Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-11-4
pubmed:abstractText
The NO/superoxide (O2-) balance is a key regulator of endothelial function. O2- levels are elevated in many forms of cardiovascular disease; therefore, decreasing O2- should improve endothelial function. To explore this hypothesis, internal mammary arteries and saphenous veins, obtained from patients undergoing coronary artery revascularization, and aortic and carotid arteries from Wistar-Kyoto and spontaneously hypertensive stroke-prone rats were incubated with O2- dismutase or NAD(P)H oxidase inhibitors. O2- levels were measured using lucigenin chemiluminescence; NO bioavailability was assessed in organ chambers; and mRNA expression of NAD(P)H oxidase components was quantified by use of a Light Cycler. In rat arteries, phenylarsine oxide, 4-(2-aminoethyl)-benzenesulfanyl fluoride, and apocynin all decreased NADH-stimulated O2- production, but only apocynin increased NO bioavailability. In human internal mammary arteries and saphenous veins, apocynin decreased NAD(P)H-stimulated O2- generation and caused vasorelaxation that was endothelium dependent and reversed on addition of the NO synthase inhibitor N(G)-nitro-L-arginine methyl ester. In addition, it increased NO production from cultured human endothelial saphenous vein cells. Polyethylene-glycolated O2- dismutase also increased NO bioavailability in rat carotid arteries and human blood vessels, but the effects were smaller than those observed with apocynin. NADH-generated O2- and mRNA expression of p22(phox), gp91(phox), and nox-1 were comparable between the 2 strains of rat. This is the first study to demonstrate pharmacological effects of apocynin in human blood vessels. The increases in NO bioavailability shown here suggest that the NAD(P)H oxidase pathway may be a novel target for drug intervention in cardiovascular disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetophenones, http://linkedlifedata.com/resource/pubmed/chemical/CYBA protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Dehydrogenase, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Superoxides, http://linkedlifedata.com/resource/pubmed/chemical/acetovanillone
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1524-4563
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
755-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12411473-Acetophenones, pubmed-meshheading:12411473-Animals, pubmed-meshheading:12411473-Blood Vessels, pubmed-meshheading:12411473-Endothelium, Vascular, pubmed-meshheading:12411473-Enzyme Inhibitors, pubmed-meshheading:12411473-Humans, pubmed-meshheading:12411473-Mammary Arteries, pubmed-meshheading:12411473-Membrane Transport Proteins, pubmed-meshheading:12411473-NADH, NADPH Oxidoreductases, pubmed-meshheading:12411473-NADPH Dehydrogenase, pubmed-meshheading:12411473-NADPH Oxidase, pubmed-meshheading:12411473-Nitric Oxide, pubmed-meshheading:12411473-Phosphoproteins, pubmed-meshheading:12411473-RNA, Messenger, pubmed-meshheading:12411473-Rats, pubmed-meshheading:12411473-Rats, Inbred SHR, pubmed-meshheading:12411473-Rats, Inbred WKY, pubmed-meshheading:12411473-Saphenous Vein, pubmed-meshheading:12411473-Superoxides
pubmed:year
2002
pubmed:articleTitle
NAD(P)H oxidase inhibition improves endothelial function in rat and human blood vessels.
pubmed:affiliation
BHF Blood Pressure Group, Department of Medicine and Therapeutics, Western Infirmary, Glasgow, Scotland. c.a.hamilton@clinmed.gla.ac.uk
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't