| Dalton, Stephen | E-mail: sdalton@uga.edu | | For further information go to www.daltonlab.uga.edu and www.sestemcells.uga.edu
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Our work focuses on the generation of therapeutically useful cell types that can be used to treat cardiovascular disease, diabetes, stroke, autoimmune disease, spinal cord injury and neurological diseases. | | Keywords: stem cells,
cell therapy,
diabetes,
cardiovascular disease,
developmental biology.
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| Glover, Claiborne | E-mail: glover@uga.edu | | Dr. Glover's group is involved in the study of protein phosphorylation as a regulatory mechanism in eukaryotic cells. His group is currently focusing on casein kinase II (CKII), a ubiquitous and highly conserved Ser/Thr protein kinase that phosphorylates a broad spectrum of nuclear and cytoplasmic substrates. The physiological role of CKII is being explored using the budding yeast Saccharomyces cerevisiae as a model system. Biochemical, molecular, genetic, and genomics approaches are employed. | | Keywords: Protein phosphorylation in budding yeast |
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| Kannan, Natarajan | E-mail: kannan@bmb.uga.edu | | Research in my lab is at the intersection of genome biology, evolutionary biology and computational structural biology. We combine techniques and approaches from these diverse disciplines to understand the underlying mechanisms of signaling proteins in atomic detail. | | Keywords: genomics, cancer informatics, evolutionary systems biology, computational structural biology, protein phosphorylation |
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| 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: Biosynthesis and function of the plant cell wall polysaccharide pectin. Anti-cancer effects of pectin |
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| Moremen, Kelley | 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: Biochemistry, molecular, and structural biology of mammalian glycoprotein biosynthesis and catabolism |
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| Pierce, 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: Glycosyltransferase regulation of tumor cell adhesion and invasion; structure/function of lectins |
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| Puett, David | E-mail: puett@bmb.uga.edu | | The current research interests of the Puett lab encompass two major interrelated areas: (1) molecular and cellular biochemical endocrinology of the glycoprotein hormones and their G protein-coupled receptors (GPCRs), and (2) cancer biology and detection.
(1) Molecular and cellular biochemical endocrinology: Research in this area represents a long-standing major focus of the laboratory. Current research is concentrated on: (a) the family of homologous, heterodimeric glycoprotein hormones, composed of LH (luteinizing hormone), FSH (follicle-stimulating hormone), TSH (thyroid-stimulating hormone), and hCG (human chorionic gonadotropin; (b) their cognate GPCRs, members of the largest gene family in the human genome; and (c) the G proteins activated by these receptors, notably Gs. These ligand-receptor-downstream signaling systems regulate the reproductive axis and basal metabolic rate in humans and other animals. The major goals of this project are to elucidate structure-function relationships of the ligands, receptors, and G proteins, including the molecular aspects of ligand-receptor interaction, followed by transmembrane and intracellular signaling leading to biological responses. The experimental approaches include site-directed mutagenesis of the glycoprotein hormones and their receptors, protein engineering, biophysical studies, molecular modeling, and elucidation of cellular signaling pathways mediated by constitutively active and ligand-activated gonadotropin receptor.
(2) Cancer biology and detection:
One of the GPCRs mentioned above, the LH receptor, is expressed in a number of ovarian cancers and believed to influence properties of the tumor. This lab is studying the consequences of ligand-mediated LH receptor expression in cultured human ovarian cancer cells. Approaches include investigations on hormone binding, signaling, gene expression, protein expression, and the effects of receptor activation on cell migration, invasiveness, and metastatic potential. Another study, in collaboration with Prof. Ying Xu, involves gene expression and proteomics on a variety of cancers. The overall aims of these studies are to better understand the expression profiles of different cancers and to seek cancer markers. | | Keywords: Molecular & cellular reproductive biochemical endocrinology, G protein-coupled receptors, tumor biology and early cancer detection |
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| Schmidt, Walter | E-mail: wschmidt@bmb.uga.edu | | Research in our lab is focused on proteases:
The CaaX proteases: Rce1 and Ste24 mediate a proteolytic cleavage event associated with the maturation of proteins that contain a covalently attached isoprenyl lipid at their C-terminus (e.g. Ras, nuclear lamins, fungal pheromones). We are investigating the mechanism and specificity of these proteases in an effort to better understand their role in human disease (e.g. Ras and cancer; lamins and progeria).
