Publication Name	World Journal of Biological Chemistry
Manuscript ID	7308
Country	Japan

Received	2013-11-13 08:09
Peer-Review Started	2013-11-14 10:00
To Make the First Decision	2013-12-10 14:39
Return for Revision	2013-12-17 16:57
Revised	2014-01-20 00:09
Second Decision	2014-04-09 16:30
Accepted by Journal Editor-in-Chief
Accepted by Executive Editor-in-Chief	2014-04-09 16:35
Articles in Press
Publication Fee Transferred
Edit the Manuscript by Language Editor
Typeset the Manuscript	2014-05-22 14:41
Publish the Manuscript Online	2014-06-11 10:30

ISSN	1949-8454 (online)
Open Access
Copyright
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Category	Biochemistry & Molecular Biology
Manuscript Type	Minireviews
Article Title	Extracellular O-linked β-N-acetylglucosamine: Its biology and relationship to human disease
Manuscript Source	Invited Manuscript
All Author List	Mitsutaka Ogawa, Koichi Furukawa and Tetsuya Okajima
Funding Agency and Grant Number	Funding Agency Grant Number grant-in-aid for Challenging Exploratory Research from the Japan Society for the Promotion of Science to Okajima T Scientific Research on Innovative Areas from the Ministry of Education, Culture, Sports, Science and Technology to Okajima T Takeda Foundation to Okajima T
Corresponding Author	Tetsuya Okajima, MD, PhD, Associate Professor, Department of Biochemistry Ⅱ, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-0065, Japan. tokajima@med.nagoya-u.ac.jp
Key Words	Extracellular O-linked β-N-acetylglucosamine; Notch; Adams-Oliver syndrome
Core Tip	The O-linked β-N-acetylglucosamine (O-GlcNAc) on extracellular protein domains is the most recently identified O-glycosylation of epidermal growth factor repeat-containing proteins such as Notch receptors. This O-GlcNAc modification occurs in the secretory pathway by an endoplasmic reticulum-resident O-GlcNAc transferase, extracellular O-linked β-N-acetylglucosamine (EOGT). In Drosophila, Dumpy, a membrane-tethered cuticle protein, was identified as a major O-GlcNAcylated protein that mediates the interaction between epithelial cells and the extracellular matrix. In mammals, extracellular O-GlcNAc was detected on Hspg2, Nell1, Lama5, Pamr1, and Notch receptors, although the physiological function of O-GlcNAc in mammals has not yet been elucidated. However, the recent finding that EOGT is a causative gene for Adams-Oliver syndrome provided important insights into the significance of extracellular O-GlcNAc in mammals. This review summarizes the current knowledge of extracellular O-GlcNAc and its implications in the pathological processes in Adams-Oliver syndrome.
Publish Date	2014-06-11 10:30
Citation	Ogawa M, Furukawa K, Okajima T. Extracellular O-linked β-N-acetylglucosamine: Its biology and relationship to human disease. World J Biol Chem 2014; 5(2): 224-230
URL	http://www.wjgnet.com/1949-8454/full/v5/i2/224.htm
DOI	http://dx.doi.org/10.4331/wjbc.v5.i2.224

Full Article (PDF)	wjbc-5-224.pdf
Full Article (Word)	wjbc-5-224.doc
Manuscript File	7308-Review.docx
Answering Reviewers	7308-Answering reviewers.pdf
Copyright License Agreement	7308-Copyright assignment.pdf
Non-Native Speakers of English Editing Certificate	7308-Language certificate.pdf
Peer-review Report	7308-Peer reviews.pdf
Scientific Editor Work List	7308-Scientific editor work list.doc