Animation showing the effect of the cholera toxin, which is secreted by the bacterium Vibrio cholerae. Shown first is the normal activation of adenylate cyclase. A molecule (green sphere) binds to its receptor (pink, left), forming a hormone-receptor complex. This complex binds to a G protein and induces the release of GDP (guanosine diphosphate) from the protein. This allows GTP (guanosine triphosphate) to bind to the G protein instead, causing the alpha subunit (purple) of the G protein to disassociate from the beta/gamma subunit (yellow). The alpha subunit-GTP complex then activates adenylate cyclase (pink, centre right). Adenylate cyclase is an enzyme that catalyses the formation of cAMP (cyclic adenosine monophosphate), a secondary messenger. In the presence of cholera toxin (blue and orange) adenylate cyclase is irreversibly activated and so creates an abnormally high amount of cAMP. This causes cells to excrete large numbers of chlorine ions into the intestinal lumen (top). This creates osmotic and electrical gradients that lead to the excretion of water and sodium ions, causing dehydration and diarrhoea. | |
Licence : | Droits gérés |
Crédit : | Science Photo Library / Biocosmos / Francis Leroy & Nathan Petit |
Model Release : | Non requis |
Durée : | 30 Secondes |
Aspect ratio : | 16/9 |
Restrictions : | - |