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Extraction of Structural Extracellular Polymeric Substances from Aerobic Granular Sludge
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Structure and function of extracellular O-GlcNAc.

Mitsutaka Ogawa1, Tetsuya Okajima1

  • 1Department of Molecular Biochemistry, Nagoya University Graduate School of Medicine, 65 Tsurumai, Showa-ku, Nagoya 466-8550, Japan.

Current Opinion in Structural Biology
|January 23, 2019
PubMed
Summary
This summary is machine-generated.

Extracellular O-linked N-acetylglucosamine (O-GlcNAc) modification, catalyzed by EGF-domain specific O-GlcNAc transferase (EOGT), impacts vascular development and cell-matrix interactions in animals.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Developmental Biology

Background:

  • Extracellular O-GlcNAc is a unique post-translational modification found on epidermal growth factor (EGF) domain-containing glycoproteins.
  • This modification is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), an enzyme located within the endoplasmic reticulum lumen.

Purpose of the Study:

  • To review the current understanding of the structure and functions of extracellular O-GlcNAc in animal systems.
  • To highlight the role of EOGT in biological processes and disease.

Main Methods:

  • Literature review of studies on extracellular O-GlcNAc and EOGT.
  • Analysis of EOGT's role in human disease (Adams-Oliver syndrome) and animal models (Drosophila).

Main Results:

  • EOGT is implicated in Adams-Oliver syndrome, a human congenital disease.
  • EOGT regulates vascular development and integrity via Notch signaling in endothelial cells.
  • In Drosophila, Eogt affects cell-matrix interactions by modifying the Dumpy glycoprotein.

Conclusions:

  • Extracellular O-GlcNAc, mediated by EOGT, plays critical roles in animal development and physiology.
  • Further research into EOGT and extracellular O-GlcNAc is warranted for understanding vascular biology and congenital disorders.