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  1. Artikel ; Online: Ca

    Miyano, Kei / Kajikawa, Mizuho

    FEBS letters

    2023  Band 597, Heft 5, Seite(n) 702–713

    Abstract: Six gene splice variants of superoxide-generating NADPH oxidase 5 (Nox5) have been identified in humans, and they differ in the sequence of their N-terminal cytoplasmic domains, which comprise four EF-hand motifs. Here, we demonstrated that the ... ...

    Abstract Six gene splice variants of superoxide-generating NADPH oxidase 5 (Nox5) have been identified in humans, and they differ in the sequence of their N-terminal cytoplasmic domains, which comprise four EF-hand motifs. Here, we demonstrated that the Ca
    Mesh-Begriff(e) Humans ; NADPH Oxidase 5/genetics ; NADPH Oxidase 5/metabolism ; Membrane Proteins/metabolism ; NADPH Oxidases/metabolism ; Cell Membrane/metabolism ; Superoxides/metabolism ; Reactive Oxygen Species/metabolism
    Chemische Substanzen NADPH Oxidase 5 (EC 1.6.3.-) ; Membrane Proteins ; NADPH Oxidases (EC 1.6.3.-) ; Superoxides (11062-77-4) ; Reactive Oxygen Species ; NOX5 protein, human (EC 1.6.3.-)
    Sprache Englisch
    Erscheinungsdatum 2023-01-25
    Erscheinungsland England
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14577
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  2. Artikel ; Online: Ca2+‐binding‐region‐dependent cell surface localization of NADPH oxidase Nox5

    Miyano, Kei / Kajikawa, Mizuho

    FEBS Letters. 2023 Mar., v. 597, no. 5 p.702-713

    2023  

    Abstract: Six gene splice variants of superoxide‐generating NADPH oxidase 5 (Nox5) have been identified in humans, and they differ in the sequence of their N‐terminal cytoplasmic domains, which comprise four EF‐hand motifs. Here, we demonstrated that the Ca²⁺‐ ... ...

    Abstract Six gene splice variants of superoxide‐generating NADPH oxidase 5 (Nox5) have been identified in humans, and they differ in the sequence of their N‐terminal cytoplasmic domains, which comprise four EF‐hand motifs. Here, we demonstrated that the Ca²⁺‐dependent association and dissociation between the N‐ and C‐terminal cytoplasmic domains of the Nox5β variant are affected by the alanine substitution of the conserved Ile‐113 or Leu‐115 at the connecting loop between the third and fourth EF‐hand motifs. These substitutions impair the cell surface localization of Nox5β. In addition, the Nox5ε/S variant, lacking all EF‐hand motifs, does not localize to the plasma membrane. Thus, the Ca²⁺‐sensitive intramolecular interaction determines the Nox5 subcellular localization, that is, whether Nox5 variants generate superoxide in the extracellular or intracellular space.
    Schlagwörter NAD(P)H oxidase (H2O2-forming) ; alanine ; dissociation ; genes ; intracellular space ; plasma membrane
    Sprache Englisch
    Erscheinungsverlauf 2023-03
    Umfang p. 702-713.
    Erscheinungsort John Wiley & Sons, Ltd
    Dokumenttyp Artikel ; Online
    Anmerkung JOURNAL ARTICLE
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1002/1873-3468.14577
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  3. Artikel ; Online: Hypoxia stabilizes the H

    Matsunaga, Shogo / Kohda, Akira / Kamakura, Sachiko / Hayase, Junya / Miyano, Kei / Shiose, Akira / Sumimoto, Hideki

    Genes to cells : devoted to molecular & cellular mechanisms

    2023  Band 29, Heft 1, Seite(n) 63–72

    Abstract: The hydrogen peroxide ( ... ...

    Abstract The hydrogen peroxide (H
    Mesh-Begriff(e) Rats ; Animals ; NADPH Oxidase 4/genetics ; NADPH Oxidase 4/metabolism ; Oxidoreductases ; Myocytes, Cardiac/metabolism ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Hypoxia ; Autophagy ; Reactive Oxygen Species/metabolism
    Chemische Substanzen NADPH Oxidase 4 (EC 1.6.3.-) ; Oxidoreductases (EC 1.-) ; NADPH Oxidases (EC 1.6.3.-) ; Reactive Oxygen Species ; Nox4 protein, rat (EC 1.6.3.-)
    Sprache Englisch
    Erscheinungsdatum 2023-11-20
    Erscheinungsland England
    Dokumenttyp Journal Article
    ZDB-ID 1330000-3
    ISSN 1365-2443 ; 1356-9597
    ISSN (online) 1365-2443
    ISSN 1356-9597
    DOI 10.1111/gtc.13085
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  4. Artikel ; Online: Characterization of missense mutations in the NADPH oxidase partner p22

    Kawai, Chikage / Kajikawa, Mizuho / Yamauchi, Akira / Okamoto, Shuichiro / Kuribayashi, Futoshi / Miyano, Kei

    Microbiology and immunology

    2023  Band 67, Heft 4, Seite(n) 194–200

    Abstract: Defective superoxide production by NADPH oxidase 2 (Nox2) in phagocyte cells results in the development of chronic granulomatous disease (CGD), a hereditary disease characterized by recurrent and life-threatening infections. The partner protein ... ...

