Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-7-12
pubmed:abstractText
Oxidized analogs of cholesterol (oxysterols) are produced through both enzymatic and non-enzymatic pathways and have been shown to perturb membrane properties in vitro and in vivo. In the present study, the membrane behavior of two naturally occurring oxysterols, 25-hydroxycholesterol and 7-ketocholesterol, was examined in two model systems. The presence of an additional oxygen moiety was found to alter membrane properties compared to native cholesterol and to each other in lipid monolayers, composed of either pure sterol or sterol-glycerophospholipid and sterol-sphingomyelin binary films, as well as in mixed multilamellar vesicles. The ability of oxysterols to condense phosphatidylcholine and sphingomyelin films, their capacity to cause changes in in-plane elasticity moduli, and their propensity to form detergent-resistant membrane domains were all found to be dependant on the location of the oxygen functionality in the oxysterol, the chemical nature of the phospholipid in the model systems, and the oxysterol/phospholipid ratio in the membrane. The findings described in this study with respect to their biophysical/biophysiological implications provide additional insight into the activity of cytotoxic oxysterols in model membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1873-2941
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Elsevier Ireland Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
163
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
586-93
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Interaction of two oxysterols, 7-ketocholesterol and 25-hydroxycholesterol, with phosphatidylcholine and sphingomyelin in model membranes.
pubmed:affiliation
Department of Chemistry and Biochemistry, Stern College for Women, Yeshiva University, 245 Lexington Avenue, New York, NY 10016, United States. mintzer@yu.edu
pubmed:publicationType
Journal Article