This proposal is a competing renewal for the NIGMS P41 National Center for Biomedical Glycomics. Glycomics can be defined in several ways, but in terms of our Center, we define Glycomics as the study of glycans, glycoconjugates, the proteins that regulate their expression, and the proteins that recognize them;in particular, we are interested in developing tools to facilitate learning how these molecules change during early embryonic development and during the onset of disease as a result of mutations that affect glycan expression. To develop technologies that will impact the understanding and regulation of the diversity of glycosylation, therefore, we felt it necessary to focus on Glycomics from more of a Systems Biology approach: investigation of glycosylation in a particular biological context, analysis of the fine details of glycan expression on glycoconjugates produced in specific cell types, identification of the glyco-genes that participate in glycan biosynthesis and the biosynthetic pathways that the enzymes and transporters expressed from the glyco-genes constitute. The structure of the Resource is focused on four Technological Research &Development programs plus Analytical Service and Training: TR&D1: Stem Cell and Induced Pluripotent Stem Cell (IPSC) Resources;TR&D2: Glycomics and Glycoproteomics;TR&D3: Transcriptome and Glycome Regulation;TR&D4: Glycobioinformatics. Our Center lists 31 DBPs, 73 Collaborative Projects, 192 Service projects, and four Courses/Workshops that have had 245 participants over the last four years. We also report 83 publications resulting from research associated with the Center. We have developed technologies in each of our TR&D that have significantly impacted the biomedical research community, and our over-arching goal is to amplify that impact over the next funding period.

Public Health Relevance

The study of Glycomics is in its early stages and is very dependent on the development of tools and technologies. Glycomics involves types of molecules called glycans that are on the surfaces of cells which regulate many physiological processes such as inflammation and innate immunity. We have developed tools to assist biomedical researchers in understanding the structure and functions of these fascinating biomolecules.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Biotechnology Resource Grants (P41)
Project #
2P41GM103490-11
Application #
8475856
Study Section
Special Emphasis Panel (ZRG1-IMST-J (40))
Program Officer
Sheeley, Douglas
Project Start
2003-09-01
Project End
2018-07-31
Budget Start
2013-08-01
Budget End
2014-07-31
Support Year
11
Fiscal Year
2013
Total Cost
$2,859,327
Indirect Cost
$622,334
Name
University of Georgia
Department
None
Type
Organized Research Units
DUNS #
004315578
City
Athens
State
GA
Country
United States
Zip Code
30602
Talabnin, Krajang; Talabnin, Chutima; Ishihara, Mayumi et al. (2016) Differential Expression of O-glycoprotein Glycans in Cholangiocarcinoma Cell Lines. Asian Pac J Cancer Prev 17:691-5
Yu, Seok-Ho; Zhao, Peng; Sun, Tiantian et al. (2016) Selective Exo-Enzymatic Labeling Detects Increased Cell Surface Sialoglycoprotein Expression upon Megakaryocytic Differentiation. J Biol Chem 291:3982-9
Parkinson, William M; Dookwah, Michelle; Dear, Mary Lynn et al. (2016) Synaptic roles for phosphomannomutase type 2 in a new Drosophila congenital disorder of glycosylation disease model. Dis Model Mech 9:513-27
Berger, Ryan P; Dookwah, Michelle; Steet, Richard et al. (2016) Glycosylation and stem cells: Regulatory roles and application of iPSCs in the study of glycosylation-related disorders. Bioessays 38:1255-1265
Deligny, Audrey; Dierker, Tabea; Dagälv, Anders et al. (2016) NDST2 (N-Deacetylase/N-Sulfotransferase-2) Enzyme Regulates Heparan Sulfate Chain Length. J Biol Chem 291:18600-7
Durning, Sean P; Flanagan-Steet, Heather; Prasad, Nripesh et al. (2016) O-Linked β-N-acetylglucosamine (O-GlcNAc) Acts as a Glucose Sensor to Epigenetically Regulate the Insulin Gene in Pancreatic Beta Cells. J Biol Chem 291:2107-18
Sanda, Miloslav; Benicky, Julius; Wu, Jing et al. (2016) Increased sialylation of site specific O-glycoforms of hemopexin in liver disease. Clin Proteomics 13:24
LaMattina, Joseph W; Nix, David B; Lanzilotta, William Nicholas (2016) Radical new paradigm for heme degradation in Escherichia coli O157:H7. Proc Natl Acad Sci U S A 113:12138-12143
Hildebrandt, Emily R; Cheng, Michael; Zhao, Peng et al. (2016) A shunt pathway limits the CaaX processing of Hsp40 Ydj1p and regulates Ydj1p-dependent phenotypes. Elife 5:
Aoki-Kinoshita, Kiyoko; Agravat, Sanjay; Aoki, Nobuyuki P et al. (2016) GlyTouCan 1.0 - The international glycan structure repository. Nucleic Acids Res 44:D1237-42

Showing the most recent 10 out of 76 publications