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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1992-9-21
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pubmed:abstractText |
Secretory leukoprotease inhibitor (SLPI), a 12-kDa serine antiprotease, normally protects the upper airway epithelial surface from attack by neutrophil elastase (NE). In the context that a variety of inflammatory lung diseases are characterized by large neutrophil burdens with resultant high levels of NE in the lung, recombinant SLPI (rSLPI), a molecule identical to natural SLPI, may be an effective means to augment the anti-NE protective screen of the lung. To determine whether intravenous rSLPI will augment respiratory tract and epithelial surface levels of SLPI and anti-NE capacity, rSLPI was administered intravenously to sheep and SLPI levels were quantified in plasma, lung lymph (as a measure of lung interstitial levels), lung epithelial lining fluid (ELF), and urine. rSLPI (1 g) was administered over 10 min, and after 30 min plasma levels of SLPI were 8 microM and decreased with a half-life of 1.8 h. Lymph SLPI levels paralleled the plasma levels: 4 h after infusion the lymph-to-plasma ratio was 0.8. ELF SLPI levels paralleled the lymph levels: 4 h after infusion the ELF-to-lymph ratio was 0.3. Western analysis demonstrated intact SLPI in lymph and ELF, and functional analysis showed increases in lymph and ELF anti-NE capacity that paralleled the levels of SLPI. As might be expected from a protein with a molecular mass of 12 kDa, urine excretion was high, with 20% of the SLPI excreted over 5 h. However, if the rate of infusion was slowed, SLPI excretion decreased significantly, with a 3-h infusion associated with 9% excretion and a 12-h infusion associated with less than 0.2% excretion.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteinase Inhibitory Proteins...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteinase Inhibitors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
8750-7587
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
73
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
317-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1354669-Animals,
pubmed-meshheading:1354669-Blotting, Western,
pubmed-meshheading:1354669-Chromatography, High Pressure Liquid,
pubmed-meshheading:1354669-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:1354669-Epithelium,
pubmed-meshheading:1354669-Female,
pubmed-meshheading:1354669-Injections, Intravenous,
pubmed-meshheading:1354669-Lung,
pubmed-meshheading:1354669-Neutrophils,
pubmed-meshheading:1354669-Pancreatic Elastase,
pubmed-meshheading:1354669-Proteinase Inhibitory Proteins, Secretory,
pubmed-meshheading:1354669-Proteins,
pubmed-meshheading:1354669-Recombinant Proteins,
pubmed-meshheading:1354669-Serine Proteinase Inhibitors,
pubmed-meshheading:1354669-Sheep
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pubmed:year |
1992
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pubmed:articleTitle |
Intravenous recombinant secretory leukoprotease inhibitor augments antineutrophil elastase defense.
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pubmed:affiliation |
Pulmonary Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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