Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2004-4-16
pubmed:abstractText
Heme oxygenase-1 (HO-1) catalyzes the conversion of heme to bilirubin, carbon monoxide (CO), and free iron, thus controlling the level of cellular heme. The medullary thick ascending limb of the loop of Henle (TALH) is situated in a site of markedly diminished oxygen tension and, as such, is highly vulnerable to ischemic insult. We hypothesize that selective upregulation of HO-1 in TALH by gene transfer attenuates oxidative stress caused by angiotensin II (Ang II).
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II, http://linkedlifedata.com/resource/pubmed/chemical/Cyclooxygenase 2, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone, http://linkedlifedata.com/resource/pubmed/chemical/Glutathione, http://linkedlifedata.com/resource/pubmed/chemical/HMOX1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Heme, http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase (Decyclizing), http://linkedlifedata.com/resource/pubmed/chemical/Heme Oxygenase-1, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PTGS2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Prostaglandin-Endoperoxide Synthases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Potassium-Chloride Symporters, http://linkedlifedata.com/resource/pubmed/chemical/heme oxygenase-2, http://linkedlifedata.com/resource/pubmed/chemical/sodium-potassium chloride...
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0085-2538
pubmed:author
pubmed:issnType
Print
pubmed:volume
65
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1628-39
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15086901-Angiotensin II, pubmed-meshheading:15086901-Animals, pubmed-meshheading:15086901-Base Sequence, pubmed-meshheading:15086901-Cells, Cultured, pubmed-meshheading:15086901-Cyclooxygenase 2, pubmed-meshheading:15086901-DNA, Complementary, pubmed-meshheading:15086901-DNA Damage, pubmed-meshheading:15086901-Dinoprostone, pubmed-meshheading:15086901-Gene Expression, pubmed-meshheading:15086901-Glutathione, pubmed-meshheading:15086901-Heme, pubmed-meshheading:15086901-Heme Oxygenase (Decyclizing), pubmed-meshheading:15086901-Heme Oxygenase-1, pubmed-meshheading:15086901-Humans, pubmed-meshheading:15086901-Isoenzymes, pubmed-meshheading:15086901-Loop of Henle, pubmed-meshheading:15086901-Membrane Proteins, pubmed-meshheading:15086901-Oxidative Stress, pubmed-meshheading:15086901-Promoter Regions, Genetic, pubmed-meshheading:15086901-Prostaglandin-Endoperoxide Synthases, pubmed-meshheading:15086901-Rats, pubmed-meshheading:15086901-Recombinant Proteins, pubmed-meshheading:15086901-Sodium-Potassium-Chloride Symporters, pubmed-meshheading:15086901-Transduction, Genetic
pubmed:year
2004
pubmed:articleTitle
Expression of human heme oxygenase-1 in the thick ascending limb attenuates angiotensin II-mediated increase in oxidative injury.
pubmed:affiliation
Department of Pharmacology, Division of Nephrology, New York Medical College, Valhalla, New York 10595, USA. nader_abraham@nymc.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't