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Quantifying Protein-Specific N-Glycome Profiles by Focused Protein and Immunoprecipitation Glycomics

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Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/79019

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)

Submitter: 坂本 直哉

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