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  1. Article ; Online: Desmosealin and other components of the epidermal extracellular matrix.

    Sandjeu, Y / Haftek, M

    Journal of physiology and pharmacology : an official journal of the Polish Physiological Society

    2009  Volume 60 Suppl 4, Page(s) 23–30

    Abstract: Integrity of the skin is necessary for maintaining body's homeostasis. Barrier function of human skin largely depends on the final product of epidermal cell differentiation, the horny layer, i.e. stratum corneum. As epidermis is constantly in self- ... ...

    Abstract Integrity of the skin is necessary for maintaining body's homeostasis. Barrier function of human skin largely depends on the final product of epidermal cell differentiation, the horny layer, i.e. stratum corneum. As epidermis is constantly in self-renewal, the superficial desquamation is adequately compensated by keratinocyte proliferation in epidermal basal layer. Cohesion in the epidermis depends on the presence of specialized adhering junctions, desmosomes, and their modified version encountered in the horny layer, corneodesmosomes. These structures must be finely regulated to allow a regular flow of differentiating keratinocytes through the epidermal layers and their release at the top of the skin, without compromising tissue resilience and cohesion. Extracellular matrix (ECM) molecules, which fill the inter-keratinocyte spaces in living epidermal layers, are involved in tissue hydration, nutrition, and regulation of cell proliferation and differentiation. In the stratum corneum, extracellular lipids self-organize into multilayered sheets, essential for establishing of the permeability barrier. Desmosealin is a new epidermal proteoglycan, part of the tissue-specific ECM, that shows affinity to the extracellular compartment of desmosomes. This highly glycosylated molecule may play a role in the protection of desmosomes against premature proteolysis of its components, and, thus, in the skin barrier function.
    MeSH term(s) Animals ; Desmosomes/metabolism ; Epidermis/chemistry ; Epidermis/metabolism ; Extracellular Matrix/chemistry ; Extracellular Matrix/metabolism ; Humans ; Hyaluronic Acid/metabolism ; Proteoglycans/metabolism ; Syndecan-1/chemistry ; Syndecan-1/metabolism
    Chemical Substances Proteoglycans ; SDC1 protein, human ; Syndecan-1 ; Hyaluronic Acid (9004-61-9)
    Language English
    Publishing date 2009-10
    Publishing country Poland
    Document type Journal Article ; Review
    ZDB-ID 1125221-2
    ISSN 1899-1505 ; 0867-5910 ; 0044-6033
    ISSN (online) 1899-1505
    ISSN 0867-5910 ; 0044-6033
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Human epidermal desmosome-enriched tissue fractions for analytical and prospective studies.

    Sandjeu, Yongoua / Callejon, Sylvie / Vincent, Claude / Haftek, Marek

    Experimental dermatology

    2011  Volume 20, Issue 4, Page(s) 357–360

    Abstract: Here, we report a method, adapted to the human epidermis, allowing isolation of desmosomes in small tissue fractions. The methods previously developed for animal skin did not work efficiently with human tissue. Enrichment of desmosomes was performed by ... ...

    Abstract Here, we report a method, adapted to the human epidermis, allowing isolation of desmosomes in small tissue fractions. The methods previously developed for animal skin did not work efficiently with human tissue. Enrichment of desmosomes was performed by the association of two incubation steps in acidic solutions containing detergent NP-40 at two different concentrations followed by a sonication step. The suspension was centrifuged twice: first to remove the heavy cell fragments and then at 16000 g on a discontinuous sucrose gradient. A desmosome-enriched fraction (DsF) was collected at the 30-50% sucrose interface. We demonstrate by immunoelectron microscopy and by western blotting that the central part of the desmosome structure is preserved as well as the antigenicity of its components. Our approach, allowing a significant enrichment of the cell fractions containing desmosomes, can be used to immunize animals and create new antibodies directed against desmosomal components. Using this strategy, new and so far poorly studied molecules incorporated into the desmosome cores could be targeted more easily.
    MeSH term(s) Cell Fractionation/methods ; Desmosomes ; Epidermis/cytology ; Humans ; Immunohistochemistry ; Microscopy, Electron
    Language English
    Publishing date 2011-04
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1130936-2
    ISSN 1600-0625 ; 0906-6705
    ISSN (online) 1600-0625
    ISSN 0906-6705
    DOI 10.1111/j.1600-0625.2011.01252.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Compartmentalization of the human stratum corneum by persistent tight junction-like structures.

    Haftek, Marek / Callejon, Sylvie / Sandjeu, Yongoua / Padois, Karine / Falson, Françoise / Pirot, Fabrice / Portes, Pascal / Demarne, Frédéric / Jannin, Vincent

    Experimental dermatology

    2011  Volume 20, Issue 8, Page(s) 617–621

    Abstract: Several tight junction (TJ) proteins were detected in the living layers of adult human epidermis, and TJ-like membrane ridges were observed at the top of the stratum granulosum (SG) in freeze-fracture studies. We applied standard and immunoelectron ... ...

