title: GlycoFly: a database of Drosophila N-linked glycoproteins identified using SPEG--MS techniques.
abstract: Protein glycosylation affects cellular functions of the central nervous system (CNS). Its deficiency leads to neurological disorders such as ataxia, paralysis, learning disability, mental retardation, and memory loss. However, the glycoproteins that are responsible for these diseases are not well characterized. In this study, Drosophila melanogaster was used as a model organism to identify the N-glycosylated proteins and N-glycosylation sites of its CNS by means of proteomics. Adult fly heads were digested with chymotrypsin or trypsin and the N-linked glycopeptides were captured using solid phase extraction of N-linked glycopeptides (SPEG) technique followed by mass spectrometry (MS) analysis using LTQ OrbiTrap Velos. Three hundred and thirty new and 147 previously known glycoproteins were identified from 721 uniquely detected peptides that have 740 NXS/T glycosylation sites. The N-glycosylation sites were highly abundant in cell adhesion, ion channel, and ion binding molecules, which are important for nerve maturation, organ development, axon guidance, learning, and memory. Identification of the N-glycosylated sites of these proteins will enhance our knowledge of these proteins and serve as a basis for future studies to address the roles of these proteins in neurological function and disorders. A database for Drosophila N-linked glycopeptides ( http://betenbaugh.jhu.edu/GlycoFly ) has been established in this study as a resource for study of neurological disorders.
authors.affiliation: Department of Chemical and Biomolecular Engineering, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: Deniz
authors.initials: D
authors.lastname: Baycin-Hizal
authors.forename: Yuan
authors.initials: Y
authors.lastname: Tian
authors.forename: Ilhan
authors.initials: I
authors.lastname: Akan
authors.forename: Elena
authors.initials: E
authors.lastname: Jacobson
authors.forename: Dean
authors.initials: D
authors.lastname: Clark
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Chu
authors.forename: Karen
authors.initials: K
authors.lastname: Palter
authors.forename: Hui
authors.initials: H
authors.lastname: Zhang
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Betenbaugh
mesh_terms: D000818:Animals; D030562:Databases, Protein; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D004331:Drosophila melanogaster; D006023:Glycoproteins / Q000737:chemistry / Q000378:metabolism*; D009862:Online Systems; D010446:Peptide Fragments / Q000737:chemistry; D040901:Proteomics; D052616:Solid Phase Extraction / Q000379:methods*; D053719:Tandem Mass Spectrometry / Q000379:methods*
chemical_list: D029721:Drosophila Proteins; D006023:Glycoproteins; D010446:Peptide Fragments