectin
is a family of complex polysaccharides present in all plant
primary cell walls. Pectin plays multiple roles in plant growth,
development, and defense responses; in part through contributing
to cell wall strength, wall ion exchange and sieving properties,
cell-cell adhesion, and cell-cell communication. Pectin is a
food fiber and a commercial gelling agent that has beneficial
effects on human health. Our long term goal is to decipher how
the 53 distinct enzyme activities required for pectin synthesis
interact to synthesize pectin and to modify pectin synthesis
in order to study pectin function. Towards this goal we are
purifying, cloning, and characterizing the biosynthetic enzymes;
many of which are Golgi localized and membrane bound enzymes.
Current emphasis is on the galacturonosyltransferase and the
methyltransferase that synthesize the pectic polysaccharide
homogalacturonan. |
| Keywords:
pectin, cell wall, polysaccharide, homogalacturonan, glycosyltransferase,
galacturonosyltransferase, methyltransferase, epimerase, oligosaccharide,
oligogalacturonide, Golgi, membrane, tendon, proteoglycan, glycosaminoglycan
|
|
| 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 |
|
| 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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