    Abstract Defective superoxide production by NADPH oxidase 2 (Nox2) in phagocyte cells results in the development of chronic granulomatous disease (CGD), a hereditary disease characterized by recurrent and life-threatening infections. The partner protein p22
    Mesh-Begriff(e) Cricetulus ; Animals ; Cell Line ; Humans ; NADPH Oxidases/chemistry ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Mutation, Missense ; NADPH Oxidase 2/metabolism
    Chemische Substanzen CYBA protein, human (EC 1.6.3.1) ; NADPH Oxidases (EC 1.6.3.-) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-)
    Sprache Englisch
    Erscheinungsdatum 2023-01-22
    Erscheinungsland Australia
    Dokumenttyp Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/1348-0421.13051
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  5. Artikel: Fine definition of the epitopes on the human gp91phox/NOX2 for the monoclonal antibodies CL-5 and 48

    Kawai, Chikage / Miyano, Kei / Okamoto, Shuichiro / Yamauchi, Akira / Kuribayashi, Futoshi

    Journal of immunological methods. 2022 Feb., v. 501

    2022  

    Abstract: Superoxide-producing NADPH oxidase, gp91ᵖʰᵒˣ/NOX2, in phagocytes plays a critical role in the host defenses against pathogens. Moreover, gp91ᵖʰᵒˣ/NOX2 contributes to the oxidative stress in endothelial cells. Therefore, investigating the level of ... ...

    Abstract Superoxide-producing NADPH oxidase, gp91ᵖʰᵒˣ/NOX2, in phagocytes plays a critical role in the host defenses against pathogens. Moreover, gp91ᵖʰᵒˣ/NOX2 contributes to the oxidative stress in endothelial cells. Therefore, investigating the level of gp91ᵖʰᵒˣ/NOX2 with immunoblotting is important for estimating the amount of superoxide produced. Here, we showed that the epitopes in human gp91ᵖʰᵒˣ/NOX2 recognized by monoclonal antibodies (mAbs) CL-5 and 48 were in amino acids 132–147 and 136–144, respectively. Although the epitopes were close to the N-glycosylation sites, N-glycan maturation did not affect mAbs recognition. When Pro-136 was substituted with Arg, the corresponding mouse residue, human gp91ᵖʰᵒˣ/NOX2 was not recognized by mAbs CL-5 and 48; however, the substitution did not affect gp91ᵖʰᵒˣ/NOX2-based oxidase activity. This finding explains why these mAbs specifically recognize the human but not mouse gp91ᵖʰᵒˣ/NOX2. Hence, these mAbs are useful for investigating the level of gp91ᵖʰᵒˣ/NOX2 without amino acid substitutions in the epitopes.
    Schlagwörter NAD(P)H oxidase (H2O2-forming) ; amino acids ; epitopes ; glycosylation ; humans ; immunoblotting ; mice ; oxidative stress
    Sprache Englisch
    Erscheinungsverlauf 2022-02
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 120142-6
    ISSN 1872-7905 ; 0022-1759
    ISSN (online) 1872-7905
    ISSN 0022-1759
    DOI 10.1016/j.jim.2021.113213
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  6. Artikel ; Online: Fine definition of the epitopes on the human gp91

    Kawai, Chikage / Miyano, Kei / Okamoto, Shuichiro / Yamauchi, Akira / Kuribayashi, Futoshi

    Journal of immunological methods

    2021  Band 501, Seite(n) 113213

    Abstract: Superoxide-producing NADPH oxidase, ... ...

    Abstract Superoxide-producing NADPH oxidase, gp91
    Mesh-Begriff(e) Animals ; Antibodies, Monoclonal/immunology ; Antibody Specificity ; CHO Cells ; COS Cells ; Chlorocebus aethiops ; Cricetulus ; Epitope Mapping ; Epitopes ; Glycosylation ; HL-60 Cells ; Humans ; Mice ; NADPH Oxidase 2/genetics ; NADPH Oxidase 2/immunology ; NADPH Oxidase 2/metabolism ; Protein Processing, Post-Translational ; RAW 264.7 Cells ; Receptors, Immunologic/genetics ; Receptors, Immunologic/immunology ; Receptors, Immunologic/metabolism ; Superoxides/metabolism
    Chemische Substanzen Antibodies, Monoclonal ; Epitopes ; Pirb protein, mouse ; Receptors, Immunologic ; Superoxides (11062-77-4) ; CYBB protein, human (EC 1.6.3.-) ; NADPH Oxidase 2 (EC 1.6.3.-)
    Sprache Englisch
    Erscheinungsdatum 2021-12-28
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 120142-6
    ISSN 1872-7905 ; 0022-1759
    ISSN (online) 1872-7905
    ISSN 0022-1759
    DOI 10.1016/j.jim.2021.113213
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  7. Artikel ; Online: Regulation of Derlin-1-mediated degradation of NADPH oxidase partner p22

