Intestinal epithelial cell protein phosphorylation in enteropathogenic Escherichia coli diarrhoea

Manjarrez-Hernández, H. Ángel; Aitken, A.; Baldwin, Thomas J.; Williams, Peter H.; Knutton, Stuart

doi:10.1016/0140-6736(92)90340-9

Cited by 75 publications

(46 citation statements)

References 9 publications

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“…Con A-induced capping of cell surface proteins induces RLC phosphorylation in Dictyostelium (21) as does colchicine-induced capping in mouse lymphoma cells (17). Cytoskeletal changes during capping also bear similarity to those observed in intestinal cells during adhesion of pathogenic Escherichia coli (19). In both conditions, a patch of actin and myosin is formed under a specific region of the plasma membrane.…”

Section: Discussionmentioning

confidence: 97%

“…This phosphorylation increases the actinactivated ATPase activity of myosin and is carried out by myosin light chain kinase (MLCK). In animal cells, increased RLC phosphorylation is observed during mitosis (13)(14)(15), after exposure to chemoattractant (16), during colchicine-induced capping (17), in agonist-driven shape changes (18), and in response to adsorption of pathogenic bacteria to the intestinal cell surface (19). In Dictyostelium, activating RLC phosphorylation is induced after exposure to chemoattractant (20) and during Con A-induced capping (21).…”

mentioning

confidence: 99%

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MLCK-A, an unconventional myosin light chain kinase from Dictyostelium , is activated by a cGMP-dependent pathway

Silveira

Smith

Tan

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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Section: Discussionmentioning

confidence: 97%

mentioning

confidence: 99%

MLCK-A, an unconventional myosin light chain kinase from Dictyostelium , is activated by a cGMP-dependent pathway

Silveira

Smith

Tan

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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“…Beneath this lesion is an accumulation of host cytoskeletal proteins (Knutton et al, 1987;1989;Finlay et al, 1992), many of which are phosphorylated upon infection by EPEC (Manjarrez-Hernandez et al, 1992;Rosenshine et al, 1992). The predominant protein that is phosphorylated in response to EPEC infection is the 20 kDa light chain of myosin (MLC 20 ;Manjarrez-Hernandez et al, 1992;Yuhan et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

“…The predominant protein that is phosphorylated in response to EPEC infection is the 20 kDa light chain of myosin (MLC 20 ;Manjarrez-Hernandez et al, 1992;Yuhan et al, 1997). In addition to controlling smooth muscle contraction, MLC 20 phosphorylation also regulates various non-muscle events including tight junction (TJ) permeability (Madara and Pappenheimer, 1987;Hecht et al, 1996;Turner et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions

Simonović¹,

Rosenberg²,

Koutsouris³

et al. 2000

Cell Microbiol

238

186

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SummaryEnteropathogenic Escherichia coli (EPEC) increases tight junction permeability in part by phosphorylating the 20 kDa myosin light chain (MLC 20 ) that induces cytoskeletal contraction. The impact of this enteric pathogen on specific tight junction (TJ) proteins has not been investigated. We examined the effect of EPEC infection on occludin localization and phosphorylation in intestinal epithelial cells. After infection by EPEC, a progressive shift of occludin from a primarily TJ-associated domain to an intracellular compartment occurred, as demonstrated by immunofluorescent staining. A reverse in the ratio of phosphorylated to dephosphorylated occludin accompanied this morphological change. Eradication of EPEC with gentamicin resulted in the normalization of occludin localization and phosphorylation. The serine/threonine phosphatase inhibitor, calyculin A, prevented these events. The EPEC-associated decrease in transepithelial electrical resistance, a measure of TJ barrier function, returned to baseline after gentamicin treatment. Non-pathogenic E. coli, K-12, did not induce these changes. Transformation of K-12 with the pathogenicity island of EPEC, however, conferred the phenotype of wild-type EPEC. Deletion of specific EPEC genes encoding proteins involved in EPEC type III secretion markedly attenuated these effects. These findings suggest that EPEC-induced alterations in occludin contribute to the pathophysiology associated with this infection.

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“…Both in vitro and in vivo studies have identified several bacterial and host components participating in these EPEC-induced alterations of the host cell. EPEC-host cell interaction induces host protein phosphorylation events and inositol phosphate and calcium fluxes, as well as cytoskeletal rearrangements (1,7,8,10,20,26,32). Several of these events are dependent on the secretion of at least two EPEC-secreted proteins (EspA and EspB, formerly EaeB) and a dedicated type III secretion apparatus (15,18,19).…”

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confidence: 99%

Gastrointestinal Tract

2006

Understanding Drug Release and Absorption Mechanisms

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The pathogenicity of enteropathogenic Escherichia coli (EPEC) is associated with the expression and secretion of specific bacterial factors. EspB is one such secreted protein which is required to trigger host signaling pathways resulting in effacement of microvilli and cytoskeletal rearrangements. These events presumably contribute to the ensuing diarrhea associated with EPEC infections. EPEC encounters several environmental changes and stimuli during its passage from the external environment into the host gastrointestinal tract. In this paper we show that the secretion of EspB is subject to environmental regulation, and maximal secretion occurs under conditions reminiscent of those in the gastrointestinal tract. Thus, secretion is maximal at 37°C, pH 7, and physiological osmolarity. In addition, maximal secretion requires the presence of sodium bicarbonate and calcium and is stimulated by millimolar concentrations of Fe(NO 3 ) 3 . The secretion of the four other EPEC-secreted proteins appears to be modulated in a manner similar to that of EspB. Our results also show that secretion is not dependent on CO 2 , as originally reported by Haigh et al. (FEMS Microbiol. Lett. 129: 63-67, 1995), but that CO 2 more likely acts as a component of the medium buffering system, since CO 2 dependence was abolished by the use of alternative buffers.

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Intestinal epithelial cell protein phosphorylation in enteropathogenic Escherichia coli diarrhoea

Cited by 75 publications

References 9 publications

MLCK-A, an unconventional myosin light chain kinase from Dictyostelium , is activated by a cGMP-dependent pathway

MLCK-A, an unconventional myosin light chain kinase from Dictyostelium , is activated by a cGMP-dependent pathway

Enteropathogenic Escherichia coli dephosphorylates and dissociates occludin from intestinal epithelial tight junctions

Gastrointestinal Tract

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