Cholera toxin: Difference between revisions

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&nbsp;Cholera Toxin is an enzyme secreted by the cholera causing bacterium ''Vibrio cholerae.'' It ribosylates the alpha subunit of a G-protein associated with an intestinal epithelial cell, preventing the hydrolysis of GTP bound to the same G-protein. This locks the G-protein in an active state, leading to the indefinite stimulation of adenylyl cyclase, causing a rise in cAMP concentration. This then causes water and Cl<sup>- </sup>to leave the cell and enter the intestinal lumen, leading to the severe diarrhoea and dehydration associated with cholera<ref>Molecular Biology of the Cell (5th edition), Alberts et al., pg 906.</ref>.<sup>&nbsp;</sup>
Cholera Toxin is an enzyme secreted by the cholera causing bacterium ''Vibrio cholerae.'' It ribosylates the alpha subunit of a G-protein associated with an intestinal epithelial cell, preventing the hydrolysis of GTP bound to the same G-protein. This locks the G-protein in an active state, leading to the indefinite stimulation of adenylyl cyclase, causing a rise in cAMP concentration. This then causes water and Cl<sup>- </sup>to leave the cell and enter the intestinal lumen, leading to the severe diarrhoea and dehydration associated with cholera<ref>Molecular Biology of the Cell (5th edition), Alberts et al., pg 906.</ref>.<sup>&nbsp;</sup>  


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== References ==
== References ==


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Revision as of 16:44, 11 December 2012

Cholera Toxin is an enzyme secreted by the cholera causing bacterium Vibrio cholerae. It ribosylates the alpha subunit of a G-protein associated with an intestinal epithelial cell, preventing the hydrolysis of GTP bound to the same G-protein. This locks the G-protein in an active state, leading to the indefinite stimulation of adenylyl cyclase, causing a rise in cAMP concentration. This then causes water and Cl- to leave the cell and enter the intestinal lumen, leading to the severe diarrhoea and dehydration associated with cholera[1]. 


References

  1. Molecular Biology of the Cell (5th edition), Alberts et al., pg 906.