    Miyano, Kei / Okamoto, Shuichiro / Kajikawa, Mizuho / Kiyohara, Takuya / Kawai, Chikage / Yamauchi, Akira / Kuribayashi, Futoshi

    Redox biology

    2022  Band 56, Seite(n) 102479

    Abstract: The transmembrane protein ... ...

    Abstract The transmembrane protein p22
    Mesh-Begriff(e) Granulomatous Disease, Chronic ; Humans ; Membrane Proteins/metabolism ; Mutant Proteins ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Reactive Oxygen Species/metabolism ; Serine ; Sulfhydryl Compounds
    Chemische Substanzen DERL1 protein, human ; Membrane Proteins ; Mutant Proteins ; Reactive Oxygen Species ; Sulfhydryl Compounds ; Serine (452VLY9402) ; NADPH Oxidases (EC 1.6.3.-) ; CYBA protein, human (EC 1.6.3.1)
    Sprache Englisch
    Erscheinungsdatum 2022-09-13
    Erscheinungsland Netherlands
    Dokumenttyp Journal Article
    ZDB-ID 2701011-9
    ISSN 2213-2317 ; 2213-2317
    ISSN (online) 2213-2317
    ISSN 2213-2317
    DOI 10.1016/j.redox.2022.102479
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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  8. Artikel ; Online: A basic charge cluster near the C-terminus of the cytoplasmic tail contributes to the molecular stability of human herpesvirus 8 E3 ubiquitin ligases.

    Kajikawa, Mizuho / Kato, Koya / Takahashi, Hayato / Kitajima, Seiya / Kusunoki, Yosuke / Haga, Mizuki / Kimura, Minako / Inoue, Yoshihiro / Miyano, Kei / Kanamoto, Taisei

    Microbiology and immunology

    2023  Band 67, Heft 6, Seite(n) 293–302

    Abstract: Human herpesvirus 8 (HHV8; also known as Kaposi's sarcoma-associated herpesvirus [KSHV]) utilizes the viral E3 ubiquitin ligase family members K3 and K5 for immune evasion. Both K3 and K5 mediate the ubiquitination of host MHC class I (MHC-I) molecules, ... ...

    Abstract Human herpesvirus 8 (HHV8; also known as Kaposi's sarcoma-associated herpesvirus [KSHV]) utilizes the viral E3 ubiquitin ligase family members K3 and K5 for immune evasion. Both K3 and K5 mediate the ubiquitination of host MHC class I (MHC-I) molecules, which play a key role in antigen presentation to cytotoxic T lymphocytes (CTLs). Because ubiquitinated MHC-I is immediately down-regulated from the cell surface, HHV8-infected cells can escape surveillance by CTLs. K3 and K5 have similar domain structures and topologies. They contain an N-terminal RINGv ubiquitin ligase domain, two transmembrane helices, and an intrinsically disordered cytoplasmic tail at the C-terminus. The cytoplasmic tail contains a membrane-proximal "conserved region" involved in ligase activity. On the other hand, the role of the membrane-distal region of the cytoplasmic tail, termed the "C-tail" in this study, remains unclear. Here, we demonstrate that the C-tail contributes to the protein expression of both K3 and K5. The C-tail-truncated K3 and K5 mutants were rapidly reduced in cells. The recombinant C-tail proteins bind to acidic lipids via a basic charge cluster located near the C-terminus of the C-tails. Similar to the C-tail-truncated mutants, the basic charge cluster-substituting mutants showed decreased protein expression of K3 and K5. These findings suggest that the basic charge cluster near the C-terminus of the cytoplasmic tail contributes to the molecular stability of K3 and K5.
    Mesh-Begriff(e) Humans ; Ubiquitin-Protein Ligases/genetics ; Ubiquitin-Protein Ligases/metabolism ; Herpesvirus 8, Human/genetics ; Herpesvirus 8, Human/metabolism ; Histocompatibility Antigens Class I/metabolism ; Ubiquitin/metabolism
    Chemische Substanzen Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Histocompatibility Antigens Class I ; Ubiquitin
    Sprache Englisch
    Erscheinungsdatum 2023-04-17
    Erscheinungsland Australia
    Dokumenttyp Journal Article
    ZDB-ID 224792-6
    ISSN 1348-0421 ; 0385-5600
    ISSN (online) 1348-0421
    ISSN 0385-5600
    DOI 10.1111/1348-0421.13068
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  9. Artikel: Coculture in vitro with endothelial cells induces cytarabine resistance of acute myeloid leukemia cells in a VEGF-A/VEGFR-2 signaling–independent manner

