Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli

Baldwin, Thomas J.; Brooks, Susan F.; Knutton, Stuart; Hernández, Helena; Aitken, A.; Williams, Peter H.

doi:10.1128/iai.58.3.761-765.1990

Cited by 69 publications

(26 citation statements)

References 32 publications

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“…Inhibition of this elevation by dantrolene suggests that the calcium is released from inositol 1,4,5-trisphosphate (IP3)sensitive stores (12). This [Ca]i elevation stimulates calciumdependent serine/threonine protein kinases to phosporylate several host cell proteins, including the myosin light chain (13)(14)(15). In this communication we examined whether EPEC triggered the formation of IPs in infected epithelial cells.…”

Section: Discussionmentioning

confidence: 99%

A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells.

Foubister

Rosenshine

1994

The Journal of Experimental Medicine

117

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SummaryEnteropathogenic Escherichia coli (EPEC) is a bacterial pathogen that causes diarrhea in infants by adhering to intestinal epithelial cells. EPEC induces host cell protein phosphorylation and increases intraceUular calcium levels that may function to initiate cytoskeletal rearrangement. We found that EPEC triggers the release of inositol phosphates (IPs) after adherence of bacteria to cultured epithelial cells. We also demonstrated that the EPEC-induced flux of IPs precedes actin rearrangement and bacterial invasion. EPEC mutants and tyrosine protein kinase inhibitors were used to establish that formation of IPs is dependent on tyrosine phosphorylation of a 90-kD HeLa protein. Collectively these results suggest that EPEC-induced tyrosine phosphorylation of a host cell substrate(s) leads to release of IPs, which may then trigger cytoskeletal rearrangement.

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Section: Discussionmentioning

confidence: 99%

A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells.

Foubister

Rosenshine

1994

The Journal of Experimental Medicine

117

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“…EPEC activates several signaling molecules like NF-kB , MAP kinases (Czerucka et al, 2001) and protein kinase C (Baldwin et al, 1990). EPEC infection stimulates phosphorylation of myosin light chain by myosin light chain kinase (MLCK) and this results in intestinal barrier dysfunction (Yuhan et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Modulation of tight junction barrier function by outer membrane proteins of enteropathogenic Escherichia coli: Role of F‐actin and junctional adhesion molecule‐1

Puthenedam

Williams

Lakshmi

et al. 2007

Cell Biology International

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Enteropathogenic Escherichia coli (EPEC) is a major cause of infantile diarrhea. In this work we investigated the effect of outer membrane proteins (OMP) of EPEC on barrier integrity and the role of actin, junctional adhesion molecule (JAM) and signaling pathways contributing to these changes. Barrier function was assessed by transepithelial electrical resistance (TER). OMP of wild type EPEC, eaeA and maltoporin mutants decreased TER levels of Caco-2 cells. The OMP of espB mutant was deficient in decreasing TER of Caco-2 cells. The proteinase K-digested wild type OMP and EAF mutant OMP did not cause any change in barrier function. Our previous studies have demonstrated that EPEC OMP induced changes in cadherin junctions of Caco-2 cells. Immunofluorescence revealed disruption in actin cytoskeleton by EPEC OMP. However, no change in expression of junctional adhesion molecule-1 was observed. NF-kappaB inhibitor slightly blocked the decrease in TER and protected against actin disruption while ERK1/2 inhibitor had no effect in blocking these changes. In conclusion, our data suggest that the OMP of EPEC alter intestinal barrier function by disrupting actin cytoskeleton and signaling pathways like NF-kappaB may have a role in regulating barrier changes.

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“…Coincident with AE lesion formation, EPEC trigger host signal-transduction pathways (Baldwin et al, 1990;Foubister et al, 1994;Rosenshine et al, 1992). These pathways are manifest by a number of biochemical hallmarks, including rises in intracellular levels of calcium and inositol triphosphate and by the phosphorylation of several host proteins.…”

Section: Introductionmentioning

confidence: 99%

**A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K‐12**

McDaniel

Kaper

1997

Molecular Microbiology

503

407

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SummaryAttaching and effacing (AE) bacteria are a diverse group of gastrointestinal pathogens, comprising members of four genera, that cause the intestinal epithelial microvilli to be replaced with raised clusters of filamentous actin that conform to the surface of attached bacteria. We have cloned a 35.4 kb 'pathogenicity island' from the prototype AE bacterium, enteropathogenic Escherichia coli, containing all previously described AE genes. Transfer of this pathogenicity island to avirulent E. coli converts the recipients into strains that secrete virulence proteins, induce host signaltransduction pathways, and cause AE lesions on cultured epithelial cells. These results demonstrate that this pathogenicity island contains all pathogen-specific genes necessary for inducing AE lesions, and that the defining feature of this class of pathogens can be acquired by an avirulent bacterium in a single genetic step.

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Protein phosphorylation by protein kinase C in HEp-2 cells infected with enteropathogenic Escherichia coli

Cited by 69 publications

References 32 publications

A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells.

A diarrheal pathogen, enteropathogenic Escherichia coli (EPEC), triggers a flux of inositol phosphates in infected epithelial cells.

Modulation of tight junction barrier function by outer membrane proteins of enteropathogenic Escherichia coli: Role of F‐actin and junctional adhesion molecule‐1

**A cloned pathogenicity island from enteropathogenic Escherichia coli confers the attaching and effacing phenotype on E. coli K‐12**

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