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  1. Article ; Online: Claudin targeting as an effective tool for directed barrier modulation of the viable epidermis.

    Beier, Laura-Sophie / Waldow, Ayk / Khomeijani Farahani, Saeed / Mannweiler, Roman / Vidal-Y-Sy, Sabine / Brandner, Johanna M / Piontek, Jörg / Günzel, Dorothee

    Annals of the New York Academy of Sciences

    2022  Volume 1517, Issue 1, Page(s) 251–265

    Abstract: Tight junction (TJ) formation is vital for epidermal barrier function. We aimed to specifically manipulate TJ barriers in the reconstructed human epidermis (RHE) by claudin-1 and -4 knockdown (KD) and by claudin-binding fusion proteins of glutathione S- ... ...

    Abstract Tight junction (TJ) formation is vital for epidermal barrier function. We aimed to specifically manipulate TJ barriers in the reconstructed human epidermis (RHE) by claudin-1 and -4 knockdown (KD) and by claudin-binding fusion proteins of glutathione S-transferase and modified C-terminal fragments of Clostridium perfringens enterotoxin (GST-cCPE). Impedance spectroscopy and tracer permeability imaging were employed for functional barrier assessment and investigation of claudin contribution. KD of claudin-1, but not claudin-4, impaired the paracellular barrier in vitro. Similarly, claudin-binding GST-cCPE variants weakened the paracellular but not the stratum corneum barrier. Combining both TJ targeting methods, we found that claudin-1 targeting by GST-cCPE after claudin-4 KD led to a marked decrease in paracellular barrier properties. Conversely, after claudin-1 KD, GST-cCPE did not further impair the barrier. Comparison of GST-cCPE variants with different claudin-1/claudin-4 affinities, NHS-fluorescein tracer detection, and immunostaining of RHE paraffin sections showed that GST-cCPE variants bind to extrajunctional claudin-1 and -4, which are differentially distributed along the stratum basale-stratum granulosum axis. GST-cCPE binding blocks these claudins, thereby specifically opening the paracellular barrier of RHE. The data indicate a critical role for claudin-1 in regulating paracellular permeability for ions and small molecules in the viable epidermis. Claudin targeting is presented as a proof-of-concept for precise barrier modulation.
    MeSH term(s) Humans ; Claudins/metabolism ; Claudin-1/metabolism ; Claudin-4/metabolism ; Epidermis/metabolism ; Permeability ; Tight Junctions/metabolism ; Claudin-5/metabolism
    Chemical Substances Claudins ; Claudin-1 ; Claudin-4 ; Claudin-5
    Language English
    Publishing date 2022-08-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 211003-9
    ISSN 1749-6632 ; 0077-8923
    ISSN (online) 1749-6632
    ISSN 0077-8923
    DOI 10.1111/nyas.14879
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: cCPE Fusion Proteins as Molecular Probes to Detect Claudins and Tight Junction Dysregulation in Gastrointestinal Cell Lines, Tissue Explants and Patient-Derived Organoids.

    Waldow, Ayk / Beier, Laura-Sophie / Arndt, Janine / Schallenberg, Simon / Vollbrecht, Claudia / Bischoff, Philip / Farrera-Sal, Martí / Loch, Florian N / Bojarski, Christian / Schumann, Michael / Winkler, Lars / Kamphues, Carsten / Ehlen, Lukas / Piontek, Jörg

    Pharmaceutics

    2023  Volume 15, Issue 7

    Abstract: Claudins regulate paracellular permeability, contribute to epithelial polarization and are dysregulated during inflammation and carcinogenesis. Variants of the claudin-binding domain ... ...

    Abstract Claudins regulate paracellular permeability, contribute to epithelial polarization and are dysregulated during inflammation and carcinogenesis. Variants of the claudin-binding domain of
    Language English
    Publishing date 2023-07-19
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2527217-2
    ISSN 1999-4923
    ISSN 1999-4923
    DOI 10.3390/pharmaceutics15071980
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket.

    Schmidt, Edward N / Lamprinaki, Dimitra / McCord, Kelli A / Joe, Maju / Sojitra, Mirat / Waldow, Ayk / Nguyen, Jasmine / Monyror, John / Kitova, Elena N / Mozaneh, Fahima / Guo, Xue Yan / Jung, Jaesoo / Enterina, Jhon R / Daskhan, Gour C / Han, Ling / Krysler, Amanda R / Cromwell, Christopher R / Hubbard, Basil P / West, Lori J /
    Kulka, Marianne / Sipione, Simonetta / Klassen, John S / Derda, Ratmir / Lowary, Todd L / Mahal, Lara K / Riddell, Meghan R / Macauley, Matthew S

    Nature communications

    2023  Volume 14, Issue 1, Page(s) 2327

    Abstract: Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands. Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing the complex behaviors of glycolipids in a membrane. Through optimizing ... ...

    Abstract Immunomodulatory Siglecs are controlled by their glycoprotein and glycolipid ligands. Siglec-glycolipid interactions are often studied outside the context of a lipid bilayer, missing the complex behaviors of glycolipids in a membrane. Through optimizing a liposomal formulation to dissect Siglec-glycolipid interactions, it is shown that Siglec-6 can recognize glycolipids independent of its canonical binding pocket, suggesting that Siglec-6 possesses a secondary binding pocket tailored for recognizing glycolipids in a bilayer. A panel of synthetic neoglycolipids is used to probe the specificity of this glycolipid binding pocket on Siglec-6, leading to the development of a neoglycolipid with higher avidity for Siglec-6 compared to natural glycolipids. This neoglycolipid facilitates the delivery of liposomes to Siglec-6 on human mast cells, memory B-cells and placental syncytiotrophoblasts. A physiological relevance for glycolipid recognition by Siglec-6 is revealed for the binding and internalization of extracellular vesicles. These results demonstrate a unique and physiologically relevant ability of Siglec-6 to recognize glycolipids in a membrane.
    MeSH term(s) Female ; Humans ; Pregnancy ; Extracellular Vesicles/metabolism ; Glycolipids/chemistry ; Glycolipids/metabolism ; Liposomes ; Mast Cells/metabolism ; Memory B Cells/metabolism ; Placenta/metabolism ; Sialic Acid Binding Immunoglobulin-like Lectins/metabolism
    Chemical Substances Glycolipids ; Liposomes ; Sialic Acid Binding Immunoglobulin-like Lectins
    Language English
    Publishing date 2023-04-22
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-023-38030-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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