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  1. Article ; Online: Inhibitory machinery for the functional dystroglycan glycosylation.

    Kondo, Yuji / Okajima, Tetsuya

    Journal of biochemistry

    2023  Volume 173, Issue 5, Page(s) 333–335

    Abstract: Dystroglycan (DG), a muscular transmembrane protein, plays a critical role in transducing extracellular matrix-derived signals to the cytoskeleton and provides physical strength to skeletal muscle cell membranes. The extracellular domain of DG, α-DG, ... ...

    Abstract Dystroglycan (DG), a muscular transmembrane protein, plays a critical role in transducing extracellular matrix-derived signals to the cytoskeleton and provides physical strength to skeletal muscle cell membranes. The extracellular domain of DG, α-DG, displays unique glycosylation patterns. Fully functional glycosylation is required for this domain to interact with components of extracellular matrices, including laminin. One of the unique sugar compositions found in such functional glycans on DG is two ribitol phosphates that are transferred by the sequential actions of fukutin (FKTN) and fukutin-related protein (FKRP), which use CDP-ribitol as a donor substrate. These are then further primed for matriglycan biosynthesis. A recent in vitro study reported that glycerol phosphate could be similarly added to α-DG by FKTN and FKRP if they used CDP-glycerol (CDP-Gro) as a donor substrate. However, the physiological relevance of these findings remains elusive. Imae et al. addressed the knowledge gap regarding whether CDP-Gro is present in mammals and how CDP-Gro is synthesized and functions in mammals.
    MeSH term(s) Animals ; Dystroglycans/metabolism ; Glycerol ; Glycosylation ; Pentosyltransferases/metabolism ; Ribitol/metabolism ; Ribitol/pharmacology
    Chemical Substances Dystroglycans (146888-27-9) ; Glycerol (PDC6A3C0OX) ; Pentosyltransferases (EC 2.4.2.-) ; Ribitol (488-81-3)
    Language English
    Publishing date 2023-02-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 218073-x
    ISSN 1756-2651 ; 0021-924X
    ISSN (online) 1756-2651
    ISSN 0021-924X
    DOI 10.1093/jb/mvad003
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.202: Show issues Location:
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  2. Article ; Online: Efficient Escorting Strategy for Aggregation-Prone Notch EGF Repeats with Sparcl1.

    Kondo, Yuji / Li, Yuxin / Okajima, Tetsuya

    Molecules (Basel, Switzerland)

    2024  Volume 29, Issue 5

    Abstract: Epidermal growth factor (EGF) repeats are present in various proteins and form well-defined structures with three disulfide bonds. One representative protein is the Notch receptor. Each EGF repeat contains unique ... ...

    Abstract Epidermal growth factor (EGF) repeats are present in various proteins and form well-defined structures with three disulfide bonds. One representative protein is the Notch receptor. Each EGF repeat contains unique atypical
    MeSH term(s) Humans ; Animals ; Mice ; Epidermal Growth Factor/chemistry ; HEK293 Cells ; Receptors, Notch/metabolism ; Receptor, Notch1/chemistry ; Acetylglucosamine/metabolism ; Calcium-Binding Proteins ; Extracellular Matrix Proteins/metabolism
    Chemical Substances Epidermal Growth Factor (62229-50-9) ; Receptors, Notch ; Receptor, Notch1 ; Acetylglucosamine (V956696549) ; Sparcl1 protein, mouse ; Calcium-Binding Proteins ; Extracellular Matrix Proteins
    Language English
    Publishing date 2024-02-27
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules29051031
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    Zs.MO 81: Show issues

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  3. Article ; Online: Notch signaling: A sweet strategy.

    Okajima, Tetsuya

    Nature chemical biology

    2017  Volume 14, Issue 1, Page(s) 3–4

    MeSH term(s) Fucose ; Receptors, Notch ; Signal Transduction
    Chemical Substances Receptors, Notch ; Fucose (28RYY2IV3F)
    Language English
    Publishing date 2017-12-08
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/nchembio.2532
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  4. Article ; Online: Significant Roles of Notch

    Wang, Weiwei / Okajima, Tetsuya / Takeuchi, Hideyuki

    Molecules (Basel, Switzerland)

    2022  Volume 27, Issue 6

    Abstract: Notch signaling, which was initially identified ... ...

    Abstract Notch signaling, which was initially identified in
    MeSH term(s) Animals ; Fucose/chemistry ; Glycosylation ; N-Acetylglucosaminyltransferases/metabolism ; Neoplasms ; Receptors, Notch/metabolism
    Chemical Substances Receptors, Notch ; Fucose (28RYY2IV3F) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2022-03-09
    Publishing country Switzerland
    Document type Journal Article ; Review
    ZDB-ID 1413402-0
    ISSN 1420-3049 ; 1431-5165 ; 1420-3049
    ISSN (online) 1420-3049
    ISSN 1431-5165 ; 1420-3049
    DOI 10.3390/molecules27061783
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    Zs.MO 81: Show issues

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  5. Article ; Online: Current Views on the Roles of

    Saiki, Wataru / Ma, Chenyu / Okajima, Tetsuya / Takeuchi, Hideyuki

    Biomolecules

    2021  Volume 11, Issue 2

    Abstract: The 100th anniversary of Notch discovery ... ...

