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  1. Article ; Online: The combination of levodopa with levodopa-metabolizing enzyme inhibitors prevents severe fever with thrombocytopenia syndrome virus infection in vitro more effectively than single levodopa.

    Ogawa, Motohiko / Murae, Mana / Mizukami, Tomoharu / Gemba, Ryutaro / Irie, Takuya / Shimojima, Masayuki / Ebihara, Hideki / Noguchi, Kohji / Fukasawa, Masayoshi

    Journal of infection and chemotherapy : official journal of the Japan Society of Chemotherapy

    2023  Volume 29, Issue 5, Page(s) 549–553

    Abstract: Severe fever with thrombocytopenia syndrome is a hemorrhagic fever caused by a tick-borne infection. The causative agent, Dabie bandavirus, is also called the severe fever with thrombocytopenia syndrome virus (SFTSV). Ogawa et al. (2022) reported that ... ...

    Abstract Severe fever with thrombocytopenia syndrome is a hemorrhagic fever caused by a tick-borne infection. The causative agent, Dabie bandavirus, is also called the severe fever with thrombocytopenia syndrome virus (SFTSV). Ogawa et al. (2022) reported that levodopa, an antiparkinsonian drug with an o-dihydroxybenzene backbone, which is important for anti-SFTSV activity, inhibited SFTSV infection. Levodopa is metabolized by dopa decarboxylase (DDC) and catechol-O-methyltransferase (COMT) in vivo. We evaluated the anti-SFTSV efficacy of two DDC inhibitors, benserazide hydrochloride and carbidopa, and two COMT inhibitors, entacapone and nitecapone, which also have an o-dihydroxybenzene backbone. Only DDC inhibitors inhibited SFTSV infection with pretreatment of the virus (half-maximal inhibitory concentration [IC
    MeSH term(s) Humans ; Levodopa/pharmacology ; Levodopa/therapeutic use ; Carbidopa ; Catechol O-Methyltransferase/metabolism ; Severe Fever with Thrombocytopenia Syndrome/drug therapy ; Catechols/pharmacology ; Catechols/therapeutic use ; Enzyme Inhibitors/therapeutic use ; Phlebovirus
    Chemical Substances Levodopa (46627O600J) ; entacapone (4975G9NM6T) ; Carbidopa (MNX7R8C5VO) ; Catechol O-Methyltransferase (EC 2.1.1.6) ; Catechols ; Enzyme Inhibitors
    Language English
    Publishing date 2023-03-03
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 1355399-9
    ISSN 1437-7780 ; 1341-321X
    ISSN (online) 1437-7780
    ISSN 1341-321X
    DOI 10.1016/j.jiac.2023.02.017
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5236: Show issues Location:
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  2. Article ; Online: CUB and Sushi multiple domains 3 regulates dendrite development.

    Mizukami, Tomoharu / Kohno, Takao / Hattori, Mitsuharu

    Neuroscience research

    2016  Volume 110, Page(s) 11–17

    Abstract: CUB and Sushi multiple domains 3 (CSMD3) is a large protein expressed in fetal and adult brain. Recently, mutations of the CSMD3 gene were identified in schizophrenia and autism patients. However, biochemical properties and functions of the CSMD3 protein ...

