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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2005-5-13
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pubmed:abstractText |
Lung surfactant dipalmitoylphosphatidylcholine (DPPC) is endocytosed by alveolar epithelial cells and degraded by lysosomal-type phospholipase A2 (aiPLA2). This enzyme is identical to peroxiredoxin 6 (Prdx6), a bifunctional protein with PLA2 and GSH peroxidase activities. Lung phospholipid was studied in Prdx6 knockout (Prdx6-/-) mice. The normalized content of total phospholipid, phosphatidylcholine (PC), and disaturated phosphatidylcholine (DSPC) in bronchoalveolar lavage fluid, lung lamellar bodies, and lung homogenate was unchanged with age in wild-type mice but increased progressively in Prdx6-/- animals. Degradation of internalized [3H]DPPC in isolated mouse lungs after endotracheal instillation of unilamellar liposomes labeled with [3H]DPPC was significantly decreased at 2 h in Prdx6-/- mice (13.6 +/- 0.3% vs. 26.8 +/- 0.8% in the wild type), reflected by decreased dpm in the lysophosphatidylcholine and the unsaturated PC fractions. Incorporation of [14C]palmitate into DSPC at 24 h after intravenous injection was decreased by 73% in lamellar bodies and by 54% in alveolar lavage surfactant in Prdx6-/- mice, whereas incorporation of [3H]choline was decreased only slightly. Phospholipid metabolism in Prdx6-/- lungs was similar to that in wild-type lungs treated with MJ33, an inhibitor of aiPLA2 activity. These results confirm an important role for Prdx6 in lung surfactant DPPC degradation and synthesis by the reacylation pathway.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1,2-Dipalmitoylphosphatidylcholine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxin VI,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxiredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Prdx6 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Surface-Active Agents
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-2275
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
46
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1248-56
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:15772425-1,2-Dipalmitoylphosphatidylcholine,
pubmed-meshheading:15772425-Animals,
pubmed-meshheading:15772425-Bronchoalveolar Lavage Fluid,
pubmed-meshheading:15772425-Calcium,
pubmed-meshheading:15772425-Epithelial Cells,
pubmed-meshheading:15772425-Gene Deletion,
pubmed-meshheading:15772425-Glutathione Peroxidase,
pubmed-meshheading:15772425-Hydrogen-Ion Concentration,
pubmed-meshheading:15772425-Liposomes,
pubmed-meshheading:15772425-Lung,
pubmed-meshheading:15772425-Lysophosphatidylcholines,
pubmed-meshheading:15772425-Lysosomes,
pubmed-meshheading:15772425-Mice,
pubmed-meshheading:15772425-Mice, Inbred C57BL,
pubmed-meshheading:15772425-Mice, Knockout,
pubmed-meshheading:15772425-Mice, Transgenic,
pubmed-meshheading:15772425-Perfusion,
pubmed-meshheading:15772425-Peroxidases,
pubmed-meshheading:15772425-Peroxiredoxin VI,
pubmed-meshheading:15772425-Peroxiredoxins,
pubmed-meshheading:15772425-Phenotype,
pubmed-meshheading:15772425-Phosphatidylcholines,
pubmed-meshheading:15772425-Phospholipases A,
pubmed-meshheading:15772425-Phospholipases A2,
pubmed-meshheading:15772425-Phospholipids,
pubmed-meshheading:15772425-Pulmonary Alveoli,
pubmed-meshheading:15772425-Surface-Active Agents,
pubmed-meshheading:15772425-Time Factors
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pubmed:year |
2005
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pubmed:articleTitle |
Altered lung phospholipid metabolism in mice with targeted deletion of lysosomal-type phospholipase A2.
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pubmed:affiliation |
Institute for Environmental Medicine, University of Pennsylvania Medical Center, Philadelphia, PA, USA. abf@mail.med.upenn.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Extramural
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