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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1992-11-20
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pubmed:abstractText |
Studies in Aplysia and Drosophila have suggested that Ca2+/calmodulin-sensitive adenylyl cyclase may act as a site of convergence for the cellular representations of the conditioned stimulus (Ca2+ influx) and unconditioned stimulus (facilitatory transmitter) during elementary associative learning. This hypothesis predicts that the rise in intracellular free Ca2+ concentration produced by spike activity during the conditioned stimulus will cause an increase in the activity of adenylyl cyclase. However, published values for the Ca2+ sensitivity of Ca2+/calmodulin-sensitive adenylyl cyclase in mammals and in Drosophila vary widely. The difficulty in evaluating whether adenylyl cyclase would be activated by physiological elevations in intracellular Ca2+ levels is in part a consequence of the use of Ca2+/EGTA buffers, which are prone to several types of errors. Using a procedure that minimizes these errors, we have quantified the Ca2+ sensitivity of adenylyl cyclase in membranes from Aplysia, Drosophila, and rat brain with purified species-specific calmodulins. In all three species, adenylyl cyclase was activated by an increase in free Ca2+ concentration in the range caused by spike activity. Ca2+ sensitivity was dependent on both calmodulin concentration and Mg2+ concentration. Mg2+ raised the threshold for adenylyl cyclase activation by Ca2+ but also acted synergistically with Ca2+ to activate maximally adenylyl cyclase.
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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/Adenylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
59
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1736-44
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1402918-Adenylate Cyclase,
pubmed-meshheading:1402918-Animals,
pubmed-meshheading:1402918-Aplysia,
pubmed-meshheading:1402918-Calcium,
pubmed-meshheading:1402918-Calmodulin,
pubmed-meshheading:1402918-Cerebral Cortex,
pubmed-meshheading:1402918-Drosophila,
pubmed-meshheading:1402918-Drug Synergism,
pubmed-meshheading:1402918-Enzyme Activation,
pubmed-meshheading:1402918-Kinetics,
pubmed-meshheading:1402918-Magnesium,
pubmed-meshheading:1402918-Male,
pubmed-meshheading:1402918-Nerve Tissue Proteins,
pubmed-meshheading:1402918-Rats,
pubmed-meshheading:1402918-Rats, Sprague-Dawley
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pubmed:year |
1992
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pubmed:articleTitle |
A quantitative study of the Ca2+/calmodulin sensitivity of adenylyl cyclase in Aplysia, Drosophila, and rat.
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pubmed:affiliation |
Howard Hughes Medical Institute, Columbia University College of Physicians and Surgeons, New York.
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pubmed:publicationType |
Journal Article,
Comparative Study
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