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  1. AU="Mihwa Lee"
  2. AU="Yuanting Jin"
  3. AU="Ter Haar, Eva"
  4. AU="Wolin, Dan L"
  5. AU="Zhang, Tenan"
  6. AU="Piedrafita, Lídia"
  7. AU="Nandy, Ananya"
  8. AU="Bansemer, Sven"
  9. AU="Kochetov, O"
  10. AU="Liu, Fen"

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  1. Artikel ; Online: The Emerging Role of the RNA-Binding Protein SFPQ in Neuronal Function and Neurodegeneration

    Yee Wa Lim / Dylan James / Jie Huang / Mihwa Lee

    International Journal of Molecular Sciences, Vol 21, Iss 7151, p

    2020  Band 7151

    Abstract: RNA-binding proteins (RBPs) are a class of proteins known for their diverse roles in RNA biogenesis, from regulating transcriptional processes in the nucleus to facilitating translation in the cytoplasm. With higher demand for RNA metabolism in the ... ...

    Abstract RNA-binding proteins (RBPs) are a class of proteins known for their diverse roles in RNA biogenesis, from regulating transcriptional processes in the nucleus to facilitating translation in the cytoplasm. With higher demand for RNA metabolism in the nervous system, RBP misregulation has been linked to a wide range of neurological and neurodegenerative diseases. One of the emerging RBPs implicated in neuronal function and neurodegeneration is splicing factor proline- and glutamine-rich (SFPQ). SFPQ is a ubiquitous and abundant RBP that plays multiple regulatory roles in the nucleus such as paraspeckle formation, DNA damage repair, and various transcriptional regulation processes. An increasing number of studies have demonstrated the nuclear and also cytoplasmic roles of SFPQ in neurons, particularly in post-transcriptional regulation and RNA granule formation. Not surprisingly, the misregulation of SFPQ has been linked to pathological features shown by other neurodegenerative disease-associated RBPs such as aberrant RNA splicing, cytoplasmic mislocalization, and aggregation. In this review, we discuss recent findings on the roles of SFPQ with a particular focus on those in neuronal development and homeostasis as well as its implications in neurodegenerative diseases.
    Schlagwörter SFPQ ; DBHS protein family ; Drosophila behavior human splicing ; RNA-binding protein ; nuclear protein ; neurodegenerative disease ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Thema/Rubrik (Code) 570
    Sprache Englisch
    Erscheinungsdatum 2020-09-01T00:00:00Z
    Verlag MDPI AG
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  2. Artikel ; Online: Familial ALS-associated SFPQ variants promote the formation of SFPQ cytoplasmic aggregates in primary neurons

    Jocelyn Widagdo / Saumya Udagedara / Nishita Bhembre / Jing Zhi Anson Tan / Lara Neureiter / Jie Huang / Victor Anggono / Mihwa Lee

    Open Biology, Vol 12, Iss

    2022  Band 9

    Abstract: Splicing factor proline- and glutamine-rich (SFPQ) is a nuclear RNA-binding protein that is involved in a wide range of physiological processes including neuronal development and homeostasis. However, the mislocalization and cytoplasmic aggregation of ... ...

    Abstract Splicing factor proline- and glutamine-rich (SFPQ) is a nuclear RNA-binding protein that is involved in a wide range of physiological processes including neuronal development and homeostasis. However, the mislocalization and cytoplasmic aggregation of SFPQ are associated with the pathophysiology of amyotrophic lateral sclerosis (ALS). We have previously reported that zinc mediates SFPQ polymerization and promotes the formation of cytoplasmic aggregates in neurons. Here we characterize two familial ALS (fALS)-associated SFPQ variants, which cause amino acid substitutions in the proximity of the SFPQ zinc-coordinating centre (N533H and L534I). Both mutants display increased zinc-binding affinities, which can be explained by the presence of a second zinc-binding site revealed by the 1.83 Å crystal structure of the human SFPQ L534I mutant. Overexpression of these fALS-associated mutants significantly increases the number of SFPQ cytoplasmic aggregates in primary neurons. Although they do not affect the density of dendritic spines, the presence of SFPQ cytoplasmic aggregates causes a marked reduction in the levels of the GluA1, but not the GluA2 subunit of AMPA-type glutamate receptors on the neuronal surface. Taken together, our data demonstrate that fALS-associated mutations enhance the propensity of SFPQ to bind zinc and form aggregates, leading to the dysregulation of AMPA receptor subunit composition, which may contribute to neuronal dysfunction in ALS.
    Schlagwörter amyotrophic lateral sclerosis ; protein aggregation ; DBHS proteins ; glutamate receptors ; RNA binding proteins ; zinc ; Biology (General) ; QH301-705.5
    Thema/Rubrik (Code) 571
    Sprache Englisch
    Erscheinungsdatum 2022-09-01T00:00:00Z
    Verlag The Royal Society
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  3. Artikel ; Online: Phosphatidylserine synthase plays an essential role in glia and affects development, as well as the maintenance of neuronal function