The M16A proteases: Ste23 and Axl1 yeast members of the M16A subfamily of metalloproteases. This subfamily includes the human insulin-degrading enzyme, which mediates degradation of amyloidogenic peptides such as the Abeta peptide associated with Alzheimer’s disease. We are investigating the mechanism and specificity of these enzymes to better understand their physiological role in the cell. | | Keywords: proteases, CaaX proteins, isoprenylation, cancer, Alzheimer's disease, yeast |
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| Terns, Michael | E-mail: mterns@bmb.uga.edu | Two major research projects in the Terns Lab:
- Telomerase and cancer: We are investigating the regulation of the biogenesis and transport of the telomerase RNP, a key molecule in the processes of aging and cancer. Telomerase maintains telomeres at the ends of chromosomes. Telomerase activity and telomere length are lost with aging, resulting in cell senescence and death. In order to be able to grow indefinitely, nearly all cancer cells re-activate telomerase. Thus telomerase is a promising target for anti-cancer and anti-aging therapies. In cancer cells, we have found that the two essential components of telomerase (telomerase RNA and TERT) travel distinct, cell cycle-regulated pathways within the nucleus that culminate in co-localization at telomeres during S phase for telomere synthesis. We are working to identify the factors responsible for the regulated activity of telomerase in normal and cancer cells.
- Virus defense in prokaryotes: All bacteria (including human pathogens) are subject to attack by viruses and other genome invaders. We are working to delineate a newly-identified RNA-mediated pathway that protects bacteria and archaea from viruses and other invaders. The pathway appears to parallel the eukaryotic RNAi pathway and is referred to as "prokaryotic RNAi". This is a very exciting new research area with significant biomedical and biotechnological importance.
| | Keywords: non-coding RNAs, RNA-protein complexes, regulation of telomerase, cancer, RNAi, virus defense |
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| Urbauer, Jeffrey | E-mail: urbauer@chem.uga.edu | | Our research focuses on protein structure and function and protein-protein interactions. We employ an approach combining modern analytical, biophysical and molecular biology techniques, with an emphasis on biomolecular NMR spectroscopy. Our core projects include the study of gene regulation and novel regulators of transcription initiation in bacteria, oxidative stress and calcium signaling, steroid hormone (estrogen) receptor activation, and regulation of biofilm formation and pathogenesis in Pseudomonas aeruginosa. These projects are important fundamentally, and they important biomedically with respect to antibiotic target development, oxidative stress and biological aging, and diseases such as breast cancer and cystic fibrosis. | | Keywords: Transcription regulation, steroid hormone receptors, estrogen receptor, breast cancer, oxidative stress, calcium signaling, calmodulin, NMR spectroscopy, physical biochemistry |
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| Wang, Lianchun | E-mail: lwang@ccrc.uga.edu | | Research in the Wang laboratory focuses on the structure and function of heparan sulfate proteoglycans in vasculature and cancer biology. Heparan sulfate proteoglycans are glycoconjugates which are abundant on the cell surface and in the extracellular matrix. In vitro studies have suggested that heparan sulfate proteoglycans interact with growth factors, growth factor binding proteins, extracellular proteases, protease inhibitors, chemokines, morphogens, and cell adhesive proteins to modulate cell differentiation, proliferation, migration, blood coagulation, lipid metabolism, and leukocyte trafficking. However, the biological and pathological functions of heparan sulfate proteoglycans in vivo are still largely unknown. Using techniques, including conditional mouse gene targeting, embryonic stem (ES) cell differentiation, primary cell culture, and mouse models, the Wang lab is aiming to understand the roles and the underlying mechanisms of heparan sulfate proteoglycan in vascular development, cancer biology and blood coagulation in vivo, and to develop novel approaches to cure the related pathological conditions. | | Keywords: Heparan sulfate proteoglycan, angiogenesis, tumorigenesis, tumor metastasis, stem cell, coagulation |
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| Wells, Lance | E-mail: lwells@ccrc.uga.edu | | Our laboratory is interested in how post-translational modifications of proteins increase functional diversity. Primarily, we are interested in glycosylation, with a focus on 1. O-GlcNAc in Type II diabetes and stem cell biology , 2. O-Mannosylation in Congenital Muscular Dystrophy and viral entry into host cells, 3. Glycoproteins as biomarkers in human disease, specifically pancreatic cancer and metabolic syndrome, 4. Development of technology-based approaches, primarily mass-spectrometry, for quantitive proteomics/glycomics/glycoproteomics. | | Keywords: O-glycoslyation, type II diabetes, congenital muscular dystrophy, cancer, glyco/proteomics. |
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