Title: | Quantifying Protein-Specific N-Glycome Profiles by Focused Protein and Immunoprecipitation Glycomics |
Authors: | Kobayashi, Takashi Browse this author |
Ogawa, Koji Browse this author →KAKEN DB |
Furukawa, Jun-ichi Browse this author →KAKEN DB |
Hanamatsu, Hisatoshi Browse this author →KAKEN DB |
Hato, Megumi Browse this author |
Yoshinaga, Tomoyo Browse this author |
Morikawa, Kenichi Browse this author |
Suda, Goki Browse this author →KAKEN DB |
Sho, Takuya Browse this author |
Nakai, Masato Browse this author |
Higashino, Kenichi Browse this author |
Numata, Yoshito Browse this author |
Shinohara, Yasuro Browse this author |
Sakamoto, Naoya Browse this author →KAKEN DB |
Keywords: | biomarker |
glycomics |
fucosylation |
alpha-1 antitrypsin |
ceruloplasmin |
NASH |
MALDI-TOF MS |
Issue Date: | Aug-2019 |
Publisher: | American Chemical Society |
Journal Title: | Journal of proteome research |
Volume: | 18 |
Issue: | 8 |
Start Page: | 3133 |
End Page: | 3141 |
Publisher DOI: | 10.1021/acs.jproteome.9b00232 |
PMID: | 31266306 |
Abstract: | Serum N-glycans have been reported to be potential diagnostic and therapeutic biomarkers for many diseases and conditions, such as inflammation, fibrosis, and cancer progression. We previously described the focused protein glycomic analysis (FPG) from gel-separated serum proteins. With this methodology, we sought novel glycan biomarkers for nonalcoholic steatohepatitis (NASH) and successfully identified some N-glycans that were significantly elevated in NASH patients compared to nonalcoholic fatty liver patients. Among them, trisialylated monofucosylated triantennary glycan (A3F) of alpha-1 antitrypsin showed the most dynamic change. For rapid identification of N-glycans on the focused proteins, we constructed a simplified method called immunoprecipitation glycomics (IPG), where the target proteins were immunoprecipitated with affinity beads and subsequently subjected to glycomic analysis by MALDI-TOF MS. Focusing on alpha-1 antitrypsin and ceruloplasmin as the target proteins, we compared the values of N-glycans determined by FPG and IPG. The quantified values of each N-glycan by these two methods showed a statistically significant correlation, indicating that high throughput and quantitative N-glycomics of targeted proteins can be achieved by the simplified IPG method. Thus, an analytical strategy combining FPG and IPG can be adapted to general biomarker discovery and validation in appropriate disease areas. |
Rights: | This document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of proteome research, copyright c American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see https://doi.org/10.1021/acs.jproteome.9b00232. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/79019 |
Appears in Collections: | 医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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