    Abstract The 100th anniversary of Notch discovery in
    MeSH term(s) Animals ; Glycosylation ; Humans ; Mass Spectrometry ; Protein Binding ; Receptors, Notch/genetics ; Receptors, Notch/metabolism
    Chemical Substances Receptors, Notch
    Language English
    Publishing date 2021-02-18
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2701262-1
    ISSN 2218-273X ; 2218-273X
    ISSN (online) 2218-273X
    ISSN 2218-273X
    DOI 10.3390/biom11020309
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  6. Article ; Online: Structure and function of extracellular O-GlcNAc.

    Ogawa, Mitsutaka / Okajima, Tetsuya

    Current opinion in structural biology

    2019  Volume 56, Page(s) 72–77

    Abstract: Extracellular O-GlcNAc is a unique modification restricted to the epidermal growth factor (EGF) domain-containing glycoproteins. This O-GlcNAcylation is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), which is localized in the lumen of ... ...

    Abstract Extracellular O-GlcNAc is a unique modification restricted to the epidermal growth factor (EGF) domain-containing glycoproteins. This O-GlcNAcylation is catalyzed by the EGF-domain specific O-GlcNAc transferase (EOGT), which is localized in the lumen of endoplasmic reticulum. In humans, EOGT is one of the causative genes of a congenital disease, Adams-Oliver syndrome. EOGT is highly expressed in endothelial cells and regulates vascular development and integrity by potentiating Delta-like ligand-mediated Notch signaling. In Drosophila, Eogt modifies Dumpy, an apical extracellular matrix glycoprotein, and affects Dumpy-dependent cell-matrix interaction. In this review, we summarize the current findings of the structure and functions of extracellular O-GlcNAc in animals.
    MeSH term(s) Acetylglucosamine/chemistry ; Acetylglucosamine/metabolism ; Amino Acid Sequence ; Animals ; Epidermal Growth Factor/chemistry ; Epidermal Growth Factor/metabolism ; Extracellular Space/metabolism ; Humans ; Protein Domains
    Chemical Substances Epidermal Growth Factor (62229-50-9) ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2019-01-19
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1068353-7
    ISSN 1879-033X ; 0959-440X
    ISSN (online) 1879-033X
    ISSN 0959-440X
    DOI 10.1016/j.sbi.2018.12.002
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    Zs.A 3206: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  7. Article ; Online: Evidence that only EWS among the FET proteins acquires a low partitioning property for the hyperosmotic stress response by O-GlcNAc glycosylation on its low-complexity domain.

    Kakuo, Manami / Horii, Takeshi / Tonomura, Naoto / Sato, Runa / Ogawa, Mitsutaka / Okajima, Tetsuya / Kamemura, Kazuo

    Experimental cell research

    2023  Volume 424, Issue 1, Page(s) 113504

    Abstract: FET proteins (FUS, EWS, and TAF15) share a common domain organization, bind RNA/DNA, and perform similarly multifunctional roles in the regulation of gene expression. Of the FET proteins, however, only EWS appears to have a distinct property in the ... ...

    Abstract FET proteins (FUS, EWS, and TAF15) share a common domain organization, bind RNA/DNA, and perform similarly multifunctional roles in the regulation of gene expression. Of the FET proteins, however, only EWS appears to have a distinct property in the cellular stress response. Therefore, we focused on the relationship between hyperosmotic stress response and post-translational modifications of the FET proteins. We confirmed that the hyperosmotic stress-dependent translocation from the nucleus to the cytoplasm and the cellular granule formation of FET proteins, and that EWS is less likely to partition into cellular granules in the cytoplasm than FUS or TAF15. The domain involved in the less partitioning property of EWS was found to be its low-complexity domain (LCD). Chemoenzymatic labeling analysis of O-linked β-N-acetylglucosamine (O-GlcNAc) residues revealed that O-GlcNAc glycosylation occurs frequently in the LCD of EWS. A correlation was observed between the glycosylation of EWS and the less partitioning property under the hyperosmotic stress. These results suggest that among the FET proteins, only EWS has acquired the unique property through O-GlcNAc glycosylation. The glycosylation may play an essential role in regulating physiological functions of EWS, such as transcriptional activity, in addition to the property in cellular stress response.
    MeSH term(s) Glycosylation ; RNA-Binding Protein EWS/genetics ; RNA-Binding Protein EWS/metabolism ; Protein Processing, Post-Translational ; Cytoplasmic Granules/metabolism ; Cytoplasm/metabolism ; Acetylglucosamine/metabolism
    Chemical Substances RNA-Binding Protein EWS ; Acetylglucosamine (V956696549)
    Language English
    Publishing date 2023-02-02
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1493-x
    ISSN 1090-2422 ; 0014-4827
    ISSN (online) 1090-2422
    ISSN 0014-4827
    DOI 10.1016/j.yexcr.2023.113504
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    Zs.A 563: Show issues Location:
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  8. Article ; Online: Dissection and Whole Mount Staining of Retina from Neonatal Mice.

