Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1982-8-7
pubmed:abstractText
Cell lysates from cultured human alveolar macrophages contain detectable amounts of an elastinolytic enzyme. Although particulate elastin was solubilized only after prolonged incubations, lysates readily hydrolyzed T-OC-alanyl-p-nitrophenol-ester. Hydrolysis of the latter substrate was inhibited by the leukocyte elastase site-specific inhibitor, N-ac-(ala)4-chloromethyl ketone. In addition, radioimmunoelectrophoresis of concentrated alveolar macrophage lysates, previously incubated with 3H diisopropyl-phosphofluoridate (DFP), revealed the presence of DFP binding material that comigrated with inactivated human leukocyte elastase. Human leukocyte elastase can cause lung lesions resembling pulmonary emphysema in experimental animals; therefore, the clearance of this enzyme by alveolar macrophages may represent a significant route for the removal of this potentially pathogenic enzyme from the lung.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0003-0805
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
779-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Evidence for in vivo internalization of human leukocyte elastase by alveolar macrophages.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't