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  1. Article: Decreased IL-10 expression in stefin B-deficient macrophages is regulated by the MAP kinase and STAT-3 signaling pathways

    Maher, Katarina / Janja Završnik / Barbara Jerič-Kokelj / Olga Vasiljeva / Boris Turk / Nataša Kopitar-Jerala

    Federation of European Biochemical Societies FEBS letters. 2014 Mar. 03, v. 588, no. 5

    2014  

    Abstract: Innate immune responses are tightly regulated to avoid excessive activation and subsequent inflammatory damage to the host, and interleukin-10 (IL-10) plays a crucial role in preventing inflammation. Stefin B (cystatin B) is an endogenous inhibitor of ... ...

    Abstract Innate immune responses are tightly regulated to avoid excessive activation and subsequent inflammatory damage to the host, and interleukin-10 (IL-10) plays a crucial role in preventing inflammation. Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases. In stefin B-deficient bone marrow-derived macrophages (BMDMs), we detected an increase in the induction of the LPS-induced pro-inflammatory signal nitric oxide (NO) but decreased IL-10 expression. The phosphorylation of ERK and p38 MAP-kinases was significantly decreased in stefin B-deficient macrophages, as was STAT-3 phosphorylation. These findings show that stefin B influences the expression of anti-inflammatory IL-10 in response to the TLR4 agonist LPS.
    Keywords Toll-like receptor 4 ; agonists ; cysteine proteinases ; inflammation ; innate immunity ; interleukin-10 ; macrophages ; mitogen-activated protein kinase ; nitric oxide ; phosphorylation ; signal transduction
    Language English
    Dates of publication 2014-0303
    Size p. 720-726.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2014.01.015
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  2. Article ; Online: Cystatin F regulates proteinase activity in IL-2-activated natural killer cells.

    Maher, Katarina / Konjar, Spela / Watts, Colin / Turk, Boris / Kopitar-Jerala, Natasa

    Protein and peptide letters

    2014  Volume 21, Issue 9, Page(s) 957–965

    Abstract: Cystatin F is a unique member of the cystatin family of cysteine protease inhibitors, which is synthesized as an inactive dimer and it is activated by N-terminal cleavage in the endolysosomes. It is expressed in the cells of the immune system: myeloid ... ...

    Abstract Cystatin F is a unique member of the cystatin family of cysteine protease inhibitors, which is synthesized as an inactive dimer and it is activated by N-terminal cleavage in the endolysosomes. It is expressed in the cells of the immune system: myeloid cells and the cells involved in target cell killing: natural killer (NK) cells and cytotoxic T cells (CTLs). Upon activation of the NK cells with interleukin 2 (IL-2), cystatin F was found upregulated and co-localized in cytotoxic granules with cathepsin C (CatC) and CatV. However, cystatin F inhibits the CatC in cells only when its N-terminal part is processed. Although cystatin F could inhibit both CatV and CatC, the IL-2 stimulation of the YT cells resulted in an increased CatV activity, while the CatC activity was unchanged. The incubation of IL-2 activated NK cells with a cysteine proteinase inhibitor E-64d increased the cystatin F dimer formation. Our results suggest that cystatin F not only inhibits CatV, but it is processed by the CatV in order to inhibit the CatC activity in cytotoxic granules. The regulation of the CatC activity in the cytotoxic granules of the NK cells by the cystatin F could be important for the processing and activation of granule-associated serine proteases - granzymes.
    MeSH term(s) Biomarkers, Tumor/metabolism ; Blotting, Western ; Cells, Cultured ; Cystatins/metabolism ; Enzyme Activation/drug effects ; Enzyme Inhibitors/pharmacology ; Humans ; Interleukin-2/pharmacology ; Killer Cells, Natural/drug effects ; Killer Cells, Natural/enzymology ; Leucine/analogs & derivatives ; Leucine/pharmacology ; Microscopy, Confocal ; Peptide Hydrolases/metabolism ; Up-Regulation/drug effects
    Chemical Substances (3-ethoxycarbonyloxirane-2-carbonyl)leucine (3-methylbutyl) amide ; Biomarkers, Tumor ; CST7 protein, human ; Cystatins ; Enzyme Inhibitors ; Interleukin-2 ; Peptide Hydrolases (EC 3.4.-) ; Leucine (GMW67QNF9C)
    Language English
    Publishing date 2014-04-02
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1280776-x
    ISSN 1875-5305 ; 0929-8665
    ISSN (online) 1875-5305
    ISSN 0929-8665
    DOI 10.2174/0929866521666140403124146
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    Zs.A 4452: Show issues Location:
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  3. Article ; Online: Decreased IL-10 expression in stefin B-deficient macrophages is regulated by the MAP kinase and STAT-3 signaling pathways.

