Abstract
Desmosomes are the most prominent and mechanically important epidermal intercellular junctions. Transmembrane proteins of desmosomes, desmogleins and desmocollins, are responsible for extracellular binding and, thus, are important for interkeratinocyte cohesion. We show here, using three different approaches, that the extracellular "cores" of epidermal desmosomes contain a highly glycosylated antigen, different from desmosomal cadherins. This protein, recognised by KM48 monoclonal antibody, is likely to be involved in the processes of keratinocyte differentiation, desmosome turnover and epidermal cohesion.
MeSH terms
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Animals
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Antibodies, Monoclonal / immunology*
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Antigen-Antibody Reactions
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Autoantigens / immunology*
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Cadherins / immunology*
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Cell Adhesion Molecules / immunology
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Cell Differentiation
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Cytoskeletal Proteins / immunology
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Desmocollins
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Desmoglein 3
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Desmogleins
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Desmoplakins
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Desmosomes / immunology*
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Enzyme-Linked Immunosorbent Assay
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Epidermis / immunology
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Fluorescent Antibody Technique, Indirect
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Humans
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Immunoblotting
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Immunoglobulin M / immunology
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Keratinocytes / immunology
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Membrane Glycoproteins / immunology
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Mice
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Microscopy, Fluorescence
Substances
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Antibodies, Monoclonal
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Autoantigens
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Cadherins
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Cell Adhesion Molecules
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Cytoskeletal Proteins
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DSC1 protein, human
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DSC2 protein, human
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DSC3 protein, human
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DSG3 protein, human
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Desmocollins
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Desmoglein 3
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Desmogleins
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Desmoplakins
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Immunoglobulin M
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Membrane Glycoproteins