Corneodesmosin, a Component of Epidermal Corneocyte Desmosomes, Displays Homophilic Adhesive Properties

Corneodesmosomes, the modified desmosomes of the uppermost layers of the epidermis, play an important role in corneocyte cohesion. Corneodesmosin is a secreted glycoprotein located in the corneodesmosomal core and covalently linked to the cornified envelope of corneocytes. Its glycine- and serine-ri...

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Bibliographic Details
Published in:The Journal of biological chemistry 2002-02, Vol.277 (7), p.5024-5029
Main Authors: Jonca, Nathalie, Guerrin, Marina, Hadjiolova, Krassimira, Caubet, Cecile, Gallinaro, Helene, Simon, Michel, Serre, Guy
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Animals
Blotting, Western
Calcium - metabolism
Cell Adhesion
Cell Movement
Desmosomes - metabolism
DNA, Complementary - metabolism
Dose-Response Relationship, Drug
Epidermis - metabolism
Escherichia coli - metabolism
Fibroblasts - metabolism
Glutathione Transferase - metabolism
Glycine - chemistry
Glycoproteins - chemistry
Humans
Immunoblotting
Intercellular Signaling Peptides and Proteins
Mice
Microscopy, Fluorescence
Protein Binding
Protein Structure, Tertiary
Recombinant Fusion Proteins - metabolism
Recombinant Proteins - metabolism
Serine - chemistry
Time Factors
Transfection
Trypsin - pharmacology
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Summary:Corneodesmosomes, the modified desmosomes of the uppermost layers of the epidermis, play an important role in corneocyte cohesion. Corneodesmosin is a secreted glycoprotein located in the corneodesmosomal core and covalently linked to the cornified envelope of corneocytes. Its glycine- and serine-rich NH 2 -terminal domain may fold to give structural motifs similar to the glycine loops described in epidermal cytokeratins and loricrin and proposed to display adhesive properties. A chimeric protein comprising human corneodesmosin linked to the transmembrane and cytoplasmic domains of mouse E-cadherin was expressed in mouse fibroblasts to test the ability of corneodesmosin to promote cell-cell adhesion. Classic aggregation assays indicated that corneodesmosin mediates homophilic cell aggregation. Moreover, Ca 2+ depletion showed a moderate effect on aggregation. To assess the involvement of the glycine loop domain in adhesion, full-length corneodesmosin, corneodesmosin lacking this domain, or this domain alone were expressed as glutathione S -transferase fusion proteins and tested for protein-protein interactions by overlay binding assays. The results confirmed that corneodesmosin presents homophilic interactions and indicated that its NH 2 -terminal glycine loop domain is sufficient but not strictly necessary to promote binding. Altogether, these results provide the first experimental evidence for the adhesive properties of corneodesmosin and for the involvement of its glycine loop domain in adhesion.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M108438200