    Maher, Katarina / Završnik, Janja / Jerič-Kokelj, Barbara / Vasiljeva, Olga / Turk, Boris / Kopitar-Jerala, Nataša

    FEBS letters

    2014  Volume 588, Issue 5, Page(s) 720–726

    Abstract: Innate immune responses are tightly regulated to avoid excessive activation and subsequent inflammatory damage to the host, and interleukin-10 (IL-10) plays a crucial role in preventing inflammation. Stefin B (cystatin B) is an endogenous inhibitor of ... ...

    Abstract Innate immune responses are tightly regulated to avoid excessive activation and subsequent inflammatory damage to the host, and interleukin-10 (IL-10) plays a crucial role in preventing inflammation. Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases. In stefin B-deficient bone marrow-derived macrophages (BMDMs), we detected an increase in the induction of the LPS-induced pro-inflammatory signal nitric oxide (NO) but decreased IL-10 expression. The phosphorylation of ERK and p38 MAP-kinases was significantly decreased in stefin B-deficient macrophages, as was STAT-3 phosphorylation. These findings show that stefin B influences the expression of anti-inflammatory IL-10 in response to the TLR4 agonist LPS.
    MeSH term(s) Animals ; Cells, Cultured ; Cystatin B/deficiency ; Cystatin B/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Interferon-gamma/genetics ; Interleukin-10/genetics ; Interleukin-10/metabolism ; Lipopolysaccharides/pharmacology ; MAP Kinase Signaling System ; Macrophage Activation ; Macrophages/immunology ; Macrophages/metabolism ; Mice, Knockout ; Nitric Oxide/metabolism ; STAT3 Transcription Factor/metabolism ; Transcriptional Activation/immunology
    Chemical Substances IL10 protein, mouse ; Lipopolysaccharides ; STAT3 Transcription Factor ; Stat3 protein, mouse ; Interleukin-10 (130068-27-8) ; Nitric Oxide (31C4KY9ESH) ; Interferon-gamma (82115-62-6) ; Cystatin B (88844-95-5) ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24)
    Language English
    Publishing date 2014-03-03
    Publishing country England
    Document type 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 10.1016/j.febslet.2014.01.015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.B 282: Show issues Location:
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  4. Article ; Online: A role for stefin B (cystatin B) in inflammation and endotoxemia.

    Maher, Katarina / Jerič Kokelj, Barbara / Butinar, Miha / Mikhaylov, Georgy / Manček-Keber, Mateja / Stoka, Veronika / Vasiljeva, Olga / Turk, Boris / Grigoryev, Sergei A / Kopitar-Jerala, Nataša

    The Journal of biological chemistry

    2014  Volume 289, Issue 46, Page(s) 31736–31750

    Abstract: Stefin B (cystatin B) is an endogenous cysteine cathepsin inhibitor, and the loss-of-function mutations in the stefin B gene were reported in patients with Unverricht-Lundborg disease (EPM1). In this study we demonstrated that stefin B-deficient (StB KO) ...

    Abstract Stefin B (cystatin B) is an endogenous cysteine cathepsin inhibitor, and the loss-of-function mutations in the stefin B gene were reported in patients with Unverricht-Lundborg disease (EPM1). In this study we demonstrated that stefin B-deficient (StB KO) mice were significantly more sensitive to the lethal LPS-induced sepsis and secreted higher amounts of pro-inflammatory cytokines IL-1β and IL-18 in the serum. We further showed that increased caspase-11 gene expression and better pro-inflammatory caspase-1 and -11 activation determined in StB KO bone marrow-derived macrophages resulted in enhanced IL-1β processing. Pretreatment of macrophages with the cathepsin inhibitor E-64d did not affect secretion of IL-1β, suggesting that the increased cathepsin activity determined in StB KO bone marrow-derived macrophages is not essential for inflammasome activation. Upon LPS stimulation, stefin B was targeted into the mitochondria, and the lack of stefin B resulted in the increased destabilization of mitochondrial membrane potential and mitochondrial superoxide generation. Collectively, our study demonstrates that the LPS-induced sepsis in StB KO mice is dependent on caspase-11 and mitochondrial reactive oxygen species but is not associated with the lysosomal destabilization and increased cathepsin activity in the cytosol.
    MeSH term(s) Animals ; Caspases/metabolism ; Caspases, Initiator ; Cystatin B/physiology ; Endotoxemia/metabolism ; Escherichia coli/metabolism ; Gene Expression Regulation ; Inflammasomes/metabolism ; Inflammation/metabolism ; Lipopolysaccharides ; Macrophages/cytology ; Macrophages/metabolism ; Mice ; Mice, Knockout ; Mice, Transgenic ; Mitochondria/metabolism ; NF-kappa B/metabolism ; Reactive Oxygen Species/metabolism
    Chemical Substances Cstb protein, mouse ; Inflammasomes ; Lipopolysaccharides ; NF-kappa B ; Reactive Oxygen Species ; Cystatin B (88844-95-5) ; Casp4 protein, mouse (EC 3.4.22.-) ; Caspases (EC 3.4.22.-) ; Caspases, Initiator (EC 3.4.22.-)
    Language English
    Publishing date 2014-10-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M114.609396
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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  5. Article: Stefin B Interacts with Histones and Cathepsin L in the Nucleus

