Linked Life Data

2764383

Source:http://linkedlifedata.com/resource/pubmed/id/2764383

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1989-9-8
pubmed:abstractText
Human lung antileukoprotease (ALP) is a potent inhibitor of neutrophil elastase that is locally produced by submucosal bronchial glands and by secretory cells in the bronchiolar epithelium. In a recent light microscopic investigation, ALP was detected in the connective tissue matrix of the lung. The present immunoelectron microscopic study was performed in order to extend our knowledge about the exact localization of ALP in the extracellular matrix of the lung. Both elastin and ALP were detected in central and peripheral human lung specimens using specific antibodies in a two-step, gold-labeling procedure. ALP could be demonstrated in the parenchymal matrix of the alveolar walls exclusively in association with the amorphous elastin fibers. In addition, the subepithelial connective tissue of the bronchial wall also showed a clear labeling for ALP, which was present exclusively over the elastin fibers. The results of this study strongly suggest that ALP play a modulating role in destructive pulmonary diseases such as emphysema in which degradation of elastin fibers by elastase is thought to occur.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0003-0805
pubmed:author
pubmed:issnType
Print
pubmed:volume
140
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
471-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Antileukoprotease is associated with elastin fibers in the extracellular matrix of the human lung. An immunoelectron microscopic study.
pubmed:affiliation
Department of Pulmonology, University Hospital, Leiden, The Netherlands.
pubmed:publicationType
Journal Article, In Vitro