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  1. Book ; Online ; E-Book: Tight junctions

    Gonzalez-Mariscal, Lorenza

    2022  

    Author's details edited by Lorenza González-Mariscal
    Keywords Tight junctions (Cell biology) ; Life sciences
    Subject code 571.6
    Language English
    Size 1 online resource (340 pages)
    Publisher Springer
    Publishing place Cham, Switzerland
    Document type Book ; Online ; E-Book
    Note Includes index.
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 9783030972042 ; 9783030972035 ; 3030972046 ; 3030972038
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Tight junctions

    González-Mariscal, Lorenza

    (Molecular biology intelligence unit)

    2006  

    Author's details Lorenza González-Mariscal [Hrsg.]
    Series title Molecular biology intelligence unit
    Keywords Tight Junctions ; Biologie
    Subject Allgemeine Biologie
    Language English
    Size 224 S. : Ill., graph. Darst.
    Publisher Landes Bioscience ; Springer
    Publishing place Georgetown, Tex ; New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT014858318
    ISBN 0-387-33201-4 ; 978-0-387-33201-7
    Database Catalogue ZB MED Medicine, Health

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  3. Article: Editorial: Investigating the Factors that Control Epithelial Cell Polarity and Adhesion During Morphogenesis.

    González-Mariscal, Lorenza

    Frontiers in cell and developmental biology

    2021  Volume 9, Page(s) 802568

    Language English
    Publishing date 2021-11-18
    Publishing country Switzerland
    Document type Editorial
    ZDB-ID 2737824-X
    ISSN 2296-634X
    ISSN 2296-634X
    DOI 10.3389/fcell.2021.802568
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Book: Role of tight junctions in cell proliferation and cancer

    González-Mariscal, Lorenza / Lechuga, Susana / Garay, Erika

    (Progress in histochemistry and cytochemistry ; 42,1)

    2007  

    Author's details Lorenza González-Mariscal ; Susana Lechuga ; Erika Garay
    Series title Progress in histochemistry and cytochemistry ; 42,1
    Collection
    Language English
    Size 57 S. : Ill.
    Publisher Elsevier
    Publishing place Amsterdam u.a.
    Publishing country Netherlands
    Document type Book
    HBZ-ID HT015217800
    Database Catalogue ZB MED Medicine, Health

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  5. Article ; Online: A short guide to the tight junction.

    Citi, Sandra / Fromm, Michael / Furuse, Mikio / González-Mariscal, Lorenza / Nusrat, Asma / Tsukita, Sachiko / Turner, Jerrold R

    Journal of cell science

    2024  Volume 137, Issue 9

    Abstract: Tight junctions (TJs) are specialized regions of contact between cells of epithelial and endothelial tissues that form selective semipermeable paracellular barriers that establish and maintain body compartments with different fluid compositions. As such, ...

    Abstract Tight junctions (TJs) are specialized regions of contact between cells of epithelial and endothelial tissues that form selective semipermeable paracellular barriers that establish and maintain body compartments with different fluid compositions. As such, the formation of TJs represents a critical step in metazoan evolution, allowing the formation of multicompartmental organisms and true, barrier-forming epithelia and endothelia. In the six decades that have passed since the first observations of TJs by transmission electron microscopy, much progress has been made in understanding the structure, function, molecular composition and regulation of TJs. The goal of this Perspective is to highlight the key concepts that have emerged through this research and the future challenges that lie ahead for the field.
    MeSH term(s) Tight Junctions/metabolism ; Tight Junctions/ultrastructure ; Humans ; Animals ; Epithelial Cells/metabolism ; Epithelial Cells/ultrastructure ; Epithelial Cells/cytology
    Language English
    Publishing date 2024-05-07
    Publishing country England
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.261776
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Polyubiquitination and SUMOylation Sites Regulate the Stability of ZO-2 Protein and the Sealing of Tight Junctions.

    Cano-Cortina, Misael / Alarcón, Lourdes / Miranda, Jael / Huber, Otmar / González-Mariscal, Lorenza

    Cells

    2022  Volume 11, Issue 20

    Abstract: Tight junctions (TJs) regulate the transit of ions and molecules through the paracellular pathway in epithelial cells. ...

