Role of protein kinase C in the deficient gap junctional intercellular communication of K-ras-transformed murine lung epithelial cells
Autor: | K, Cesen-Cummings, K A, Warner, R J, Ruch |
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Rok vydání: | 1999 |
Předmět: |
Flavonoids
Indoles Lung Neoplasms Plants Medicinal Chamomile Gap Junctions Epithelial Cells Cell Communication Oligonucleotides Antisense Maleimides Mice Cell Transformation Neoplastic Genes ras Connexin 43 Oils Volatile Animals Anticarcinogenic Agents Tetradecanoylphorbol Acetate Lovastatin Enzyme Inhibitors Phosphorylation Lung Protein Kinase C Cell Line Transformed |
Zdroj: | Anticancer research. 18(6A) |
ISSN: | 0250-7005 |
Popis: | Protein kinase C (PKC) activity is increased and gap junctional intercellular communication (GJIC) is decreased frequently in Ras-transformed cells. We investigated the roles of Ras and PKC in the deficient gap junctional intercellular communication (GJIC) of K-ras-transformed E9 mouse lung carcinoma cells.GJIC was measured by fluorescent dye microinjection. Ras activity was blocked with lovastatin or a K-ras antisense oligonucleotide. PKC activity was inhibited with GF 109203X or apigenin or was downregulated by overnight treatment with 12-O-tetradecanoylphorbol-13-acetate. The content and phosphorylation of the gap junction protein, connexin43 (Cx43), was assessed by Western blot.E9 cell GJIC was increased two-three fold by lovastatin, the K-ras antisense oligonucleotide, and PKC inhibition/downregulation. Cx43 content and phosphorylation were unchanged, however.Oncogenic Ras blocks GJIC in E9 cells through a PKC-dependent mechanism, but this does not directly involve Cx43 expression or phosphorylation. |
Databáze: | OpenAIRE |
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