Linked Life Data

1362620

Source:http://linkedlifedata.com/resource/pubmed/id/1362620

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1993-2-19
pubmed:abstractText
Neutrophil proteinase 4 (NP4) is a major neutral proteinase of the human polymorphonuclear (PMN) leukocyte, which is present in amounts similar to leukocyte elastase. NP4(3) is a potent, non-specific proteinase, which may degrade structural and soluble proteins in the tissues and body fluids, and it has been implicated as an important pathogenetic factor in lung emphysema. We have studied the release of elastase and NP4(3) in an in vitro model of phagocytosis. alpha 1-proteinase inhibitor (alpha 1-PI) is the major plasma inhibitor of both leukocyte elastase and NP4(3), but alpha 1-PI bound leukocyte elastase more readily than NP4(3). The basic conditions were designed so that some proteolytic activity was present in the medium. Addition of increasing amounts of Secretory leukocyte protease inhibitor (SLPI) to the incubation mixtures resulted in binding of leukocyte elastase to this inhibitor and extinction of free proteolytic activity against both natural and synthetic substrates. The progressive binding of leukocyte elastase to SLPI instead of alpha 1-PI was paralleled by an increasing binding of NP4(3) to alpha 1-PI. SLPI is a potent inhibitor of leukocyte elastase and cathepsin G, and although it lacks inhibitory effect on NP4(3), it may obviously indirectly aid in the binding and inhibition of NP4(3) to alpha 1-PI, by taking care of at least part of the leukocyte elastase. As a specific NP4(3)-inhibitor is not readily available for therapeutic use, this effect may prove useful under in vivo conditions and enhance the protective effect of administered recombinant human SLPI.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0036-5513
pubmed:author
pubmed:issnType
Print
pubmed:volume
52
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
823-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:1362620-Amino Acid Sequence, pubmed-meshheading:1362620-Biotin, pubmed-meshheading:1362620-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:1362620-Humans, pubmed-meshheading:1362620-Immunochemistry, pubmed-meshheading:1362620-Leukocyte Elastase, pubmed-meshheading:1362620-Leukocytes, pubmed-meshheading:1362620-Molecular Sequence Data, pubmed-meshheading:1362620-Myeloblastin, pubmed-meshheading:1362620-Pancreatic Elastase, pubmed-meshheading:1362620-Phagocytosis, pubmed-meshheading:1362620-Proteinase Inhibitory Proteins, Secretory, pubmed-meshheading:1362620-Proteins, pubmed-meshheading:1362620-Secretory Leukocyte Peptidase Inhibitor, pubmed-meshheading:1362620-Serine Endopeptidases, pubmed-meshheading:1362620-Serine Proteinase Inhibitors, pubmed-meshheading:1362620-alpha 1-Antitrypsin
pubmed:year
1992
pubmed:articleTitle
Release of neutrophil proteinase 4(3) and leukocyte elastase during phagocytosis and their interaction with proteinase inhibitors.
pubmed:affiliation
Department of Surgery, Lund University, Malmö General Hospital, Sweden.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't