Cholera

Finkelstein, Richard A.; Feeley, John C.

doi:10.3109/10408417309108394

Cited by 425 publications

(190 citation statements)

References 298 publications

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“…A variety of mammalian cells and membranes derived therefrom exhibit increased adenylate cyclase activity subsequent to treatment with cholera toxin and NAD' [40,41]. It was suggested [42] and subsequently shown [43] that cholera toxin inhibits the GTPase step, thus increasing the steady state concentration of the activated form of adenylate cyclase in the presence of hormone and GTP ( fig.…”

Section: The Action Of Cholera Toxinmentioning

confidence: 99%

Hormone‐receptor‐adenylate cyclase interactions

Levitzki¹,

Helmreich²

1979

FEBS Letters

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Section: The Action Of Cholera Toxinmentioning

confidence: 99%

Hormone‐receptor‐adenylate cyclase interactions

Levitzki¹,

Helmreich²

1979

FEBS Letters

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“…100,000) (2,7) which acts at the plasma membrane to exert its biological effect (3)(4)(5)(6)(7). The diverse actions of the toxin (2,(8)(9)(10)(11)(12)(13) can be attributed to its ability to stimulate specifically the membrane-localized enzyme, adenylate cyclase (EC 4.6.1.1), thereby raising intracellular levels of cAMP. It is presumably by this mechanism that choleragen acts as a potent inhibitor of mitogen-induced DNA synthesis in human fibroblasts (14).…”

mentioning

confidence: 99%

“…TAL/N (P < 60) Effects of Cholera Toxin on Adenylate Cyclase. It is very likely that all of the biological effects of choleragen are mediated by its action on adenylate cyclase (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13). Direct measurements of membrane adenylate cyclase were performed 4.5 hr after exposure of cell monolayers to increasing amounts of choleragen (Fig.…”

mentioning

confidence: 99%

Cholera Toxin and Cell Growth: Role of Membrane Gangliosides

Hollenberg

Fishman

Bennett

et al. 1974

Proc. Natl. Acad. Sci. U.S.A.

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The bindikg of cholera toxin to three transformed mouse cell lines derived from the same parent strain, and the effects of the toxin on DNA synthesis and adenylate cyclase activity, vary in parallel with the ganglioside composition of the cells. TAL/N cells of early passage, which contain large quantities of gangliosides Gm3, GM2, G11, and GDWa, as well as the glycosyltransferases necessary for the synthesis of these gangliosides, bind the most cholera toxin and are the most sensitive to its action.TAL/N cells of later passage, which lack chemically detectable GM, and GD1a and which have no UDP-Gal:GM2 Cholera toxin (choleragen), the principal exoenterotoxin of Vibrio cholerae, is an oligomeric protein (molecular weight, approx. 100,000) (2, 7) which acts at the plasma membrane to exert its biological effect (3-7). The diverse actions of the toxin (2, 8-13) can be attributed to its ability to stimulate specifically the membrane-localized enzyme, adenylate cyclase (EC 4.6.1.1), thereby raising intracellular levels of cAMP. It is presumably by this mechanism that choleragen acts as a potent inhibitor of mitogen-induced DNA synthesis in human fibroblasts (14). Also, stimulation of adenylate cyclase probably explains the toxin's ability to inhibit mitogenic transformation of lymphocytes (15), to stimulate steroidogenesis in adrenal cells (16,17), and to induce differentiation in melanoma cells (18). In all cells so far studied, choleragen is nontoxic by several criteria (14-17) and the action of choleragen is observed to persist for at least two weeks in culture (18).It has been observed that gangliosides can interact specifically with choleragen so as to block the binding of the toxin to cell membranes (3)(4)(5)(6)(7)(19)(20)(21)(22)(23). In particular, GM1 is a highly potent inhibitor of choleragen binding; GD1a and GM2 are at least 50-fold, and GM3 at least 250-fold less effective than

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“…Choleragen is believed to exert its effects on mammalian cells through activation of adenylate cyclase (1). The initial step in the activation process is presumed to be the binding of the B protomer of choleragen to cell surface receptors, presumably the monosialoganglioside GM1 (2-7).…”

mentioning

confidence: 99%

Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its A protomer: possible role in the activation of adenylate cyclase.

Moss¹,

Manganiello²,

Vaughan³

1976

Proc. Natl. Acad. Sci. U.S.A.

206

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Choleragen and the isolated A protomer catalyzed the hydrolysis of NAD to ADP-ribose and nicotinamide.The protein with NADase activity (NAD nucleosidase; NAD glycohydrolase, EC 3.2.2.5) migrated on polyacrylamide gels with choleragen, and chromatographed on Bio-Gel P-60 columns with the A protomer. The NADase activity of choleragen and of the A protomer was increased markedly in acetate and phosphate buffers, and enhanced over 10-fold by dithiothreitol in high concentration. NAD hydrolysis was proportional to choleragen concentration; the Michaelis constant for NAD was about 4 mM with both choleragen and the A protomer. The demonstration that the A protomer of choleragen catalyzes an enzymatic reaction involving activation of the ribosyl-nicotinamide bond of NAD, a reaction analogous to those catalyzed by diphtheria toxin, supports the hypothesis that activation of adenylate cyclase by choleragen involves the ADP-ribosylation of an appropriate acceptor protein.

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Cholera

Cited by 425 publications

References 298 publications

Hormone‐receptor‐adenylate cyclase interactions

Hormone‐receptor‐adenylate cyclase interactions

Cholera Toxin and Cell Growth: Role of Membrane Gangliosides

Hydrolysis of nicotinamide adenine dinucleotide by choleragen and its A protomer: possible role in the activation of adenylate cyclase.

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