The Mass Spectrometry society of Japan - The 68th Annual Conference on Mass Spectrometry, Japan
Japanese

Abstract

Table of contents

Timetable

Plenary Lectures

Award Lecture

Oral Sessions (Day1, Day2, Day3)

Poster Presentations (Day1, Day2, Day3)

Panel Discussion

Luncheon Seminars (Day1, Day2, Day3)

Corporate Program

Poster Presentations

Day 2, June 23（Thu.）　　Room P (501, 502 and 503)

2P-26　　PDF

Glycoproteome Profiling for Subclassification of Extracellular Vesicles

(1Kyoto Univ., 2NIBIOHN, 3Kyoto Univ.)
oEisuke Kanao1,2, Shuntaro Wada3, Takuya Kubo3, Koji Otsuka3, Kazunari Akiyoshi3, Jun Adachi1,2, Yasushi Ishihama1,2

In this study, we focus on the specific separation of extracellular vesicles (EVs) by recognizing glycans on their surfaces. As a typical separation based on glycans, lectin affinity chromatography (LAC), which is currently used to purify glycoproteins, is usually employed. However, the pore size of the LAC packing material is relatively small, so the use of such materials is not suitable for the separation of EVs having over 100 nm in diameter. To achieve an effective EV separation, a spongy-like monolith (SPM), which consists of poly(ethylene-co-glycidyl methacrylate) (PEGM), is expected as a separation medium for LAC. In this study, we prepared two kinds of LAC columns made of the SPMs, immobilized with Sambucus sieboldiana lectin (SSA) or Concanavalin A (ConA). As a result, glycoproteins and liposomes effectively interacted with their respective lectins. Finally, the lectin-immobilized SPMs were employed to separate EVs, and then their different proteome profiles were determined by LC/MS/MS. These results demonstrate the heterogeneity of EVs based on their surface glycans.