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  1. Article ; Online: Biodegradable and Dual-Responsive Polypeptide-Shelled Cyclodextrin-Containers for Intracellular Delivery of Membrane-Impermeable Cargo.

    Kudruk, Sergej / Pottanam Chali, Sharafudheen / Linard Matos, Anna Livia / Bourque, Cole / Dunker, Clara / Gatsogiannis, Christos / Ravoo, Bart Jan / Gerke, Volker

    Advanced science (Weinheim, Baden-Wurttemberg, Germany)

    2021  Volume 8, Issue 18, Page(s) e2100694

    Abstract: The transport of membrane impermeable compounds into cells is a prerequisite for the efficient cellular delivery of hydrophilic and amphiphilic compounds and drugs. Transport into the cell's cytosolic compartment should ideally be controllable and it ... ...

    Abstract The transport of membrane impermeable compounds into cells is a prerequisite for the efficient cellular delivery of hydrophilic and amphiphilic compounds and drugs. Transport into the cell's cytosolic compartment should ideally be controllable and it should involve biologically compatible and degradable vehicles. Addressing these challenges, nanocontainers based on cyclodextrin amphiphiles that are stabilized by a biodegradable peptide shell are developed and their potential to deliver fluorescently labeled cargo into human cells is analyzed. Host-guest mediated self-assembly of a thiol-containing short peptide or a cystamine-cross-linked polypeptide shell on cyclodextrin vesicles produce short peptide-shelled (SPSV
    MeSH term(s) Cyclodextrins/metabolism ; Drug Delivery Systems/methods ; Drug Liberation ; Endothelial Cells/metabolism ; Humans ; Hydrophobic and Hydrophilic Interactions ; Nanoparticles/metabolism ; Peptides/metabolism
    Chemical Substances Cyclodextrins ; Peptides
    Language English
    Publishing date 2021-07-18
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2808093-2
    ISSN 2198-3844 ; 2198-3844
    ISSN (online) 2198-3844
    ISSN 2198-3844
    DOI 10.1002/advs.202100694
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: P-selectin-dependent leukocyte adhesion is governed by endolysosomal two-pore channel 2.

    Goretzko, Jonas / Pauels, Inga / Heitzig, Nicole / Thomas, Katharina / Kardell, Marina / Naß, Johannes / Krogsaeter, Einar Kleinhans / Schloer, Sebastian / Spix, Barbara / Linard Matos, Anna Lívia / Leser, Charlotte / Wegner, Tristan / Glorius, Frank / Bracher, Franz / Gerke, Volker / Rossaint, Jan / Grimm, Christian / Rescher, Ursula

    Cell reports

    2023  Volume 42, Issue 12, Page(s) 113501

    Abstract: Upon proinflammatory challenges, endothelial cell surface presentation of the leukocyte receptor P-selectin, together with the stabilizing co-factor CD63, is needed for leukocyte capture and is mediated via demand-driven exocytosis from the Weibel-Palade ...

    Abstract Upon proinflammatory challenges, endothelial cell surface presentation of the leukocyte receptor P-selectin, together with the stabilizing co-factor CD63, is needed for leukocyte capture and is mediated via demand-driven exocytosis from the Weibel-Palade bodies that fuse with the plasma membrane. We report that neutrophil recruitment to activated endothelium is significantly reduced in mice deficient for the endolysosomal cation channel TPC2 and in human primary endothelial cells with pharmacological TPC2 block. We observe less CD63 signal in whole-mount stainings of proinflammatory-activated cremaster muscles from TPC2 knockout mice. We find that TPC2 is activated and needed to ensure the transfer of CD63 from endolysosomes via Weibel-Palade bodies to the plasma membrane to retain P-selectin on the cell surface of human primary endothelial cells. Our findings establish TPC2 as a key element to leukocyte interaction with the endothelium and a potential pharmacological target in the control of inflammatory leukocyte recruitment.
    MeSH term(s) Mice ; Humans ; Animals ; P-Selectin/metabolism ; Two-Pore Channels ; Endothelial Cells/metabolism ; Weibel-Palade Bodies/metabolism ; Cell Adhesion ; Leukocytes/metabolism ; Endothelium, Vascular/metabolism
    Chemical Substances P-Selectin ; Two-Pore Channels
    Language English
    Publishing date 2023-11-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2649101-1
    ISSN 2211-1247 ; 2211-1247
    ISSN (online) 2211-1247
    ISSN 2211-1247
    DOI 10.1016/j.celrep.2023.113501
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: TSC1 binding to lysosomal PIPs is required for TSC complex translocation and mTORC1 regulation

