Linked Life Data

16664047

Source:http://linkedlifedata.com/resource/pubmed/id/16664047

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-6-29
pubmed:abstractText
Calmodulin has been isolated from the root of Zea mays. It activates the bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase and has electrophoretic mobility very similar to that of bovine brain calmodulin. Ophiobolin A, a fungal toxin, interacts with the maize calmodulin. The interaction is not reversed by dilution or denaturation in SDS and results in the loss of ability of the calmodulin to activate the phosphodiesterase. The inhibition is much faster in the presence than in the absence of Ca(2+). The electrophoretic mobility of ophiobolin A-treated calmodulin is less than that of untreated calmodulin. Several similarities are found between the inhibition of maize calmodulin by ophiobolin A in vitro and the effects of ophiobolin A on excised roots. Both are irreversible and time-dependent. The concentration of ophiobolin A for half-maximal inhibition of calmodulin in the phosphodiesterase assay is similar to that for phytotoxicity. In both cases ophiobolin A derivatives behave similarly, i.e. 18-bromo-19-methoxyophiobolin A is as potent as ophiobolin A, while 3-anhydro-ophiobolin A and 6-epi-ophiobolin A are less potent. A smaller amount of active calmodulin was measured in the extract from ophiobolin A-treated roots than in those from untreated roots. The present study suggests that calmodulin is a target molecule in the root for the toxicity of ophiobolin A.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:status
PubMed-not-MEDLINE
pubmed:month
Feb
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
77
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
303-8
pubmed:dateRevised
2010-9-14
pubmed:year
1985
pubmed:articleTitle
Role of calmodulin inhibition in the mode of action of ophiobolin a.
pubmed:affiliation
Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa 50011.
pubmed:publicationType
Journal Article