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

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Oral Sessions

Day 3, May 21（Fri.）　15:45-16:05　Room B (Zoom)

3B-O12-1545　　PDF

O-Glycosylation Analysis of Amyloid Precursor Protein 770 Produced in HEK293T Cells by LC/MS/MS

(1Yokohama City Univ., 2Fukushima Medical Univ.)
oDaisuke Takakura1, Saori Miura2, Shinobu Kitazume2, Nana Kawasaki1

O-glycosylation analysis of amyloid precursor protein 770 (APP770) produced in HEK293T cells was performed by LC/MS/MS of enriched glycopeptides, and 6 O-glycosylated peptide regions (aa269-288, aa352-359, aa364-377, aa378-393, aa649-662, and aa663-670) were successfully identified. Among then, a total of 10 O-glycosylation sites were identified by an additional LC/MS/MS of OpeRATOR-treated glycosylated peptides. Interestingly, the more frequently occurring forms attached to three peptide regions (aa269-288, aa364-377, aa649-662) were Tn (GalNAc) and T (core 1) antigens.