rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
11
|
pubmed:dateCreated |
2003-3-25
|
pubmed:abstractText |
Low-density lipoprotein (LDL) impairs endothelial cell function by uncoupling endothelial nitric oxide synthase (eNOS) activity, which allows superoxide anion (O2*-)) to be generated rather than nitric oxide (*NO). Recent reports indicate that apolipoprotein (apo) A-1 mimetics inhibit the development of atherosclerotic lesions in LDL receptor-null mice. Here we hypothesize that L-4F, an apoA-1 mimetic that inhibits atherosclerosis induced by hypercholesterolemia, protects endothelial cell function by preventing LDL from uncoupling eNOS activity.
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pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
AIM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
1524-4539
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:day |
25
|
pubmed:volume |
107
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1520-4
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:12654610-Animals,
pubmed-meshheading:12654610-Apolipoprotein A-I,
pubmed-meshheading:12654610-Cattle,
pubmed-meshheading:12654610-Cells, Cultured,
pubmed-meshheading:12654610-Endothelium, Vascular,
pubmed-meshheading:12654610-HSP90 Heat-Shock Proteins,
pubmed-meshheading:12654610-Lipoproteins, LDL,
pubmed-meshheading:12654610-Nitric Oxide,
pubmed-meshheading:12654610-Nitric Oxide Synthase,
pubmed-meshheading:12654610-Nitric Oxide Synthase Type III,
pubmed-meshheading:12654610-Peptides,
pubmed-meshheading:12654610-Superoxides
|
pubmed:year |
2003
|
pubmed:articleTitle |
L-4F, an apolipoprotein A-1 mimetic, restores nitric oxide and superoxide anion balance in low-density lipoprotein-treated endothelial cells.
|
pubmed:affiliation |
Department of Surgery, Medical College of Wisconsin, Children's Hospital of Wisconsin, Milwaukee 53226, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|