    Fitzian, Katharina / Brückner, Anne / Brohée, Laura / Zech, Reinhard / Antoni, Claudia / Kiontke, Stephan / Gasper, Raphael / Linard Matos, Anna Livia / Beel, Stephanie / Wilhelm, Sabine / Gerke, Volker / Ungermann, Christian / Nellist, Mark / Raunser, Stefan / Demetriades, Constantinos / Oeckinghaus, Andrea / Kümmel, Daniel

    Molecular cell. 2021 July 01, v. 81, no. 13

    2021  

    Abstract: The TSC complex is a critical negative regulator of the small GTPase Rheb and mTORC1 in cellular stress signaling. The TSC2 subunit contains a catalytic GTPase activating protein domain and interacts with multiple regulators, while the precise function ... ...

    Abstract The TSC complex is a critical negative regulator of the small GTPase Rheb and mTORC1 in cellular stress signaling. The TSC2 subunit contains a catalytic GTPase activating protein domain and interacts with multiple regulators, while the precise function of TSC1 is unknown. Here we provide a structural characterization of TSC1 and define three domains: a C-terminal coiled-coil that interacts with TSC2, a central helical domain that mediates TSC1 oligomerization, and an N-terminal HEAT repeat domain that interacts with membrane phosphatidylinositol phosphates (PIPs). TSC1 architecture, oligomerization, and membrane binding are conserved in fungi and humans. We show that lysosomal recruitment of the TSC complex and subsequent inactivation of mTORC1 upon starvation depend on the marker lipid PI3,5P₂, demonstrating a role for lysosomal PIPs in regulating TSC complex and mTORC1 activity via TSC1. Our study thus identifies a vital role of TSC1 in TSC complex function and mTORC1 signaling.
    Keywords guanosinetriphosphatase ; lipids ; oligomerization ; protein domains ; starvation
    Language English
    Dates of publication 2021-0701
    Size p. 2705-2721.e8.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.04.019
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Bonn / Germany

    Z 2005/501: Show issues

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  4. Article ; Online: An Imidazolium-Based Lipid Analogue as a Gene Transfer Agent.

    Paulisch, Tiffany O / Bornemann, Steffen / Herzog, Marius / Kudruk, Sergej / Roling, Lena / Linard Matos, Anna Livia / Galla, Hans-Joachim / Gerke, Volker / Winter, Roland / Glorius, Frank

    Chemistry (Weinheim an der Bergstrasse, Germany)

    2020  Volume 26, Issue 71, Page(s) 17176–17182

    Abstract: A dicationic imidazolium salt is described and investigated towards its application for gene transfer. The polar head group and the long alkyl chains in the backbone contribute to a lipid-like behavior, while an alkyl ammonium group provides the ability ... ...

