Linked Life Data

7546215

Source:http://linkedlifedata.com/resource/pubmed/id/7546215

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-10-27
pubmed:abstractText
Vanadium, believed to be an essential trace metal, exhibits numerous biological effects. Using electron spin resonance spectroscopy, we have demonstrated that vanadyl, vanadium (IV), the predominant intracellular form of vanadate (vanadium V), binds to calmodulin in the presence of physiological concentrations of magnesium, extending earlier work which showed competitive binding of vanadyl and calcium to calmodulin. In the presence of a magnesium-containing buffer, vanadyl does not lead to calmodulin activation of the calmodulin-dependent enzyme, rabbit skeletal muscle myosin light chain kinase; in the presence of calcium, vanadyl is a potent inhibitor of the calmodulin-activated form of the kinase. Thus, vanadyl can potentially interfere with some of the intracellular actions of calcium, presumably via binding to calmodulin. This observation deserves consideration in view of the potential clinical application of vanadium treatment to mimick insulin action and lower blood glucose.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0951-6433
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Vanadium (IV) inhibits calmodulin-stimulated skeletal muscle myosin light chain kinase activity.
pubmed:affiliation
Department of Chemistry, University of Miami, Coral Gables, Florida 33124, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't