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Title: Major glycan structure underlying expression of the Lewis X epitope in the developing brain is O-mannose-linked glycans on phosphacan/RPTPβ.
Authors: Yaji, Shohei
Manya, Hiroshi
Nakagawa, Naoki
Takematsu, Hiromu
Endo, Tamao
Kannagi, Reiji
Yoshihara, Toru  kyouindb  KAKEN_id
Asano, Masahide  kyouindb  KAKEN_id
Oka, Shogo  kyouindb  KAKEN_id
Author's alias: 岡, 昌吾
Keywords: Lewis X
O-mannosyl glycan
phosphacan (RPTPβ)
poly-N-acetyllactosamine
Issue Date: 31-Oct-2014
Publisher: Oxford University Press
Journal title: Glycobiology
Volume: 25
Issue: 4
Start page: 376
End page: 385
Abstract: Glycosylation is a major protein modification. Although proteins are glycosylated/further modulated by several glycosyltransferases during trafficking from the endoplasmic reticulum to the Golgi apparatus, a certain glycan epitope has only been detected on a limited number of proteins. Of these glycan epitopes, Lewis X is highly expressed in the early stage of a developing brain and plays important roles in cell-cell interaction. The Lewis X epitope is comprised of a trisaccharide (Galβ1-4 (Fucα1-3) GlcNAc), and a key enzyme for the expression of this epitope is α1, 3-fucosyltransferase 9. However, the scaffolding glycan structure responsible for the formation of the Lewis X epitope as well as its major carrier protein has not been fully characterized in the nervous system. Here we showed that the Lewis X epitope was mainly expressed on phosphacan/receptor protein tyrosine phosphatase β (RPTPβ) in the developing mouse brain. Expression of the Lewis X epitope was markedly reduced in β1, 4-galactosyltransferase 2 (β4GalT2) gene-deficient mice, which indicated that β4GalT2 is a major galactosyltransferase required for the Lewis X epitope. We also showed that the Lewis X epitope almost disappeared due to the knockout of protein O-mannose β1, 2-N-acetylglucosaminyltransferase 1, an N-acetylglucosaminyltransferase essential for the synthesis of O-mannosylated glycans, which indicated that the O-mannosylated glycan is responsible for presenting the Lewis X epitope. Since O-mannosylated glycans on phosphacan/RPTPβ could also present human natural killer-1, another glycan epitope specifically expressed in the nervous system, our results revealed the importance of O-mannosylated glycan chains in the presentation of functional glycan epitopes in the brain.
Rights: This is a pre-copyedited, author-produced PDF of an article accepted for publication in 'Glycobiology' following peer review. The version of record [Shohei Yaji, Hiroshi Manya, Naoki Nakagawa, Hiromu Takematsu, Tamao Endo, Reiji Kannagi, Toru Yoshihara, Masahide Asano, Shogo Oka. Major glycan structure underlying expression of the Lewis X epitope in the developing brain is O-mannose-linked glycans on phosphacan/RPTPβ. Glycobiology (2015) 25 (4): 376-385] is available online at: http://glycob.oxfordjournals.org/content/25/4/376.long
The full-text file will be made open to the public on 31 October 2015 in accordance with publisher's 'Terms and Conditions for Self-Archiving'.
この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。
This is not the published version. Please cite only the published version.
URI: http://hdl.handle.net/2433/200760
DOI(Published Version): 10.1093/glycob/cwu118
PubMed ID: 25361541
Appears in Collections:Journal Articles

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