    Ogawa, Mitsutaka / Okajima, Tetsuya

    Bio-protocol

    2018  Volume 8, Issue 19, Page(s) e3034

    Abstract: Here we provide a detailed protocol for whole mount staining of mouse retina. This protocol was used to analyze retinal angiogenesis in newborn mice ( ... ...

    Abstract Here we provide a detailed protocol for whole mount staining of mouse retina. This protocol was used to analyze retinal angiogenesis in newborn mice ( Sawaguchi
    Language English
    Publishing date 2018-10-05
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2833269-6
    ISSN 2331-8325 ; 2331-8325
    ISSN (online) 2331-8325
    ISSN 2331-8325
    DOI 10.21769/BioProtoc.3034
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  9. Article ; Online: Congenital diseases caused by defective

    Tashima, Yuko / Okajima, Tetsuya

    Nagoya journal of medical science

    2018  Volume 80, Issue 3, Page(s) 299–307

    Abstract: The Notch signaling pathway is highly conserved and essential for animal development. It is required for cell differentiation, survival, and proliferation. Regulation of Notch signaling is a crucial process for human health. Ligands initiate a signal ... ...

    Abstract The Notch signaling pathway is highly conserved and essential for animal development. It is required for cell differentiation, survival, and proliferation. Regulation of Notch signaling is a crucial process for human health. Ligands initiate a signal cascade by binding to Notch receptors expressed on a neighboring cell. Notch receptors interact with ligands through their epidermal growth factor-like repeats (EGF repeats). Most EGF repeats are modified by
    MeSH term(s) Animals ; Ectodermal Dysplasia/metabolism ; Epidermal Growth Factor/metabolism ; Glycosylation ; Humans ; Limb Deformities, Congenital/metabolism ; N-Acetylglucosaminyltransferases/metabolism ; Receptors, Notch/metabolism ; Scalp Dermatoses/congenital ; Scalp Dermatoses/metabolism
    Chemical Substances Receptors, Notch ; Epidermal Growth Factor (62229-50-9) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-)
    Language English
    Publishing date 2018-09-13
    Publishing country Japan
    Document type Journal Article ; Review
    ZDB-ID 193148-9
    ISSN 2186-3326 ; 0027-7622
    ISSN (online) 2186-3326
    ISSN 0027-7622
    DOI 10.18999/nagjms.80.3.299
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  10. Article: Secretory expression of mammalian NOTCH tandem epidermal growth factor-like repeats based on increased O-glycosylation

    Zhang, Ailing / Tsukamoto, Yohei / Takeuchi, Hideyuki / Nishiwaki, Kimitoshi / Tashima, Yuko / Okajima, Tetsuya

    Analytical biochemistry. 2022 Nov. 01, v. 656

    2022  

    Abstract: The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell–to–cell communication during development. Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential ... ...

    Abstract The Notch pathway represents evolutionarily conserved intercellular signaling essential for cell–to–cell communication during development. Dysregulation of Notch signaling has been implicated in various diseases, and its control represents a potential cancer treatment strategy. Notch signaling is initiated by the interaction of NOTCH receptors with their ligands on neighboring cells. Therefore, the truncated NOTCH ectodomain, composed mainly of tandem repeats of epidermal growth factor-like (EGF) domains, serves as a decoy molecule that competes for ligand binding and thus inhibits ligand-dependent Notch signaling. Although full-length NOTCH EGF repeats exhibited potent Notch inhibitory activity, they were poorly produced in the transfected cells. This study evaluated the effect of EGF domain-modifying glycosyltransferases on the secretion of NOTCH EGF repeats. Our results in HEK293T cells revealed that, unlike the effect on endogenous NOTCH receptors, overexpressed EGF domain-specific O-GlcNAc transferase (EOGT) markedly enhanced the secretion of NOTCH1 EGF repeats in an enzyme activity-dependent manner. The co-expression of protein O-glucosyltransferase 1 further manifested the effect of EOGT. The resultant changes in O-glycosylation of NOTCH3 were evaluated by label-free glycopeptide quantification. This study provides an experimental strategy to efficiently generate NOTCH EGF repeats by manipulating the expression of glycosyltransferases that alter the O-glycosylation of EGF domains.
    Keywords cancer therapy ; cell communication ; glycopeptides ; glycosylation ; glycosyltransferases ; ligands ; mammals ; secretion
    Language English
    Dates of publication 2022-1101
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2022.114881
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    Z 70/124: Show issues

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