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  • Blackwell Publishing Ltd  (5)
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  • 1
    Electronic Resource
    Electronic Resource
    STa-induced translocation of protein kinase C from cytosol to membrane in rat enterocytes (2001)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 204 (2001), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Escherichia coli heat stable enterotoxin (STa) binds to isolated rat intestinal epithelial cells and triggers a cascade reaction including increase of intracellular calcium levels ([Ca2+]i) and membrane bound protein kinase C (PKC) activity. In response to STa, the cytosolic PKC activity falls from 110 to 35 nmol with increase of membrane bound PKC activity from 15 to 78 nmol. Furthermore, the increase of PKC activity induced by STa treatment was always preceded by an increase in [Ca2+]i. Cytosolic [Ca2+]i was significantly higher (161 nM) in STa treated cells as compared to untreated cells (51.3 nM). In addition, immunoblot performed on extracts of STa treated rat enterocytes with a monoclonal antibody against PKC α showed a prominent band of PKC α. Translocation of PKC α could be blocked by dantrolene, a drug which inhibits the mobilisation of [Ca2+]i from the intracellular store. Our results, therefore, provide evidence for the role of [Ca2+]i in STa treated cells for the translocation of PKC α from cytosol to membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.2001.tb10864.x
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Escherichia coli heat-stable enterotoxin (ST) on calcium uptake by rat intestinal Brush-Border Membrane Vesicles (BBMV) (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 26 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A partially purified Escherichia coli heat-stable (ST) enterotoxin had been shown to increase the 45Ca2+ uptake by rat intestinal brush-border membrane vesicles (BBMV). The effect of ST enterotoxin on calcium uptake by BBMV was significant compared with the control and was also dose-dependent. The stimulation of calcium uptake by ST enterotoxin was inhibited by chemical agents which block the calcium entry into the cell. These data indicate that the ST acts as calcium ionophore in this particular system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb01606.x
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  • 3
    Electronic Resource
    Electronic Resource
    Comparison of cytosolic levels of calcium and G actin in diffuse and localised adherent Escherichia coli-infected HeLa cells (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 135 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract In the present study we compared the intracellular level of free calcium ([Ca2+]i) and monomeric (G)/total (G + F) actin ratio in HeLa cells infected with diffuse (DAEC) and localised adherent Escherichia coli (LAEC). The level of [Ca2+]i was increased in both DAEC- and LAEC-infected HeLa cells. However, studies with EGTA- and dantrolene-treated cells and also suspension of cells in Ca2+-free buffer suggested that the rise of [Ca2+]i in DAEC-infected cells was due to the influx of Ca2+ from extracellular medium, whereas Ca2+ mobilisation from the intracellular stores was responsible for the enhancement of [Ca2+]i in LAEC-infected cells. It was also evident that the infection of HeLa cells with DAEC and LAEC caused alteration of G / G + F actin ratio as compared to that of control cells. The ratio was much lower in LAEC-infected cells than that of DAEC-infected ones. Moreover, cytochalasin B inhibited both DAEC and LAEC invasion to HeLa cells, suggesting further the role of microfilaments in the invasion process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb07996.x
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  • 4
    Electronic Resource
    Electronic Resource
    Phosphoinositide (PI) hydrolysis by phospholipase C is accelerated by heat-stable (ST) E. coli enterotoxin in rat intestine (1985)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 30 (1985), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A partially purified E. coli heat-stable (ST) enterotoxin stimulated the phosphoinositide (PI)-specific phospholipase C (PLC) activity of the rat intestine. The effect of ST on PI-specific PLC was significant compared with the control. The importance of PI-specific phospholipase C as a potential agent to promote calcium translocation across the plasma membrane, was discussed in this communication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00977.x
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  • 5
    Electronic Resource
    Electronic Resource
    Evidence for protein kinase C stimulation in rat enterocytes pretreated with heat stable enterotoxin of Escherichia coli (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 110 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Rat intestinal epithelial cells were isolated and the activity of the calcium- and phospholipid-dependent protein kinase C (PKC) was investigated. The stimulation of activity by Escherichia coli heat stable enterotoxin (STa) was about 5-fold compared to control activity (16.91 ± 1.69 vs 93.56 ± 10.40 nmol/mg protein/min) and was dose dependent. Maximum enzyme activity was observed after incubation for 1 min with 6 ng of purified STa. The synergistic effects of calcium, phosphatidylserine and diolein on the enzyme activity were noted both in control and STa-treated cells. Staurosporine, a potent PKC inhibitor, significantly reduced the enzyme activity. Autoradiographic analysis of polyacrylamide gel electrophoresis revealed that pretreatment of the cells with STa also resulted in the phosphorylation of specific membrane proteins each with a molecular mass of 37 kDa, 100 kDa and 140 kDa. However, STa had no direct role on the enzyme activity. Our results, therefore, provide evidence for the involvement of PKC in STa-induced signal transduction in rat enterocytes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06318.x
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