    Abstract Tight junctions (TJs) regulate the transit of ions and molecules through the paracellular pathway in epithelial cells.
    MeSH term(s) Zonula Occludens-2 Protein/metabolism ; Tight Junctions/metabolism ; Zonula Occludens-1 Protein/genetics ; Zonula Occludens-1 Protein/metabolism ; Sumoylation ; Lysine/metabolism ; Phosphoproteins/metabolism ; Cell Line ; Proline/metabolism
    Chemical Substances Zonula Occludens-2 Protein ; Zonula Occludens-1 Protein ; Lysine (K3Z4F929H6) ; Phosphoproteins ; Proline (9DLQ4CIU6V)
    Language English
    Publishing date 2022-10-19
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells11203296
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: The Role of ZO-2 in Modulating JAM-A and γ-Actin Junctional Recruitment, Apical Membrane and Tight Junction Tension, and Cell Response to Substrate Stiffness and Topography.

    Pinto-Dueñas, Diana Cristina / Hernández-Guzmán, Christian / Marsch, Patrick Matthew / Wadurkar, Anand Sunil / Martín-Tapia, Dolores / Alarcón, Lourdes / Vázquez-Victorio, Genaro / Méndez-Méndez, Juan Vicente / Chanona-Pérez, José Jorge / Nangia, Shikha / González-Mariscal, Lorenza

    International journal of molecular sciences

    2024  Volume 25, Issue 5

    Abstract: This work analyzes the role of the tight junction (TJ) protein ZO-2 on mechanosensation. We found that the lack of ZO-2 reduced apical membrane rigidity measured with atomic force microscopy, inhibited the association of γ-actin and JAM-A to the cell ... ...

    Abstract This work analyzes the role of the tight junction (TJ) protein ZO-2 on mechanosensation. We found that the lack of ZO-2 reduced apical membrane rigidity measured with atomic force microscopy, inhibited the association of γ-actin and JAM-A to the cell border, and instead facilitated p114RhoGEF and afadin accumulation at the junction, leading to an enhanced mechanical tension at the TJ measured by FRET, with a ZO-1 tension probe, and increased tricellular TJ tension. Simultaneously, adherens junction tension measured with an E-cadherin probe was unaltered. The stability of JAM-A and ZO-2 binding was assessed by a collaborative in silico study. The absence of ZO-2 also impacted the cell response to the substrate, as monolayers plated in 20 kPa hydrogels developed holes not seen in parental cultures and displayed a retarded elongation and formation of cell aggregates. The absence of ZO-2 was sufficient to induce YAP and Snail nuclear accumulation in cells cultured over glass, but when ZO-2 KD cells were plated in nanostructured ridge arrays, they displayed an increased abundance of nuclear Snail and conspicuous internalization of claudin-4. These results indicate that the absence of ZO-2 also impairs the response of cells to substrate stiffness and exacerbates transformation triggered by substrate topography.
    MeSH term(s) Actins/metabolism ; Tight Junctions/metabolism ; Zonula Occludens-1 Protein/metabolism ; Phosphoproteins/metabolism
    Chemical Substances Actins ; Zonula Occludens-1 Protein ; Phosphoproteins
    Language English
    Publishing date 2024-02-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25052453
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Relationship between apical junction proteins, gene expression and cancer.

    González-Mariscal, Lorenza / Miranda, Jael / Gallego-Gutiérrez, Helios / Cano-Cortina, Misael / Amaya, Elida

    Biochimica et biophysica acta. Biomembranes

    2020  Volume 1862, Issue 9, Page(s) 183278

    Abstract: The apical junctional complex (AJC) is a cell-cell adhesion system present at the upper portion of the lateral membrane of epithelial cells integrated by the tight junction (TJ) and the adherens junction (AJ). This complex is crucial to initiate and ... ...

