POMGNT1 Is Glycosylated by Mucin-Type O-Glycans

Biological & Pharmaceutical Bulletin
Xin XinTamao Endo

Abstract

Protein O-linked mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) is a Golgi glycosyltransferase that catalyzes the formation of the N-acetylglucosamine (GlcNAc) β1→2Man linkage of O-mannosyl glycan. POMGNT1 is not modified by N-glycans because there are no potential N-glycosylation sites; however, it is not clear whether POMGNT1 is modified by O-glycans. To determine whether POMGNT1 is O-glycosylated, we prepared recombinant human POMGNT1 from HEK293T cells. The recombinant POMGNT1 was recognized by Sambucus sieboldiana lectin (SSA), and sialidase digestion of POMGNT1 decreased SSA reactivity and enhanced the reactivity of Arachis hypogaea lectin (PNA). These results suggest that POMGNT1 is modified by a sialylated core-1 O-glycan. Next, we analyzed the structures of the O-glycans on POMGNT1 by β-elimination and pyrazolone-labeling methods in combination with mass spectrometry. We identified several mucin-type O-glycans containing (NeuAc)1(Hex)1(HexNAc)1, (NeuAc)2(Hex)1(HexNAc)1, and (NeuAc)2(Hex)2(HexNAc)2. To examine whether the O-glycans affect the functions and properties of POMGNT1, we compared glycosylated and non-glycosylated forms of recombinant sPOMGNT1 for their activity and surface hydrophobicity using the h...Continue Reading

References

Jun 6, 2003·Biochemical and Biophysical Research Communications·Hiroshi ManyaTamao Endo
Jun 23, 2004·Biochemical and Biophysical Research Communications·Keiko Akasaka-ManyaTamao Endo
Oct 13, 2006·Biochemical and Biophysical Research Communications·Hui XiongTatsushi Toda
Jan 4, 2008·Pharmaceutical Research·Andrea HaweWim Jiskoot
Apr 8, 2011·Neoplasia : an International Journal for Oncology Research·Jae-Hyun ParkYusuke Nakamura
Dec 14, 2011·Cell Metabolism·Adriaan G HolleboomJan Albert Kuivenhoven
Nov 9, 2014·Journal of Biochemistry·Tamao Endo
Nov 28, 2014·Science Signaling·Catherine R WasserJoachim Herz

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Citations

Feb 26, 2016·Human Molecular Genetics·Mingchu XuRui Chen

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