Linked Life Data

3345197

Source:http://linkedlifedata.com/resource/pubmed/id/3345197

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1988-4-7
pubmed:abstractText
The existence of a postulated hepatic receptor responsible for the peroxisomal proliferation induced in rodents by hypolipidaemic drugs has been investigated. [3H]-nafenopin and [3H]-ciprofibrate were used as labelled ligands and two competitive binding assays, using either a charcoal-dextran or a hydroxylapatite method, were developed to investigate potential binding. In both assay systems, specific displaceable binding of either nafenopin or ciprofibrate to whole homogenate, microsomal and cytosolic fractions of rat liver could not be detected in a variety of buffer systems. A positive control of ligand binding to bovine serum albumin indicated the validity of the binding assays used. In addition, both nafenopin and ciprofibrate exhibited displaceable binding to serum albumin using the hydroxylapatite binding assay and a Scatchard analysis of the binding of [3H]-nafenopin to fatty acid free rat serum albumin yielded a dissociation constant of 5.2 x 10(-7) M and 86 pmol of ligand bound per mg protein. Taken collectively, our data strongly argues against the existence of a specific hepatic peroxisome proliferation receptor and indicates that the peroxisome proliferating hypolipidaemic drugs bind to serum albumin and possibly to other cellular proteins not involved in the activation of genes necessary for peroxisome proliferation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
793-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Lack of evidence for a hepatic peroxisome proliferator receptor and an explanation for the binding of hypolipidaemic drugs to liver homogenates.
pubmed:affiliation
University of Surrey, Department of Biochemistry, Guildford, U.K.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't