    Ye-Jin Park / Sungkyung Kim / Hyeon-Pyo Shim / Jae H. Park / Gyunghee Lee / Tae-Yeop Kim / Min-Cue Jo / Ah-Young Kwon / Mihwa Lee / Seongjae Lee / Jiwon Yeo / Hyung-Lok Chung / Hugo J. Bellen / Seung-Hae Kwon / Sang-Hak Jeon

    iScience, Vol 24, Iss 8, Pp 102899- (2021)

    2021  

    Abstract: Summary: Phosphatidylserine (PS) is an integral component of eukaryotic cell membranes and organelles. The Drosophila genome contains a single PS synthase (PSS)-encoding gene (Pss) homologous to mammalian PSSs. Flies with Pss loss-of-function alleles ... ...

    Abstract Summary: Phosphatidylserine (PS) is an integral component of eukaryotic cell membranes and organelles. The Drosophila genome contains a single PS synthase (PSS)-encoding gene (Pss) homologous to mammalian PSSs. Flies with Pss loss-of-function alleles show a reduced life span, increased bang sensitivity, locomotor defects, and vacuolated brain, which are the signs associated with neurodegeneration. We observed defective mitochondria in mutant adult brain, as well as elevated production of reactive oxygen species, and an increase in autophagy and apoptotic cell death. Intriguingly, glial-specific knockdown or overexpression of Pss alters synaptogenesis and axonal growth in the larval stage, causes developmental arrest in pupal stages, and neurodegeneration in adults. This is not observed with pan-neuronal up- or down-regulation. These findings suggest that precisely regulated expression of Pss in glia is essential for the development and maintenance of brain function. We propose a mechanism that underlies these neurodegenerative phenotypes triggered by defective PS metabolism.
    Schlagwörter Developmental neuroscience ; Cell biology ; Developmental biology ; Science ; Q
    Thema/Rubrik (Code) 571
    Sprache Englisch
    Erscheinungsdatum 2021-08-01T00:00:00Z
    Verlag Elsevier
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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  4. Artikel: Inhibition of lipopolysaccharide-induced nitric oxide and prostaglandin E2 production by chloroform fraction of Cudrania tricuspidata in RAW 264.7 macrophages

    Yang, Gabsik / Kyungjin Lee / Mihwa Lee / Inhye Ham / Ho-Young Choi

    BMC complementary and alternative medicine. 2012 Dec., v. 12, no. 1

    2012  

    Abstract: BACKGROUND: Cudrania tricuspidata extract is an important traditional herbal remedy for tumors, inflammation, gastritis, and liver damage and is predominantly used in Korea, China, and Japan. However, the anti-inflammatory effects of the extract have not ...

    Abstract BACKGROUND: Cudrania tricuspidata extract is an important traditional herbal remedy for tumors, inflammation, gastritis, and liver damage and is predominantly used in Korea, China, and Japan. However, the anti-inflammatory effects of the extract have not yet been conclusively proved. METHODS: In this study, we investigated the effects of the CHCl₃ fraction (CTC) of a methanol extract of C. tricuspidata on the lipopolysaccharide (LPS)-induced nitric oxide (NO) and prostaglandin E2 (PGE2) production in RAW 264.7 macrophage cells and mouse peritoneal macrophages, and the levels of pro-inflammatory cytokines tumor necrosis factor-α (TNF-α), interleukin (IL)-1β and IL-6 in RAW 264.7 macrophage cells. RESULTS: We observed that the protein expression levels of inducible NO synthase and COX-2 enzymes were markedly inhibited by CTC in a concentration-dependent manner. In addition, CTC reduced the production of TNF-α, IL-1β, and IL-6 in the LPS-stimulated RAW 264.7 macrophage cells. CONCLUSIONS: Our results show that the C. tricuspidata extract could modulate macrophage-mediated inflammatory functions such as the overproduction of cytokines, NO, and PGE2. The CTC was found to be the active fraction in this context.
    Schlagwörter Maclura tricuspidata ; alternative medicine ; anti-inflammatory activity ; chloroform ; gastritis ; inducible nitric oxide synthase ; inflammation ; interleukin-1beta ; interleukin-6 ; lipopolysaccharides ; liver ; macrophages ; methanol ; mice ; neoplasms ; nitric oxide ; prostaglandins ; protein synthesis ; tumor necrosis factor-alpha ; China ; Japan ; Korean Peninsula
    Sprache Englisch
    Erscheinungsverlauf 2012-12
    Umfang p. 250.
    Erscheinungsort BioMed Central
    Dokumenttyp Artikel
    ZDB-ID 2050429-9
    ISSN 1472-6882
    ISSN 1472-6882
    DOI 10.1186/1472-6882-12-250
    Datenquelle NAL Katalog (AGRICOLA)

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  5. Artikel: The central active site arginine in sulfite oxidizing enzymes alters kinetic properties by controlling electron transfer and redox interactions

    Hsiao, Ju-Chun / Aaron P. McGrath / Linda Kielmann / Palraj Kalimuthu / Farzana Darain / Paul V. Bernhardt / Jeffrey Harmer / Mihwa Lee / Kimberley Meyers / Megan J. Maher / Ulrike Kappler

    Biochimica et biophysica acta. 2018 Jan., v. 1859, no. 1

    2018  

    Abstract: A central conserved arginine, first identified as a clinical mutation leading to sulfite oxidase deficiency, is essential for catalytic competency of sulfite oxidizing molybdoenzymes, but the molecular basis for its effects on turnover and substrate ... ...

