Intestinal epithelial cell protein phosphorylation in enteropathogenic Escherichia coli diarrhoea

Lancet. 1992 Feb 29;339(8792):521-3. doi: 10.1016/0140-6736(92)90340-9.

Abstract

The ability of enteropathogenic Escherichia coli (EPEC) to cause diarrhoea in man is associated with the formation of characteristic histopathological lesions in small-intestine enterocytes, with gross cytoskeletal damage and loss of brush-border microvilli. Investigation of enterocyte protein phosphorylation in response to EPEC infection showed that the major phosphorylated protein, identified by immunoprecipitation, is myosin light-chain--an important cytoskeletal protein known to affect actin organisation in non-muscle cells. High enterocyte concentrations of actin and myosin were observed at sites of bacterial infection. Our findings indicate that enterocyte cytoskeletal changes in response to EPEC may be directly triggered by bacterial adherence through signal transduction pathways that stimulate protein kinase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Bacterial Adhesion
  • Cytoskeletal Proteins / metabolism*
  • Diarrhea / metabolism*
  • Diarrhea / microbiology
  • Escherichia coli / physiology
  • Escherichia coli Infections / metabolism*
  • Escherichia coli Infections / microbiology
  • Humans
  • Intestinal Mucosa / metabolism
  • Intestinal Mucosa / microbiology
  • Intestine, Small / metabolism*
  • Myosins / metabolism
  • Phosphorylation
  • Protein Kinases / metabolism

Substances

  • Actins
  • Cytoskeletal Proteins
  • Protein Kinases
  • Myosins