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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1993-2-23
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pubmed:abstractText |
The effects of cholera toxin, a secretory product of Vibrio cholerae, result from ADP-ribosylation of the stimulatory guanine nucleotide-binding (Gs) protein of the adenylyl cyclase system. Cholera toxin A subunit (CTA) also uses agmatine, a simple guanidino compound, several proteins unrelated to Gs, and CTA itself as alternative ADP-ribose acceptors. The effects of toxin occur in the jejunum presumably at body core temperature. With agmatine as a model substrate, the optimal temperature for CTA-catalyzed ADP-ribosylation was 25-30 degrees C, and that for CTA-catalyzed auto-ADP-ribosylation was 20-25 degrees C. Both activities were significantly less at 37 degrees C, reflecting lower initial velocities, not heat-inactivation of the toxin. All the transferase activities of CTA are enhanced by ADP-ribosylation factors (ARFs), approximately 20-kDa guanine nucleotide-binding proteins that are ubiquitous in mammalian cells. Phospholipids and a soluble brain ARF, in a GTP-dependent manner, activated toxin NAD:agmatine ADP-ribosyltransferase activity; their simultaneous effect was maximal at physiological temperatures (approximately 37 degrees C). At lower temperatures, the stimulation by ARF was much less. There were similar effects on other toxin-catalyzed reactions, notably, the ADP-ribosylation of Gs alpha and the hydrolysis of NAD. Thus, host factors, such as ARF and phospholipid, synergistically increase cholera toxin activity at 37 degrees C and may be important in toxin action in the mammalian gut.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Agmatine,
http://linkedlifedata.com/resource/pubmed/chemical/Cardiolipins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/Detergents,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
561-6
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pubmed:dateRevised |
2005-11-17
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pubmed:meshHeading |
pubmed-meshheading:8422366-ADP-Ribosylation Factors,
pubmed-meshheading:8422366-Agmatine,
pubmed-meshheading:8422366-Allosteric Regulation,
pubmed-meshheading:8422366-Animals,
pubmed-meshheading:8422366-Cardiolipins,
pubmed-meshheading:8422366-Cattle,
pubmed-meshheading:8422366-Cholera Toxin,
pubmed-meshheading:8422366-Detergents,
pubmed-meshheading:8422366-GTP-Binding Proteins,
pubmed-meshheading:8422366-Guanine Nucleotides,
pubmed-meshheading:8422366-Phospholipids,
pubmed-meshheading:8422366-Rabbits,
pubmed-meshheading:8422366-Substrate Specificity,
pubmed-meshheading:8422366-Temperature
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pubmed:year |
1993
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pubmed:articleTitle |
Effects of temperature on ADP-ribosylation factor stimulation of cholera toxin activity.
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pubmed:affiliation |
Laboratory of Cellular Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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