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Research Article Free access | 10.1172/JCI107039

Localization of the action of cholera toxin on adenyl cyclase in mucosal epithelial cells of rabbit intestine

David K. Parkinson, Hans Ebel, Donald R. DiBona, and Geoffrey W. G. Sharp

Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02115

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Find articles by Parkinson, D. in: PubMed | Google Scholar

Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02115

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Find articles by Ebel, H. in: PubMed | Google Scholar

Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02115

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Find articles by DiBona, D. in: PubMed | Google Scholar

Department of Medicine, Massachusetts General Hospital, Boston, Massachusetts 02115

Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115

Find articles by Sharp, G. in: PubMed | Google Scholar

Published September 1, 1972 - More info

Published in Volume 51, Issue 9 on September 1, 1972
J Clin Invest. 1972;51(9):2292–2298. https://doi.org/10.1172/JCI107039.
© 1972 The American Society for Clinical Investigation
Published September 1, 1972 - Version history
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Abstract

Brush borders and plasma membranes have been purified from mucosal epithelial cells of rabbit ileum under control conditions and after treatment for 3 hr with cholera toxin in vivo. The activity of several enzymes in these preparations was measured. It was concluded that adenyl cyclase, like NaK-ATPase, seems not to be a normal constituent of brush borders. Both these enzymes are present in plasma membrane preparations derived largely from the basal and lateral margins of the epithelial cells, both may be phospholipid dependent enzymes and both are affected by cholera toxin. Adenyl cyclase activity is increased while NaK-ATPase is decreased. The activities of alkaline phosphatase, leucineaminopeptidase, 5′-nucleotidase, glucose-6-phosphatase, and Mg-ATPase were not found to be affected by the toxin. Cholera toxin, which makes contact with the luminal side of the epithelial cells, in the natural disease and in the experimental model, would appear to exert its pathologic effect on adenyl cyclase at the opposite (basal and lateral) side of the cells.

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