Results 151 to 160 of about 175,144 (193)
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Requirement for guanosine triphosphate in the activation of adenylate cyclase by cholera toxin
Journal of Supramolecular Structure, 1979AbstractThe activation of adenylate cyclase in lysed pigeon erythrocytes requires, among several cofactors, a nucleotide which may be ATP, GTP, or many other triphosphates. However, after removal of endogenous nucleotides by gel filtration or by adsorption onto charcoal the requirement can be met only by GTP, or an analog of GTP.
Keiichi Enomoto +2 more
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The response of adenylate cyclase to GTP and to dopamine (DA) was investigated in synaptic plasma membranes isolated from rat striatum injected with pertussis toxin, which inactivates the inhibitory guanine nucleotide-binding regulatory protein (Ni) of ...
Maria C Olianas, Pierluigi Onali
exaly +2 more sources
Bordetella Adenylate Cyclase Toxin
Journal of Toxicology: Toxin Reviews, 1987AbstractA major virulence factor of the genus Bordetella is a unique toxin, a secreted adenylate cyclase, which penetrates membranes of mammalian cells resulting in unregulated generation of adenosine 3′:5′-monophosphate (CAMP). In human infections caused by Bordetella pertussis, this toxin, Bordetella Adenylate Cyclase Toxin (BACT), and a second ...
Erica M. Tenbroek, Dennis L. Confer
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Stimulation of Intestinal Adenyl Cyclase by Cholera Toxin
Nature, 1971THE molecular mechanism by which cholera toxin produces a massive loss of water and electrolytes is unknown, but it is clear that an increase in net secretion of approximately isotonic fluid occurs throughout the length of the small intestine1,2. The relative contributions of increased active ion secretion and decreased active ion reabsorption to this ...
G W, Sharp, S, Hynie
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Cholera Toxin and the Adenylate Cyclase-Activating Signal
Journal of Infectious Diseases, 1976Studies with chemically modified cholera toxin derivatives showed that all treatments that decreased the ability of toxin to bind to mouse thymus cells or to polystyrene-coupled GM1 ganglioside caused a concomitant reduction in the toxin's ability to increase adenosine 3':5'-cyclic phosphate (cyclic AMP) in thymus cells and skin vascular permeability ...
J, Holmgren, I, Lönnroth
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Influence of cholera toxin on the regulation of adenylate cyclase by GTP
Biochemical and Biophysical Research Communications, 1977Abstract In the presence of NAD+, cholera toxin activates adenylate cyclase in membranes of S49 mouse lymphoma cells. The following evidence supports the hypothesis that the toxin acts by inhibiting a specific GTPase associated with a guanyl nucleotide regulatory component of hormone-responsive cyclase: 1.
G L, Johnson, H R, Bourne
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Invasive adenylate cyclase toxin of Bordetella pertussis
Trends in Biochemical Sciences, 1989Bordetella pertussis produces an adenylate cyclase which is a toxin. The enzyme penetrates eukaryotic cells and, upon activation by host calmodulin, generates high levels of intracellular cAMP; as a result bactericidal functions of immune effector cells are considerably impaired.
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The activation of rabbit intestinal adenylate cyclase by cholera toxin
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1989Brush-border and basal-lateral membranes were prepared from rabbit intestinal epithelial cells by differential centrifugation and MgCl2 precipitation. The ADP-ribosylation of proteins in these fractions when incubated with [adenylate-32P]NAD+ and cholera toxin was investigated. Three proteins of molecular mass 45, 40 and 37 kDa were labelled in a toxin-
D, Longbottom, S, van Heyningen
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Adenylate cyclase toxin (Bordetella sp.)
1997Abstract Adenylate cyclase toxin (ACT or CyaA) is a key virulence factor produced by the human whooping cough agents, 8ordetella pertussis and parapertussis and by the related animal pathogens 8. bronchiseptica and 8. avium (Weiss and Hewlett 1986; Hanski and Coote 1991; Mock and Ullmann 1993).
P Sebo, A Ullmann
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Bordetella pertussis Adenylate Cyclase: A Toxin with Multiple Talents
Zentralblatt für Bakteriologie, 1993The adenylate cyclase toxin of Bordetella pertussis is a secreted multifunctional protein, endowed with calmodulin-activated catalytic, haemolytic and cytotoxic activities. Residues and domains involved in different functions have been localized and several permissive sites, able to accommodate insertion of peptides without impairing the different ...
S, Goyard +4 more
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