Large-scale Identification of N-Glycosylated Proteins of Mouse Tissues and Construction of a Glycoprotein Database, GlycoProtDB
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- 作者：Hiroyuki Kaji ; Toshihide Shikanai ; Akiko Sasaki-Sawa ; Hongling Wen ; Mika Fujita ; Yoshinori Suzuki ; Daisuke Sugahara ; Hiromichi Sawaki ; Yoshio Yamauchi ; Takashi Shinkawa ; Masato Taoka ; Nobuhiro Takahashi ; Toshiaki Isobe ; Hisashi Narimatsu
- 刊名：Journal of Proteome Research
- 出版年：2012
- 出版时间：September 7, 2012
- 年：2012
- 卷：11
- 期：9
- 页码：4553-4566
- 全文大小：511K
- 年卷期：v.11,no.9(September 7, 2012)
- ISSN：1535-3907
文摘
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鈥揗S 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.