2016 Participants
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NAME: Nicholas Kegley

C-mannosylation is a type of glycolysis in which the sugar mannose forms a carbon-carbon bond with the first tryptophan in trp-xaa-xaa-trp sequences. Many proteins that are instrumental in the process of inflammation have been found to possess C-mannosyltryptophan. Hsc70 is a protein that has been found to interact with C-mannosyltyptophan. The interaction of this C-mannosylated protein has been found to increase the production of TNF-α in macrophages, which can result in a strong inflammatory response, potentially leading to sepsis if unregulated. To a certain degree, this can be fatal. This research concerns the discovery of other proteins that are involved in this process through the use of Galanthus nivalis lectin (GNL) within lipopolysaccharide (LPS) induced signaling within macrophage-like RAW264.7 cells. These cells will be affected by LPS signaling, which will increase the production of TNF-α within the cell. C-linked glycosylation affects this signaling so GNL can be used to target those proteins that possess this modification. The outcome of this research is projected to result in the discovery of proteins that will bind to the C-mannosyltryptophan that are also instrumental in the regulation and initiation of inflammation, like Hsc70. These discoveries could open the doors to more research regarding this mechanism of action, as well as expanding the search for more Hsc70 binding candidates.

 

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