Desmosomes are Regulated by Protein Kinase C in Primary Rat Epithelial Cells
Autor: | Nicole Martin, Nadine Forest, A.H.M. Shabana, Laurence Amar, M. Oboeuf |
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Rok vydání: | 1998 |
Předmět: |
Keratinocytes
Cytoplasm Indoles Macromolecular Substances Desmoplakins Plakoglobin Biology Cell morphology Desmoglein Maleimides Rats Sprague-Dawley Tongue Desmosome Cell Adhesion Morphogenesis medicine Animals Enzyme Inhibitors Phosphorylation Cells Cultured Protein Kinase C Protein kinase C integumentary system Epithelial Cells Desmosomes General Medicine Rats Cell biology Microscopy Electron medicine.anatomical_structure Microscopy Fluorescence Desmosome assembly Tetradecanoylphorbol Acetate Protein Processing Post-Translational |
Zdroj: | Cell Adhesion and Communication. 5:1-12 |
ISSN: | 1029-2314 |
DOI: | 10.3109/15419069809005594 |
Popis: | In the present study, we addressed the possible relevance of protein kinase C (PKC) in the regulation of intracytoplasmic desmosome assembly. Treatment of cultured rat lingual and epidermal keratinocytes with a potent and highly selective PKC inhibitor (GF109203X) induced an increase in granular labelling for major desmosomal proteins, desmoplakins, desmoglein and plakoglobin, both intracellularly and at the cell surface. This was associated with the formation of ultrastructurally recognizable desmosomes deep in the cytoplasm and increase in intercellular desmosome number. In contrast, PKC activation upon short exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) resulted in altered cell morphology, loss of intercellular contact and accumulation of desmosomal proteins in the juxtanuclear zone. On the other hand, PKC depletion by long term TPA treatment re-established cell-cell contact, where desmosomal markers were exclusively redistributed. Taken together, these results suggest that inhibition of PKC is required for intracytoplasmic as well as intercellular desmosome assembly, whereas its activation may regulate disassembly process. |
Databáze: | OpenAIRE |
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