    Abstract Several tight junction (TJ) proteins were detected in the living layers of adult human epidermis, and TJ-like membrane ridges were observed at the top of the stratum granulosum (SG) in freeze-fracture studies. We applied standard and immunoelectron microscopy to look for TJ-derived structures in the stratum corneum (SC) of human adult epidermis and in cornified envelopes purified from the plantar SC. Besides confirming claudin-1 labelling in the proximity of SG desmosomes, we also observed immunolocalization near corneodesmosomes in the lower SC. In addition, TJ proteins were consistently detected in the purified cornified envelopes. Lateral but not horizontal walls of the corneocytes showed frequent points of molecular fusion between lipid envelopes. These structural associations were very frequently localized at the top of the lateral corneocyte membranes, thus sealing the extremities of lateral intercorneocyte spaces. We propose that TJ-like structures persist in the SC and contribute to the reinforcement of lateral contacts and to the formation of membrane interdigitations between corneocytes. Their presence could contribute to subdivision of the extracellular spaces of SC into consecutive individualized compartments. Intercellular lipids, enzymes and other (glyco)protein content could thus evolve in the keratinized epidermal layer at different paces, as preprogrammed in the underlying living cells and influenced by the environment, e.g. humidity. Such situation might explain differences in the degradation rates between the 'peripheral' and the 'non-peripheral' corneodesmosomes observed during physiological desquamation, as previously suggested by us and others.
    MeSH term(s) Claudin-1 ; Desmosomes/ultrastructure ; Epidermis/cytology ; Epidermis/metabolism ; Epidermis/ultrastructure ; Humans ; Keratinocytes/cytology ; Keratinocytes/metabolism ; Keratinocytes/ultrastructure ; Membrane Lipids/metabolism ; Membrane Proteins/metabolism ; Membrane Proteins/ultrastructure ; Microscopy, Immunoelectron ; Occludin ; Tight Junctions/metabolism ; Tight Junctions/ultrastructure
    Chemical Substances CLDN1 protein, human ; Claudin-1 ; Membrane Lipids ; Membrane Proteins ; OCLN protein, human ; Occludin
    Language English
    Publishing date 2011-08
    Publishing country Denmark
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1130936-2
    ISSN 1600-0625 ; 0906-6705
    ISSN (online) 1600-0625
    ISSN 0906-6705
    DOI 10.1111/j.1600-0625.2011.01315.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: A natural structural variant of the mouse TCR beta-chain displays intrinsic receptor function and antigen specificity.

    Aublin, Anne / Ciofani, Maria / Willkomm, Nancy / Hamrouni, Abdelbasset / Szymczak-Workman, Andrea L / Takahashi, Tomio / Sandjeu, Yongoua / Guillaume, Philippe / Vignali, Dario A A / Michielin, Olivier / Zúñiga-Pflücker, Juan Carlos / Maryanski, Janet L

    Journal of immunology (Baltimore, Md. : 1950)

    2005  Volume 177, Issue 12, Page(s) 8587–8594

    Abstract: The Cbeta0 alternate cassette exon is located between the Jbeta1 and Cbeta1 genes in the mouse TCR beta-locus. In T cells with a VDJbeta1 rearrangement, the Cbeta0 exon may be included in TCRbeta transcripts (herein called TCRbeta-Cbeta0 transcripts), ... ...

    Abstract The Cbeta0 alternate cassette exon is located between the Jbeta1 and Cbeta1 genes in the mouse TCR beta-locus. In T cells with a VDJbeta1 rearrangement, the Cbeta0 exon may be included in TCRbeta transcripts (herein called TCRbeta-Cbeta0 transcripts), potentially inserting an additional 24 aa between the V and C domains of the TCR beta-chain. These TCRbeta splice isoforms may be differentially regulated after Ag activation, because we detected TCRbeta-Cbeta0 transcripts in a high proportion (>60%) of immature and mature T cells having VDJbeta1 rearrangements but found a substantially reduced frequency (<35%) of TCRbeta-Cbeta0 expression among CD8 T cells selected by Ag in vivo. To study the potential activity of the TCRbeta-Cbeta0 splice variant, we cloned full-length TCR cDNAs by single-cell RT-PCR into retroviral expression vectors. We found that the TCRbeta-Cbeta0 splice isoform can function during an early stage of T cell development normally dependent on TCR beta-chain expression. We also demonstrate that T hybridoma-derived cells expressing a TCRbeta-Cbeta0 isoform together with the clonally associated TCR alpha-chain recognize the same cognate peptide-MHC ligand as the corresponding normal alphabetaTCR. This maintenance of receptor function and specificity upon insertion of the Cbeta0 peptide cassette signifies a remarkable adaptability for the TCR beta-chain, and our findings open the possibility that this splice isoform may function in vivo.
    MeSH term(s) Animals ; Cell Line ; Cloning, Molecular ; Epitopes ; Gene Rearrangement ; Genes, T-Cell Receptor beta ; Hybridomas/cytology ; Hybridomas/metabolism ; Mice ; Protein Isoforms ; Receptors, Antigen, T-Cell, alpha-beta/chemistry ; Receptors, Antigen, T-Cell, alpha-beta/genetics ; Receptors, Antigen, T-Cell, alpha-beta/physiology ; T-Lymphocytes/cytology ; T-Lymphocytes/metabolism
    Chemical Substances Epitopes ; Protein Isoforms ; Receptors, Antigen, T-Cell, alpha-beta
    Language English
    Publishing date 2005-04-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3056-9
    ISSN 1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
    ISSN (online) 1550-6606
    ISSN 0022-1767 ; 1048-3233 ; 1047-7381
    DOI 10.4049/jimmunol.177.12.8587
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ud II Zs.37: Show issues Location:
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