The effect of cholera toxin on the phosphorylation of protein in epithelial cells and their brush borders

Lucid, Shannon W.; Cox, Albert

doi:10.1016/0006-291x(72)90593-1

Cited by 24 publications

(3 citation statements)

References 9 publications

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“…Lucid and Cox reported in 1972 that cholera toxin increased the phosphorylation of brush border membrane proteins [17]. The suggested target of this protein kinase activity was a process controlling CI-secretion across the intestinal mucosa in a serosal-to-mucosal direction [5].…”

Section: Introductionmentioning

confidence: 99%

Activation of chloride conductance in pig jejunal brush border vesicles

Forsyth

Gabriel

1989

J. Membrain Biol.

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Requirements for the activation of Cl- conductance have been investigated in pig jejunal brush border vesicles. The stability of ATP as a substrate for protein kinase activity, the stability of the phosphoprotein product of protein kinase action, and the choice of buffer system used for vesicle preparation were studied as variables which affected the outcome of in vitro activation attempts. Arsenate was selected as the most effective agent in protecting ATP from hydrolysis by the phosphatase activity in this vesicle system. Brush border vesicle protein appeared to prevent the accumulation of phosphoprotein in a cAMP-dependent protein kinase reaction, and vesicle protein only had phosphate acceptor activity when KF was added as a presumptive inhibitor of phosphoprotein phosphatase. A Cl- conductance response to a potassium gradient and valinomycin was present in vesicles prepared in buffers containing tetramethylammonium. Cl- conductance activity was not increased in this system by the addition of ATP, dibutyryl cyclic AMP, and cyclic AMP-dependent protein kinase. There was no Cl conductance response to a potassium gradient in vesicles buffered with imidazolium-acetate. Incorporation of ATP, AsO4(3-), and F- into these nonconductive vesicles by homogenization, followed by addition of dibutyryl cAMP, produced substantial conductance activity. Maximal activation of Cl- conductance was obtained with vesicles prepared in imidazolium-acetate buffering, using precautions to stabilize ATP and phosphoprotein prior to conductance measurements.

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Section: Introductionmentioning

confidence: 99%

Activation of chloride conductance in pig jejunal brush border vesicles

Forsyth

Gabriel

1989

J. Membrain Biol.

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“…Lucid and Cox have demonstrated that cholera toxin increases the amount of phosphate incorporated into the protein fraction of intestinal epithelial cells. 23 There is therefore the alternative possibility that intestinal alkaline phosphatase may play a part in the phosphorylation of protein in intestinal epithelial cells which results in the state of hypersecretion.…”

Section: Discussionmentioning

confidence: 99%

Changes in intestinal alkaline phosphatase activity in cholera toxin-treated rats.

Miura¹,

Asakura²,

Morishita³

et al. 1982

Gut

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SUMMARY It is conceivable that brush border enzyme activities of the intestinal mucosa will change when bacterial toxins are exposed to the intestinal microvillous membranes. The effect of cholera toxin on the activity of intestinal alkaline phosphatase in rats was therefore determined in the intestinal mucosa by the histochemical method as well as in intestinal lymph by using lymph fistulated-rats. Activity of intestinal alkaline phosphatase in the intestinal mucosa and lymphatics changed biphasically after the oral administration of cholera toxin to rats. For the first three hours after the administration of cholera toxin it was depressed; it then increased and at eight hours reached a maximum. These changes in the activity of intestinal alkaline phosphatase were prevented by the administration of chlorpromazine, a known inhibitor of adenylate cyclase activity.

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“…The resulting increased tissue cyclic adenosine 3',5'-monophosphate (cAMP) concentration (20) is believed to mediate the secretion of the Cland HCO3rich fluid (4,15), mucus, and the increased cell surface glycoprotein turnover (7). As with other cAMP-mediated events, this is presumed to involve the stimulation of specific cAMP-dependent protein kinases (17). The first step in the pathogenesis of experimental cholera is the binding of the enterotoxin to a membrane receptor, most probably the glycolipid GM, (3,10,11,26).…”

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confidence: 99%

Lanthanum inhibition of Vibrio cholerae and Escherichia coli enterotoxin-induced enterosorption and its effects on intestinal mucosa cyclic adenosine 3',5'-monophosphate and cyclic guanosine 3',5'-monophosphate levels

Leitch¹,

Amer²

1975

Infect Immun

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Several trivalent cations, including lanthanum (La3+), inhibited the secretion (enterosorption) induced by the enterotoxins of Vibrio cholerae and Escherichia coli in the rabbit ileum in vivo. High concentrations (>10 mM) of La3+ were required to inhibit cholera enterotoxin (CE)-induced enterosorption, probably because of the adsorption of the La3+ to mucus and its precipitation by HCO3-. Exposure to lower concentrations of La3+ often potentiated the CE-induced enterosorption. If luminal La3+ exposure followed CE exposure, some recovery of the enterosorptive response was observed. The longer the lag between the CE exposure and the La3+ exposure, the greater was the recovery of the enterosorptive response. Lanthanum inhibited HCO,secretion more than Clsecretion.

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The effect of cholera toxin on the phosphorylation of protein in epithelial cells and their brush borders

Cited by 24 publications

References 9 publications

Activation of chloride conductance in pig jejunal brush border vesicles

Activation of chloride conductance in pig jejunal brush border vesicles

Changes in intestinal alkaline phosphatase activity in cholera toxin-treated rats.

Lanthanum inhibition of Vibrio cholerae and Escherichia coli enterotoxin-induced enterosorption and its effects on intestinal mucosa cyclic adenosine 3',5'-monophosphate and cyclic guanosine 3',5'-monophosphate levels

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