    Abstract CUB and Sushi multiple domains 3 (CSMD3) is a large protein expressed in fetal and adult brain. Recently, mutations of the CSMD3 gene were identified in schizophrenia and autism patients. However, biochemical properties and functions of the CSMD3 protein remain unknown. Here, we demonstrate that CSMD3 is an oligomeric type I transmembrane protein localized in the apical dendrites of hippocampal pyramidal neurons in the postnatal brain. In cultured hippocampal neurons, CSMD3 is expressed only after 7 days in vitro. Overexpression of CSMD3 induced dendritic branching in hippocampal neurons. Regulation of dendritic morphology by CSMD3 depended on the presence of its extracellular region, while CSMD3 intracellular region was dispensable for this activity. These results suggest that CSMD3 acts as a co-receptor of an unidentified membrane protein to regulate dendrite development. Therefore, malfunctions of CSMD3 may be one of the factors in the pathogenesis of psychiatric disorders.
    MeSH term(s) Animals ; Cells, Cultured ; Dendrites/metabolism ; Dendrites/ultrastructure ; Hippocampus/metabolism ; Hippocampus/ultrastructure ; Membrane Proteins/metabolism ; Membrane Proteins/physiology ; Mice, Inbred ICR ; Nerve Tissue Proteins/physiology ; Neurons/metabolism ; Neurons/ultrastructure
    Chemical Substances CSMD3 protein, mouse ; Membrane Proteins ; Nerve Tissue Proteins
    Language English
    Publishing date 2016-09
    Publishing country Ireland
    Document type Journal Article
    ZDB-ID 605842-5
    ISSN 1872-8111 ; 0168-0102 ; 0921-8696
    ISSN (online) 1872-8111
    ISSN 0168-0102 ; 0921-8696
    DOI 10.1016/j.neures.2016.03.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1993: Show issues Location:
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  3. Article ; Online: A single mutation in the E2 glycoprotein of hepatitis C virus broadens the claudin specificity for its infection.

    Shirasago, Yoshitaka / Fukazawa, Hidesuke / Nagase, Shotaro / Shimizu, Yoshimi / Mizukami, Tomoharu / Wakita, Takaji / Suzuki, Tetsuro / Tani, Hideki / Kondoh, Masuo / Kuroda, Takuya / Yasuda, Satoshi / Sato, Yoji / Hanada, Kentaro / Fukasawa, Masayoshi

    Scientific reports

    2022  Volume 12, Issue 1, Page(s) 20243

    Abstract: Entry of the hepatitis C virus (HCV) into host cells is a multistep process mediated by several host factors, including a tight junction protein claudin-1 (CLDN1). We repeatedly passaged HCV-JFH1-tau, an HCV substrain with higher infectivity, on Huh7.5.1- ...

    Abstract Entry of the hepatitis C virus (HCV) into host cells is a multistep process mediated by several host factors, including a tight junction protein claudin-1 (CLDN1). We repeatedly passaged HCV-JFH1-tau, an HCV substrain with higher infectivity, on Huh7.5.1-8 cells. A multi-passaged HCV-JFH1-tau lot was infectious to CLDN1-defective S7-A cells, non-permissive to original HCV-JFH1-tau infection. We identified a single mutation, M706L, in the E2 glycoprotein of the HCV-JFH1-tau lot as an essential mutation for infectivity to S7-A cells. The pseudovirus JFH1/M706L mutant could not infect human embryonic kidney 293 T (HEK293T) cells lacking CLDN family but infected HEK293T cells expressing CLDN1, CLDN6, or CLDN9. Thus, this mutant virus could utilize CLDN1, and other CLDN6 and CLDN9, making HCV possible to infect cells other than hepatocytes. iPS cells, one of the stem cells, do not express CLDN1 but express CLDN6 and other host factors required for HCV infection. We confirmed that the HCV-JFH1-tau-derived mutant with an M706L mutation infected iPS cells in a CLDN6-dependent manner. These results demonstrated that a missense mutation in E2 could broaden the CLDN member specificity for HCV infection. HCV may change its receptor requirement through a single amino acid mutation and infect non-hepatic cells.
    MeSH term(s) Humans ; Claudin-1/genetics ; HEK293 Cells ; Hepacivirus/genetics ; Hepatitis C/genetics ; Mutation, Missense ; Viral Envelope Proteins/genetics
    Chemical Substances Claudin-1 ; glycoprotein E2, Hepatitis C virus (157184-61-7) ; Viral Envelope Proteins
    Language English
    Publishing date 2022-11-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 2615211-3
    ISSN 2045-2322 ; 2045-2322
    ISSN (online) 2045-2322
    ISSN 2045-2322
    DOI 10.1038/s41598-022-23824-3
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Reelin deficiency leads to aberrant lipid composition in mouse brain.

