title: Large-scale identification of N-glycosylated proteins of mouse tissues and construction of a glycoprotein database, GlycoProtDB.
abstract: Protein glycosylation is a common post-translational modification that plays important roles in terms of protein function. However, analyzing the relationship between glycosylation and protein function remains technically challenging. This problem arises from the fact that the attached glycans possess diverse and heterogeneous structures. We believe that the first step to elucidate glycan function is to systematically determine the status of protein glycosylation under physiological conditions. Such studies involve analyzing differences in glycan structure on cell type (tissue), sex, and age, as well as changes associated with perturbations as a result of gene knockout of glycan biosynthesis-related enzyme, disease and drug treatment. Therefore, we analyzed a series of glycoproteomes in several mouse tissues to identify glycosylated proteins and their glycosylation sites. Comprehensive analysis was performed by lectin- or HILIC-capture of glycopeptide subsets followed by enzymatic deglycosylation in stable isotope-labeled water (H₂¹⁸O, IGOT) and finally LC-MS analyses. In total, 5060 peptides derived from 2556 glycoproteins were identified. We then constructed a glycoprotein database, GlycoProtDB, using our experimental-based information to facilitate future studies in glycobiology.
authors: Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba Central-2, Umezono 1-1-1, Tsukuba, Ibaraki 305-8568, Japan. kaji-cmg@aist.go.jp
authors: Hiroyuki
authors: H
authors: Kaji
authors: Toshihide
authors: T
authors: Shikanai
authors: Akiko
authors: A
authors: Sasaki-Sawa
authors: Hongling
authors: H
authors: Wen
authors: Mika
authors: M
authors: Fujita
authors: Yoshinori
authors: Y
authors: Suzuki
authors: Daisuke
authors: D
authors: Sugahara
authors: Hiromichi
authors: H
authors: Sawaki
authors: Yoshio
authors: Y
authors: Yamauchi
authors: Takashi
authors: T
authors: Shinkawa
authors: Masato
authors: M
authors: Taoka
authors: Nobuhiro
authors: N
authors: Takahashi
authors: Toshiaki
authors: T
authors: Isobe
authors: Hisashi
authors: H
authors: Narimatsu
mesh_terms: D000818:Animals; D002853:Chromatography, Liquid; D030562:Databases, Protein; D054794:Glycomics; D006023:Glycoproteins / Q000032:analysis* / Q000097:blood / Q000737:chemistry; D008297:Male; D013058:Mass Spectrometry; D051379:Mice; D008810:Mice, Inbred C57BL; D009928:Organ Specificity; D020543:Proteome / Q000032:analysis* / Q000737:chemistry; D014584:User-Computer Interface
chemical_list: D006023:Glycoproteins; D020543:Proteome