    Abstract A dicationic imidazolium salt is described and investigated towards its application for gene transfer. The polar head group and the long alkyl chains in the backbone contribute to a lipid-like behavior, while an alkyl ammonium group provides the ability for crucial electrostatic interaction for the transfection process. Detailed biophysical studies regarding its impact on biological membrane models and the propensity of vesicle fusion are presented. Fluorescence spectroscopy, atomic force microscopy and confocal fluorescence microscopy show that the imidazolium salt leads to negligible changes in lipid packing, while displaying distinct vesicle fusion properties. Cell culture experiments reveal that mixed liposomes containing the novel imidazolium salt can serve as plasmid DNA delivery vehicles. In contrast, a structurally similar imidazolium salt without a second positive charge showed no ability to support DNA transfection into cultured cells. Thus, we introduce a novel and variable structural motif for cationic lipids, expanding the field of lipofection agents.
    MeSH term(s) Cations/chemistry ; DNA/chemistry ; Imidazoles/chemistry ; Lipids ; Liposomes ; Transfection
    Chemical Substances Cations ; Imidazoles ; Lipids ; Liposomes ; DNA (9007-49-2)
    Language English
    Publishing date 2020-11-09
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1478547-X
    ISSN 1521-3765 ; 0947-6539
    ISSN (online) 1521-3765
    ISSN 0947-6539
    DOI 10.1002/chem.202003466
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: TSC1 binding to lysosomal PIPs is required for TSC complex translocation and mTORC1 regulation.

    Fitzian, Katharina / Brückner, Anne / Brohée, Laura / Zech, Reinhard / Antoni, Claudia / Kiontke, Stephan / Gasper, Raphael / Linard Matos, Anna Livia / Beel, Stephanie / Wilhelm, Sabine / Gerke, Volker / Ungermann, Christian / Nellist, Mark / Raunser, Stefan / Demetriades, Constantinos / Oeckinghaus, Andrea / Kümmel, Daniel

    Molecular cell

    2021  Volume 81, Issue 13, Page(s) 2705–2721.e8

    Abstract: The TSC complex is a critical negative regulator of the small GTPase Rheb and mTORC1 in cellular stress signaling. The TSC2 subunit contains a catalytic GTPase activating protein domain and interacts with multiple regulators, while the precise function ... ...

    Abstract The TSC complex is a critical negative regulator of the small GTPase Rheb and mTORC1 in cellular stress signaling. The TSC2 subunit contains a catalytic GTPase activating protein domain and interacts with multiple regulators, while the precise function of TSC1 is unknown. Here we provide a structural characterization of TSC1 and define three domains: a C-terminal coiled-coil that interacts with TSC2, a central helical domain that mediates TSC1 oligomerization, and an N-terminal HEAT repeat domain that interacts with membrane phosphatidylinositol phosphates (PIPs). TSC1 architecture, oligomerization, and membrane binding are conserved in fungi and humans. We show that lysosomal recruitment of the TSC complex and subsequent inactivation of mTORC1 upon starvation depend on the marker lipid PI3,5P
    Language English
    Publishing date 2021-05-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2021.04.019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5055: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
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  6. Article: Phosphorescent cationic iridium(iii) complexes dynamically bound to cyclodextrin vesicles: applications in live cell imaging.

    Schibilla, Frauke / Holthenrich, Anna / Song, Boyi / Linard Matos, Anna Lívia / Grill, David / Rota Martir, Diego / Gerke, Volker / Zysman-Colman, Eli / Ravoo, Bart Jan

    Chemical science

    2018  Volume 9, Issue 40, Page(s) 7822–7828

    Abstract: We report cationic Ir(iii) complexes functionalized with adamantyl groups designed to bind to β-cyclodextrin vesicles (CDV) with high affinity ( ...

    Abstract We report cationic Ir(iii) complexes functionalized with adamantyl groups designed to bind to β-cyclodextrin vesicles (CDV) with high affinity (
    Language English
    Publishing date 2018-08-09
    Publishing country England
    Document type Journal Article
    ZDB-ID 2559110-1
    ISSN 2041-6539 ; 2041-6520
    ISSN (online) 2041-6539
    ISSN 2041-6520
    DOI 10.1039/c8sc02875c
    Database MEDical Literature Analysis and Retrieval System OnLINE

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