Linked Life Data

6260798

Source:http://linkedlifedata.com/resource/pubmed/id/6260798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1981-6-25
pubmed:abstractText
Calmodulin is a ubiquitous, multifunctional, Ca2+-dependent regulatory protein, controlling a wide variety of Ca2+-mediated reactions. The versatility of calmodulin raises the question of how it exerts specificity at the molecular level. Cyclic nucleotide phosphodiesterase consists of multiple forms, one of which requires calmodulin for full activity. Calcineurin, a calmodulin-binding protein, inhibits the calmodulin-stimulated phosphodiesterase activity by competing with the enzyme for calmodulin. In this report, we present experiments which indicate that, although calcineurin potentially inhibits calmodulin-supported enzyme activity, its effectiveness as an inhibitor depends on the level of cAMP. In the presence of elevated levels of cAMP, the affinity of calmodulin for phosphodiesterase increased markedly, but that for calcineurin was not altered. Thus, the enzyme became relatively refractory to inhibition by calcineurin. This finding suggests that an increase of cellular cAMP could lead to a condition favorable to its own hydrolysis and that this phenomenon might represent an example of molecular specificity in calmodulin-regulated reactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4439-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
cAMP renders Ca2+-dependent phosphodiesterase refractory to inhibition by a calmodulin-binding protein (calcineurin).
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't