Abstract
A growing evidence has accumulated that glycoproteins are known to be involved in various biological events such as cell recognition and differentiation. Protein and lipid glycosylation changes are observed during development, differentiation and importantly, numerous disease state. In order to clarify the mechanism by which sugar chains of glycoproteins undergo changes during myelination and certain neurological diseases of peripheral nerves, we have performed glycome analysis of glycan chains released from glycoproteins in peripheral nerves. "Glycome" is a term meaning the whole set of glycans produced by individual organisms, as the third bioinformative macromolecules to be elucidated next to the genome and proteome. Glycans were released by glycopeptidase-A digestion of glycopeptides derived from the glycoproteins in bovine or rat peripheral nerves, pyridylaminated and then mapped by two-dimensional (2D) HPLC; ion-exchange HPLC and followed by ODS-HPLC. Characterization of each glycan was performed by MALDI-TOF mass spectrometry before and after appropriate glycosidase digestions or solvolysis to remove sulfate. More than one hundred glycan species were assigned based on these methods. Most of the glycans were of hybrid-type oligosaccharide. Several novel sugars containing non sulfated or sulfated glucuronic acid, which is known as HNK-1 carbohydrate epitope, will be reported. [Jpn J Physiol 54 Suppl:S215 (2004)]
