Source:http://linkedlifedata.com/resource/pubmed/id/15297254
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2004-11-19
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pubmed:abstractText |
The role of S-nitrosated hemoglobin (SNO-Hb) in the regulation of blood flow is a central and controversial question in cardiopulmonary physiology. In the present study, we investigate whether intact human red blood cells (RBCs) synthesized to contain high SNO-Hb levels are able to export nitric oxide bioactivity and vasodilate the pulmonary circulation, and whether SNO-Hb dependent vasodilation occurs secondary to an intrinsic oxygen-linked, allosteric function of Hb. RBCs containing supraphysiological concentrations (100-1,000x normal) of SNO-Hb (SNO-RBCs) were synthesized and added to isolated, perfused rat lungs during anoxic or normoxic ventilation, and during normoxic ventilation with pulmonary hypertension induced by the thromboxane mimetic U-46619. SNO-RBCs produced dose-dependent pulmonary vasodilation compared with control RBCs during conditions of both normoxic (U-46619) and hypoxic pulmonary vasoconstriction. These effects were associated with a simultaneous, rapid, and temperature-dependent loss of SNO from Hb. Both vasodilatory effects and the rate of SNO-Hb degradation were independent of oxygen tension and Hb oxygen saturation. Furthermore, these effects were not affected by inhibition of the RBC membrane band 3 protein (anion exchanger-1), a putative membrane facilitator of NO export from RBCs. Whereas these data support observations by multiple groups that synthesized SNO-Hb can vasodilate, this effect is not under intrinsic oxygen-dependent allosteric control, nor likely to be relevant in the pulmonary circulation at normal physiological concentrations.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/15-Hydroxy-11 alpha,9...,
http://linkedlifedata.com/resource/pubmed/chemical/Anion Exchange Protein 1...,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Nitric Oxide,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Vasoconstrictor Agents
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0363-6135
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
287
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
H2561-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15297254-15-Hydroxy-11 alpha,9...,
pubmed-meshheading:15297254-Animals,
pubmed-meshheading:15297254-Anion Exchange Protein 1, Erythrocyte,
pubmed-meshheading:15297254-Anoxia,
pubmed-meshheading:15297254-Erythrocytes,
pubmed-meshheading:15297254-Hemoglobins,
pubmed-meshheading:15297254-Humans,
pubmed-meshheading:15297254-Nitric Oxide,
pubmed-meshheading:15297254-Nitrosation,
pubmed-meshheading:15297254-Oxygen,
pubmed-meshheading:15297254-Pulmonary Circulation,
pubmed-meshheading:15297254-Rats,
pubmed-meshheading:15297254-Rats, Sprague-Dawley,
pubmed-meshheading:15297254-Vasoconstriction,
pubmed-meshheading:15297254-Vasoconstrictor Agents,
pubmed-meshheading:15297254-Vasodilation
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pubmed:year |
2004
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pubmed:articleTitle |
Pulmonary vascular effects of red blood cells containing S-nitrosated hemoglobin.
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pubmed:affiliation |
Dept. of Anesthesiology, PO Box 359724, Harborview Medical Center, Seattle, WA 98104-2499, USA. sdeem@u.washington.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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