    Mizukami, Tomoharu / Ikeda, Kazutaka / Shimanaka, Yuta / Korogi, Katsunari / Zhou, Chunyu / Takase, Hiroshi / Tsuiji, Hitomi / Kono, Nozomu / Kohno, Takao / Arai, Hiroyuki / Arita, Makoto / Hattori, Mitsuharu

    Biochemical and biophysical research communications

    2018  Volume 505, Issue 1, Page(s) 81–86

    Abstract: Reelin is a secreted protein essential for the development and function of the mammalian brain. The receptors for Reelin, apolipoprotein E receptor 2 and very low-density lipoprotein receptor, belong to the low-density lipoprotein receptor family, but it ...

    Abstract Reelin is a secreted protein essential for the development and function of the mammalian brain. The receptors for Reelin, apolipoprotein E receptor 2 and very low-density lipoprotein receptor, belong to the low-density lipoprotein receptor family, but it is not known whether Reelin is involved in the brain lipid metabolism. In the present study, we performed lipidomic analysis of the cerebral cortex of wild-type and Reelin-deficient (reeler) mice, and found that reeler mice exhibited several compositional changes in phospholipids. First, the ratio of phospholipids containing one saturated fatty acid (FA) and one docosahexaenoic acid (DHA) or arachidonic acid (ARA) decreased. Secondly, the ratio of phospholipids containing one monounsaturated FA (MUFA) and one DHA or ARA increased. Thirdly, the ratio of phospholipids containing 5,8,11-eicosatrienoic acid, or Mead acid (MA), increased. Finally, the expression of stearoyl-CoA desaturase-1 (SCD-1) increased. As the increase of MA is seen as an index of polyunsaturated FA (PUFA) deficiency, and the expression of SCD-1 is suppressed by PUFA, these results strongly suggest that the loss of Reelin leads to PUFA deficiency. Hence, MUFA and MA are synthesized in response to this deficiency, in part by inducing SCD-1 expression. This is the first report of changes of FA composition in the reeler mouse brain and provides a basis for further investigating the new role of Reelin in the development and function of the brain.
    MeSH term(s) 8,11,14-Eicosatrienoic Acid/analogs & derivatives ; 8,11,14-Eicosatrienoic Acid/metabolism ; Animals ; Arachidonic Acid/metabolism ; Brain/embryology ; Brain/metabolism ; Cell Adhesion Molecules, Neuronal/deficiency ; Cell Adhesion Molecules, Neuronal/genetics ; Docosahexaenoic Acids/metabolism ; Extracellular Matrix Proteins/deficiency ; Extracellular Matrix Proteins/genetics ; Fatty Acids/metabolism ; Gene Expression Regulation, Developmental ; Lipid Metabolism ; Lipids/chemistry ; Mice, Inbred ICR ; Mice, Neurologic Mutants ; Nerve Tissue Proteins/deficiency ; Nerve Tissue Proteins/genetics ; Phospholipids/metabolism ; Serine Endopeptidases/deficiency ; Serine Endopeptidases/genetics ; Stearoyl-CoA Desaturase/genetics ; Stearoyl-CoA Desaturase/metabolism
    Chemical Substances Cell Adhesion Molecules, Neuronal ; Extracellular Matrix Proteins ; Fatty Acids ; Lipids ; Nerve Tissue Proteins ; Phospholipids ; Docosahexaenoic Acids (25167-62-8) ; Arachidonic Acid (27YG812J1I) ; Scd1 protein, mouse (EC 1.14.19.1) ; Stearoyl-CoA Desaturase (EC 1.14.19.1) ; Serine Endopeptidases (EC 3.4.21.-) ; reelin protein (EC 3.4.21.-) ; 8,11,14-Eicosatrienoic Acid (FC398RK06S) ; mead acid (JQS194YH3X)
    Language English
    Publishing date 2018-09-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 1090-2104 ; 0006-291X ; 0006-291X
    ISSN (online) 1090-2104 ; 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2018.09.089
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 116: Show issues Location:
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