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Catenin dislocation in oral pemphigus vulgaris
- Publication Year :
- 2001
-
Abstract
- Cell-to-cell adhesion is mediated by cadherins (integral membrane proteins), which form a complex with catenins (cytoplasmatic proteins). While E-cadherin expression has been extensively studied in many human skin diseases, less is known about the expression levels of catenins in oral blistering diseases. The purpose of this study was to evaluate the role of these proteins in the pathogenesis of acantholysis in oral pemphigus vulgaris. We evaluated by immunohistochemistry beta- and gamma-catenin expression in 7 cases of oral pemphigus vulgaris (PV) at various stages of the disease and, as controls, in 18 healthy patients. Healthy cases showed, as reported in the literature, a strong reactivity with both beta- and gamma-catenins, with the intensity of staining progressively decreasing from the spinous to the keratinised layers of epithelium, which had a prevalent cellular membrane expression. In PV patients, we detected a loss of membrane expression of these molecules with a progressive displacement of the signal toward the cytosol and, for gamma-catenin, nuclear dislocation, particularly in areas with intense acantholysis.
- Subjects :
- Adult
Male
Cytosol
metabolism/pathology, Mouth Mucosa
Humans
metabolism, Cell Membrane
metabolism/pathology, Pemphigu
beta Catenin
Aged
Cell Nucleus
Cell Membrane
Mouth Mucosa
Epithelial Cells
metabolism/pathology, Female, Humans, Immunohistochemistry, Male, Middle Aged, Mouth Disease
Middle Aged
Cadherins
Immunohistochemistry
Adult, Aged, Autolysi
metabolism, Cytoskeletal Protein
Cytoskeletal Proteins
Protein Transport
metabolism/pathology, Protein Transport, Trans-Activators, beta Catenin, gamma Catenin
Desmoplakins
metabolism, Cell Nucleu
Trans-Activators
metabolism, Desmoplakins, Epithelial Cell
Female
metabolism, Cytosol
gamma Catenin
metabolism/pathology, Cadherin
Autolysis
Mouth Diseases
Pemphigus
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.pmid.dedup....1093ec4aede705ec83d6c9c91150ad4a