Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli
| Autor: | H A Manjarrez Hernandez, Peter H. Williams, A Aitken, S F Brooks, T J Baldwin, S Knutton |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Immunology
Biology medicine.disease_cause Microbiology Bacterial Adhesion Tumor Cells Cultured medicine Humans Protein phosphorylation Phosphorylation Enteropathogenic Escherichia coli Protein kinase A Laryngeal Neoplasms Escherichia coli Escherichia coli Infections Protein Kinase C Protein kinase C chemistry.chemical_classification Proteins Phosphoproteins biology.organism_classification Enterobacteriaceae Enzyme Activation Molecular Weight Infectious Diseases Enzyme chemistry Parasitology Research Article |
| Zdroj: | Infection and Immunity. 58:761-765 |
| ISSN: | 1098-5522 0019-9567 |
| DOI: | 10.1128/iai.58.3.761-765.1990 |
| Popis: | Infection of HEp-2 monolayers with enteropathogenic Escherichia coli 2036-80 (O119) stimulated phosphorylation of several target cell proteins, the most prominent of which had apparent molecular weights of 21,000 and 29,000. Proteins of the same size were phosphorylated in response to known activators of the calcium-phospholipid-dependent protein kinase C. Screening of clinical isolates of various O serogroups revealed that all strains able to form the characteristic attaching and effacing lesion of enteropathogenic E. coli showed elevated phosphorylation of 21,000- and 29,000-dalton protein species. |
| Databáze: | OpenAIRE |
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