    Okamoto, Shuichiro / Miyano, Kei / Kitakaze, Keisuke / Kato, Hitomi / Yamauchi, Akira / Kajikawa, Mizuho / Itsumi, Momoe / Kawai, Chikage / Kuribayashi, Futoshi

    Biochemical and biophysical research communications. 2022 Jan. 08, v. 587

    2022  

    Abstract: An interaction between acute myeloid leukemia (AML) cells and endothelial cells in the bone marrow seems to play a critical role in chemosensitivity on leukemia treatment. The endothelial niche reportedly enhances the paracrine action of the soluble ... ...

    Abstract An interaction between acute myeloid leukemia (AML) cells and endothelial cells in the bone marrow seems to play a critical role in chemosensitivity on leukemia treatment. The endothelial niche reportedly enhances the paracrine action of the soluble secretory proteins responsible for chemoresistance in a vascular endothelial growth factor A (VEGF-A)/VEGF receptor 2 (VEGFR-2) signaling pathway–dependent manner. To further investigate the contribution of VEGF-A/VEGFR-2 signaling to the chemoresistance of AML cells, a biochemical assay system in which the AML cells were cocultured with human endothelial EA.hy926 cells in a monolayer was developed. By coculture with EA.hy926 cells, this study revealed that the AML cells resisted apoptosis induced by the anticancer drug cytarabine. SU4312, a VEGFR-2 inhibitor, attenuated VEGFR-2 phosphorylation and VEGF-A/VEGFR-2 signaling–dependent endothelial cell migration; thus, this inhibitor was observed to block VEGF-A/VEGFR-2 signaling. Interestingly, this inhibitor did not reverse the chemoresistance. When VEGFR-2 was knocked out in EA.hy926 cells using the CRISPR–Cas9 system, the cytarabine-induced apoptosis of AML cells did not significantly change compared with that of wild-type cells. Thus, coculture-induced chemoresistance appears to be independent of VEGF-A/VEGFR-2 signaling. When the transwell, a coculturing device, separated the AML cells from the EA.hy926 cells in a monolayer, the coculture-induced chemoresistance was inhibited. Given that the migration of VEGF-A/VEGFR-2 signaling–dependent endothelial cells is necessary for the endothelial niche formation in the bone marrow, VEGF-A/VEGFR-2 signaling contributes to chemoresistance by mediating the niche formation process, but not to the chemoresistance of AML cells in the niche.
    Schlagwörter CRISPR-Cas systems ; antineoplastic agents ; apoptosis ; bone marrow ; cell movement ; coculture ; endothelial cells ; humans ; myeloid leukemia ; phosphorylation ; research ; vascular endothelial growth factor A ; vascular endothelial growth factor receptor-2
    Sprache Englisch
    Erscheinungsverlauf 2022-0108
    Umfang p. 78-84.
    Erscheinungsort Elsevier Inc.
    Dokumenttyp Artikel
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2021.11.090
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  10. Artikel ; Online: Soluble Regulatory Proteins for Activation of NOX Family NADPH Oxidases.

    Sumimoto, Hideki / Minakami, Reiko / Miyano, Kei

    Methods in molecular biology (Clifton, N.J.)

    2019  Band 1982, Seite(n) 121–137

    Abstract: NOX family NADPH oxidases deliberately produce reactive oxygen species and thus contribute to a variety of biological functions. Of seven members in the human family, the three oxidases NOX2, NOX1, and NOX3 form a heterodimer with ... ...

    Abstract NOX family NADPH oxidases deliberately produce reactive oxygen species and thus contribute to a variety of biological functions. Of seven members in the human family, the three oxidases NOX2, NOX1, and NOX3 form a heterodimer with p22
    Mesh-Begriff(e) Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Enzyme Activation ; Humans ; Isoenzymes ; NADPH Oxidases/chemistry ; NADPH Oxidases/genetics ; NADPH Oxidases/metabolism ; Oxidation-Reduction ; Phagocytes/enzymology ; Phagocytes/metabolism ; Phagocytosis ; Protein Binding ; Protein Interaction Domains and Motifs ; Reactive Oxygen Species/metabolism
    Chemische Substanzen Carrier Proteins ; Isoenzymes ; Reactive Oxygen Species ; NADPH Oxidases (EC 1.6.3.-)
    Sprache Englisch
    Erscheinungsdatum 2019-06-06
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-4939-9424-3_8
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

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