Abstract
Cholera, a devastating diarrheal disease characterized by abnormalities in fluid and electrolyte flux, results in part from the action of cholera toxin (choleragen), a secretory product of Vibrio cholerae, on the intestinal mucosa (Carpenter, 1980; Kelly, 1986). Cholera toxin exerts its effects by catalyzing the ADP-ribosylation of Gsα, the α subunit of the heterotrimeric stimulatory guanine nucleotide-regulatory protein that activates the adenylyl cyclase catalytic unit and is involved in the modulation of ion channels (Birnbaumer et al., 1987; Casey and Gilman, 1988; Moss and Vaughan, 1988). Activation of adenylyl cyclase, as well as other toxincatalyzed reactions, is enhanced by membrane and soluble factors that have been identified in preparations from numerous animal cells and tissues (Gill, 1976; Enomoto and Gill, 1980; Nakaya et al., 1980; Le Vine, III and Cuatrecasas, 1981; Pinkett and Anderson, 1982; Schleifer et al., 1982; Gill and Meren, 1983; Kahn and Gilman, 1984; Kahn and Gilman, 1986; Tsai et al., 1987, 1988; Gill and Coburn, 1987). A 21 kDa protein that stimulated the toxin-catalyzed ADP-ribosylation of Gsα was purified from liver membranes and termed ADP-ribosylation factor or ARF (Kahn and Gilman, 1984).
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© 1990 Plenum Press, New York
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Vaughan, M., Moss, J. (1990). G Proteins and Toxin-Catalyzed ADP-Ribosylation. In: Vanderhoek, J.Y. (eds) Biology of Cellular Transducing Signals. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-0559-0_20
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DOI: https://doi.org/10.1007/978-1-4613-0559-0_20
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