Linked Life Data

3034196

Source:http://linkedlifedata.com/resource/pubmed/id/3034196

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1987-6-19
pubmed:abstractText
Ion-stripped bovine brain calmodulin (CaM) binds 4 moles Cd2+ as well as 4 moles Ca2+ per mole protein, with similar affinity; in the presence of 1 mM Mg2+ the molar binding ratio of CaM for Ca2+ decreased to 3, the apparent K0.5 for Ca2+ nearly doubled, but the binding characteristics of CaM for Cd2+ were not changed. Saturating concentrations Ca2+ did not affect the molar binding ratio of CaM for Cd2+, but increased the apparent K0.5 for Cd2+; vice versa, saturating concentrations Cd2+ decreased the molar binding ratio for Ca2+ to 2 without affecting the apparent K0.5 for Ca2+. CaM-independent phosphodiesterase (PDE) activity was inhibited at [Cd2+] greater than 10(-5) M. Cd2+-CaM as well as Ca2+-CaM activated PDE. However, the Cd2+-CaM complex is less effective than the Ca2+-CaM complex in stimulating CaM-dependent enzyme activities. Cd2+ inhibits Ca2+- and CaM-dependent PDE in a competitive way. Introduction of Cd2+ in a medium containing Ca2+ and CaM may, therefore, result in a reduction of CaM-dependent enzyme stimulation. By its interference with Ca2+- and CaM- dependent PDE activity, Cd2+ could upset the catabolic pathway of cellular cyclic nucleotide metabolism.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0340-5761
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
353-9
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Calmodulin-mediated cadmium inhibition of phosphodiesterase activity, in vitro.
pubmed:publicationType
Journal Article