Source:http://linkedlifedata.com/resource/pubmed/id/21435465
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2011-3-25
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pubmed:abstractText |
Retinopathy of prematurity is a major side effect of oxygen therapy for preterm infants, and is a leading cause of blindness in children. To date, it remains unclear whether the initial microvascular obliteration is triggered by degradation of hypoxia inducible factor (HIF) ? proteins or by other mechanisms such as oxidative stress. Here we show that prolyl hydroxylase domain protein 2 (PHD2), an enzyme mostly responsible for oxygen-induced degradation of HIF-? proteins, plays a major role in oxygen-induced retinopathy in mice. In neonatal mice expressing normal amounts of PHD2, exposure to 75% oxygen caused significant degradation of retinal HIF-? proteins, accompanied by massive losses of retinal microvessels. PHD2 deficiency significantly stabilized HIF-1?, and to some extent HIF-2?, in neonatal retinal tissues, and protected retinal microvessels from oxygen-induced obliteration. After hyperoxia-treated neonatal mice were returned to ambient room air, retinal vasculature in PHD2-deficient mice remained mostly intact and showed very little neoangiogenesis. These findings demonstrate a close association between PHD2-dependent HIF-? degradation and oxygen-induced retinal microvascular obliteration, and imply that PHD2 may be a promising therapeutic target to prevent oxygen-induced retinopathy.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Egln1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Hypoxia-Inducible Factor 1, alpha...,
http://linkedlifedata.com/resource/pubmed/chemical/Oxygen,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen-Proline Dioxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1525-2191
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pubmed:author | |
pubmed:copyrightInfo |
Copyright © 2011 American Society for Investigative Pathology. Published by Elsevier Inc. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:volume |
178
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1881-90
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pubmed:meshHeading |
pubmed-meshheading:21435465-Animals,
pubmed-meshheading:21435465-Animals, Newborn,
pubmed-meshheading:21435465-Anoxia,
pubmed-meshheading:21435465-Astrocytes,
pubmed-meshheading:21435465-Hyperoxia,
pubmed-meshheading:21435465-Hypoxia-Inducible Factor 1, alpha Subunit,
pubmed-meshheading:21435465-Immunohistochemistry,
pubmed-meshheading:21435465-Mice,
pubmed-meshheading:21435465-Mice, Knockout,
pubmed-meshheading:21435465-Oxygen,
pubmed-meshheading:21435465-Pericytes,
pubmed-meshheading:21435465-Procollagen-Proline Dioxygenase,
pubmed-meshheading:21435465-Protein Structure, Tertiary,
pubmed-meshheading:21435465-Retinal Diseases,
pubmed-meshheading:21435465-Retinal Vessels,
pubmed-meshheading:21435465-Reverse Transcriptase Polymerase Chain Reaction
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pubmed:year |
2011
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pubmed:articleTitle |
Prolyl hydroxylase domain protein 2 (PHD2) mediates oxygen-induced retinopathy in neonatal mice.
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pubmed:affiliation |
Center for Vascular Biology, Department of Cell Biology, University of Connecticut Health Center, Farmington, CT 06030-3501, USA.
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pubmed:publicationType |
Journal Article
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