Clostridium sordellii cytotoxin induces phosphorylation of an 80,000 mol. wt protein in McCoy cultured cells
| Autor: | Gaynor A. Green, Henri Monteil, Raymonde Girardot, Véronique Schué |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Silver Staining
Cell Bacterial Toxins Immunoblotting Clostridium difficile toxin B Clostridium sordellii Biology Toxicology medicine.disease_cause chemistry.chemical_compound Ethers Cyclic Okadaic Acid medicine Phosphoprotein Phosphatases Humans Electrophoresis Gel Two-Dimensional Phosphorylation Cells Cultured Chromatography High Pressure Liquid Clostridium Toxin Cytotoxins Synovial Membrane Okadaic acid biology.organism_classification Molecular Weight Caldesmon Cytoskeletal Proteins medicine.anatomical_structure Biochemistry Mechanism of action chemistry biology.protein Calmodulin-Binding Proteins medicine.symptom |
| Zdroj: | Toxicon : official journal of the International Society on Toxinology. 32(12) |
| ISSN: | 0041-0101 |
| Popis: | The cytotoxins from Clostridium difficile (toxin B) and Clostridium sordellii (toxin L) induce rounding of cultured cells. The cellular effects induced by these two cytotoxins are clearly distinct, suggesting that both toxins use a similar, but not identical mechanism for cell intoxication. We have employed the technique of two-dimensional PAGE for the separation of 32P-labelled cell lysates of McCoy cultured cells to investigate changes in the phosphorylation status of cellular proteins after treatment with toxin B and with toxin L. The two-dimensional electrophoresis patterns suggest the implication of an 80,000 mol. wt cellular protein (named pp80c) in the cytopathic action of the cytotoxin from C. sordellii. This protein shows immunoreactivity with non-muscle caldesmon. Toxin B, however, does not affect the phosphorylation of pp80c, but alters the phosphorylation of another cellular protein, pp77, indicating another mechanism for cell intoxication. In addition, our experiments suggest that the mechanism of action of okadaic acid, a phosphatase inhibitor which causes cell rounding similar to that induced by C. sordellii, and these two cytotoxins are different. |
| Databáze: | OpenAIRE |
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