    Čeru, Slavko / Konjar, Špela / Maher, Katarina / Repnik, Urška / Križaj, Igor / Benčina, Mojca / Renko, Miha / Nepveu, Alain / Žerovnik, Eva / Turk, Boris / Kopitar-Jerala, Nataša

    Journal of biological chemistry. 2010 Mar. 26, v. 285, no. 13

    2010  

    Abstract: Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases localized in the nucleus and the cytosol. Loss-of-function mutations in the stefin B gene (CSTB) gene were reported in patients with Unverricht-Lundborg disease (EPM1). We have ... ...

    Abstract Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases localized in the nucleus and the cytosol. Loss-of-function mutations in the stefin B gene (CSTB) gene were reported in patients with Unverricht-Lundborg disease (EPM1). We have identified an interaction between stefin B and nucleosomes, specifically with histones H2A.Z, H2B, and H3. In synchronized T98G cells, stefin B co-immunoprecipitated with histone H3, predominantly in the G¹ phase of the cell cycle. Stefin B-deficient mouse embryonic fibroblasts entered S phase earlier than wild type mouse embryonic fibroblasts. In contrast, increased expression of stefin B in the nucleus delayed cell cycle progression in T98G cells. The delay in cell cycle progression was associated with the inhibition of cathepsin L in the nucleus, as judged from the decreased cleavage of the CUX1 transcription factor. In vitro, inhibition of cathepsin L by stefin B was potentiated in the presence of histones, whereas histones alone did not affect the cathepsin L activity. Interaction of stefin B with the Met-75 truncated form of cathepsin L in the nucleus was confirmed by fluorescence resonance energy transfer experiments in the living cells. Stefin B could thus play an important role in regulating the proteolytic activity of cathepsin L in the nucleus, protecting substrates such as transcription factors from its proteolytic processing.
    Language English
    Dates of publication 2010-0326
    Size p. 10078-10086.
    Publishing place American Society for Biochemistry and Molecular Biology
    Document type Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
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  6. Article ; Online: Stefin B interacts with histones and cathepsin L in the nucleus.

    Čeru, Slavko / Konjar, Špela / Maher, Katarina / Repnik, Urška / Križaj, Igor / Benčina, Mojca / Renko, Miha / Nepveu, Alain / Žerovnik, Eva / Turk, Boris / Kopitar-Jerala, Nataša

    The Journal of biological chemistry

    2010  Volume 285, Issue 13, Page(s) 10078–10086

    Abstract: Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases localized in the nucleus and the cytosol. Loss-of-function mutations in the stefin B gene (CSTB) gene were reported in patients with Unverricht-Lundborg disease (EPM1). We have ... ...

    Abstract Stefin B (cystatin B) is an endogenous inhibitor of cysteine proteinases localized in the nucleus and the cytosol. Loss-of-function mutations in the stefin B gene (CSTB) gene were reported in patients with Unverricht-Lundborg disease (EPM1). We have identified an interaction between stefin B and nucleosomes, specifically with histones H2A.Z, H2B, and H3. In synchronized T98G cells, stefin B co-immunoprecipitated with histone H3, predominantly in the G(1) phase of the cell cycle. Stefin B-deficient mouse embryonic fibroblasts entered S phase earlier than wild type mouse embryonic fibroblasts. In contrast, increased expression of stefin B in the nucleus delayed cell cycle progression in T98G cells. The delay in cell cycle progression was associated with the inhibition of cathepsin L in the nucleus, as judged from the decreased cleavage of the CUX1 transcription factor. In vitro, inhibition of cathepsin L by stefin B was potentiated in the presence of histones, whereas histones alone did not affect the cathepsin L activity. Interaction of stefin B with the Met-75 truncated form of cathepsin L in the nucleus was confirmed by fluorescence resonance energy transfer experiments in the living cells. Stefin B could thus play an important role in regulating the proteolytic activity of cathepsin L in the nucleus, protecting substrates such as transcription factors from its proteolytic processing.
    MeSH term(s) Animals ; Cathepsin L/metabolism ; Cell Cycle ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cystatin B/metabolism ; Cytosol/metabolism ; Fibroblasts/metabolism ; Fluorescence Resonance Energy Transfer/methods ; Gene Expression Regulation ; Histones/chemistry ; Histones/metabolism ; Humans ; Mice ; Models, Biological
    Chemical Substances Histones ; Cystatin B (88844-95-5) ; Cathepsin L (EC 3.4.22.15)
    Keywords covid19
    Language English
    Publishing date 2010-01-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M109.034793
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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