Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli.
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.
Department of Genetics, University of Leicester, United Kingdom.
T J
TJ
Baldwin
S F
SF
Brooks
S
S
Knutton
H A
HA
Manjarrez Hernandez
A
A
Aitken
P H
PH
Williams
D001422:Bacterial Adhesion; D004789:Enzyme Activation; D004927:Escherichia coli Infections / Q000378:metabolism*; D006801:Humans; D007822:Laryngeal Neoplasms / Q000201:enzymology; D008970:Molecular Weight; D010750:Phosphoproteins / Q000032:analysis; D010766:Phosphorylation; D011493:Protein Kinase C / Q000502:physiology*; D011506:Proteins / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D010750:Phosphoproteins; D011506:Proteins; D011493:Protein Kinase C