    Abstract A central conserved arginine, first identified as a clinical mutation leading to sulfite oxidase deficiency, is essential for catalytic competency of sulfite oxidizing molybdoenzymes, but the molecular basis for its effects on turnover and substrate affinity have not been fully elucidated.We have used a bacterial sulfite dehydrogenase, SorT, which lacks an internal heme group, but transfers electrons to an external, electron accepting cytochrome, SorU, to investigate the molecular functions of this arginine residue (Arg78). Assay of the SorT Mo centre catalytic competency in the absence of SorU showed that substitutions in the central arginine (R78Q, R78K and R78M mutations) only moderately altered SorT catalytic properties, except for R78M which caused significant reduction in SorT activity. The substitutions also altered the Mo-centre redox potentials (MoVI/V potential lowered by ca. 60–80mV). However, all Arg78 mutations significantly impaired the ability of SorT to transfer electrons to SorU, where activities were reduced 17 to 46-fold compared to SorTWT, precluding determination of kinetic parameters. This was accompanied by the observation of conformational changes in both the introduced Gln and Lys residues in the crystal structure of the enzymes. Taking into account data collected by others on related SOE mutations we propose that the formation and maintenance of an electron transfer complex between the Mo centre and electron accepting heme groups is the main function of the central arginine, and that the reduced turnover and increases in KMsulfite are caused by the inefficient operation of the oxidative half reaction of the catalytic cycle in enzymes carrying these mutations.
    Schlagwörter active sites ; arginine ; crystal structure ; data collection ; electron transfer ; energy metabolism ; heme ; molybdenum ; mutation ; redox potential ; sulfite dehydrogenase ; sulfite oxidase ; sulfites
    Sprache Englisch
    Erscheinungsverlauf 2018-01
    Umfang p. 19-27.
    Erscheinungsort Elsevier B.V.
    Dokumenttyp Artikel
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2017.10.001
    Datenquelle NAL Katalog (AGRICOLA)

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  6. Artikel ; Online: Vasorelaxant Effect of Osterici Radix Ethanol Extract on Rat Aortic Rings

    Kyungjin Lee / Geunyong Park / Inhye Ham / Gabsik Yang / Mihwa Lee / Youngmin Bu / Hocheol Kim / Ho-Young Choi

    Evidence-Based Complementary and Alternative Medicine, Vol

    2013  Band 2013

    Abstract: The root of Ostericum koreanum Maximowicz has been used as a traditional medicine called “Kanghwal” in Korea (or “Qianghuo” in China). The purpose of this study was to investigate the vasorelaxant activity and mechanism of action of an ethanol extract of ...

    Abstract The root of Ostericum koreanum Maximowicz has been used as a traditional medicine called “Kanghwal” in Korea (or “Qianghuo” in China). The purpose of this study was to investigate the vasorelaxant activity and mechanism of action of an ethanol extract of the O. koreanum root (EOK). We used isolated rat aortic rings to assess the effects of EOK on various vasorelaxant or vasoconstriction factors. EOK induced vasorelaxation in phenylephrine hydrochloride (PE) or KCl precontracted aortic rings in a concentration-dependent manner. However, the vasorelaxant effects of EOK on endothelium-intact aortic rings were reduced by pretreatment with L-NAME or methylene blue. In Ca2+-free Krebs-Henseleit solution, pretreatment with EOK (0.3 mg/mL) completely inhibited PE-induced constriction. In addition, EOK (0.3 mg/mL) also completely inhibited vasoconstriction induced by supplemental Ca2+ in aortic rings that were precontracted with PE or KCl. Furthermore, the EOK-induced vasorelaxation in PE-contracted aortic rings was inhibited by preincubation with nifedipine. These results indicate that the vasorelaxant effects of EOK are responsible for the induction of NO formation from L-Arg and NO-cGMP pathways, blockage of the extracellular Ca2+ entry via the receptor-operative Ca2+ channel and voltage-dependent calcium channel, and blockage of sarcoplasmic reticulum Ca2+ release via the inositol triphosphate pathway.
    Schlagwörter Other systems of medicine ; RZ201-999
    Sprache Englisch
    Erscheinungsdatum 2013-01-01T00:00:00Z
    Verlag Hindawi Limited
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

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