    Abstract The apical junctional complex (AJC) is a cell-cell adhesion system present at the upper portion of the lateral membrane of epithelial cells integrated by the tight junction (TJ) and the adherens junction (AJ). This complex is crucial to initiate and stabilize cell-cell adhesion, to regulate the paracellular transit of ions and molecules and to maintain cell polarity. Moreover, we now consider the AJC as a hub of signal transduction that regulates cell-cell adhesion, gene transcription and cell proliferation and differentiation. The molecular components of the AJC are multiple and diverse and depending on the cellular context some of the proteins in this complex act as tumor suppressors or as promoters of cell transformation, migration and metastasis outgrowth. Here, we describe these new roles played by TJ and AJ proteins and their potential use in cancer diagnostics and as targets for therapeutic intervention.
    MeSH term(s) Adherens Junctions/genetics ; Adherens Junctions/metabolism ; Cell Adhesion/genetics ; Cell Differentiation/genetics ; Cell Movement/genetics ; Cell Polarity/genetics ; Cell Proliferation/genetics ; Cell Transformation, Neoplastic/genetics ; Gene Expression Regulation/genetics ; Humans ; Intercellular Junctions/genetics ; Neoplasms/genetics ; Signal Transduction/genetics ; Tight Junctions/genetics ; Tight Junctions/metabolism ; Transcription, Genetic ; Zonula Occludens-1 Protein/genetics
    Chemical Substances Zonula Occludens-1 Protein
    Language English
    Publishing date 2020-03-30
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2020.183278
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Zonula occludens

    Hernández-Guzmán, Christian / Gallego-Gutiérrez, Helios / Chávez-Munguía, Bibiana / Martín-Tapia, Dolores / González-Mariscal, Lorenza

    Cells

    2021  Volume 10, Issue 10

    Abstract: MAGUK protein ZO-2 is present at tight junctions (TJs) and nuclei. In MDCK ZO-2 knockdown (KD) cells, nuclei exhibit an irregular shape with lobules and indentations. This condition correlates with an increase in DNA double strand breaks, however cells ... ...

    Abstract MAGUK protein ZO-2 is present at tight junctions (TJs) and nuclei. In MDCK ZO-2 knockdown (KD) cells, nuclei exhibit an irregular shape with lobules and indentations. This condition correlates with an increase in DNA double strand breaks, however cells are not senescent and instead become resistant to UV-induced senescence. The irregular nuclear shape is also observed in isolated cells and in those without TJs, due to the lack of extracellular calcium. The aberrant nuclear shape of ZO-2 KD cells is not accompanied by a reduced expression of lamins A/C and B and lamin B receptors. Instead, it involves a decrease in constitutive and facultative heterochromatin, and microtubule instability that is restored with docetaxel. ZO-2 KD cells over-express SUN-1 that crosses the inner nuclear membrane and connects the nucleoskeleton of lamin A to nesprins, which traverse the outer nuclear membrane. Nesprins-3 and -4 that indirectly bind on their cytoplasmic face to vimentin and microtubules, respectively, are also over-expressed in ZO-2 KD cells, whereas vimentin is depleted. SUN-1 and lamin B1 co-immunoprecipitate with ZO-2, and SUN-1 associates to ZO-2 in a pull-down assay. Our results suggest that ZO-2 forms a complex with SUN-1 and lamin B1 at the inner nuclear membrane, and that ZO-2 and cell-cell contacts are required for a normal nuclear shape.
    MeSH term(s) Cell Communication/immunology ; Epithelium/metabolism ; Humans ; Transfection ; Zonula Occludens-2 Protein/metabolism
    Chemical Substances Zonula Occludens-2 Protein
    Language English
    Publishing date 2021-09-28
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells10102568
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Tight junction protein ZO-2 modulates the nuclear accumulation of transcription factor TEAD.

    Gallego-Gutiérrez, Helios / González-González, Laura / Ramírez-Martínez, Leticia / López-Bayghen, Esther / González-Mariscal, Lorenza

    Molecular biology of the cell

    2021  Volume 32, Issue 15, Page(s) 1347–1358

    Abstract: The presence of tight junction ... ...

    Abstract The presence of tight junction protein
    MeSH term(s) Animals ; Cell Line ; Cell Nucleus/metabolism ; Dogs ; Epithelial Cells/metabolism ; HEK293 Cells ; Humans ; Nuclear Localization Signals ; Phosphorylation ; Protein Binding ; Protein Kinase C-epsilon/metabolism ; Protein Processing, Post-Translational ; Protein Transport ; Rats ; Signal Transduction ; TEA Domain Transcription Factors/metabolism ; Zonula Occludens-2 Protein/metabolism
    Chemical Substances Nuclear Localization Signals ; TEA Domain Transcription Factors ; Zonula Occludens-2 Protein ; Protein Kinase C-epsilon (EC 2.7.11.13)
    Language English
    Publishing date 2021-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E20-07-0470
    Database MEDical Literature Analysis and Retrieval System OnLINE

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