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NAME: Shelley Naylor

Identifying C-Mannosylated Proteins Involved in Neurite Migration

Glycosylation functions in a variety of ways including ligand recognition and a protein folding check point, ensuring that only proteins that are properly folded are transferred to the Golgi apparatus. Bonds resulting from glycosylation can be differentiated based on the nature of their sugar-peptide bonds including O-linked, N-linked, and the less commonly detected C-linked. Rather than forming carbon-oxygen or carbon-nitrogen bonds, a distinctive type of glycosylation, known as C-mannosylation, forms carbon-carbon bonds. The C-mannosylation modification involves the linkage of an α-mannose to the C2 carbon indole of tryptophan (Trp, W) through a carbon-carbon bond.

Organization of the neocortex relies heavily on the regulation of neuronal migration. The migration of neurons is dependent on proteins with the C-mannosylation modification for guidance cues. Proper neurite migration prevents neurological defects in humans. The understanding of the modification in neurite migration is significant because cell migration is an important step in the development of the nervous system.
Lectins are highly specific carbohydrate binding proteins. Galanthus nivalis lectin (GNL) specifically binds to α 1,3-mannose and α 1,6-mannose. GNL was used for the recognition of the C-mannosylation modification within a B35 glioblastoma cell sample. Disruption of the interaction between the GNL and C-mannosyltryptophan occurred by eluting the sample with guanidinium. Following this, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) was used as a protein separation technique.