Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
|
| pubmed:dateCreated |
1992-10-16
|
| pubmed:abstractText |
Cultured bovine aortic endothelial cells (BAEC) released endothelin-1 (ET-1) in the culture medium in a time-dependent fashion. Coincubation of fMLP-activated human polymorphonuclear leukocytes (PMN) with BAEC caused a fast (maximal activity was reached within 15 minutes) and cell number-dependent disappearance of ET-1 from the medium. This effect was direct to ET-1, because it was also present when PMN were incubated with the synthetic peptide in the absence of BAEC. PMN-dependent disappearance of ET-1 was associated with loss of constrictor activity on isolated rabbit aorta. PMN-released products were responsible for ET-1 degrading activity, because supernatants of activated PMN were equally effective as the intact cells. Resting PMN, in the same time frame, were uneffective. Eglin C, a potent blocker of PMN-derived elastase and cathepsin G, reversed the ET-1 inhibitory activity of fMLP-stimulated PMN and of their supernatant. Direct addition of elastase and cathepsin G to synthetic ET-1 destroyed its immunoreactivity and this effect was blocked by eglin C. High-performance liquid chromatography (HPLC) analysis supported the hypothesis that ET-1 degradation by PMN was due to enzymatic proteolysis. These data provide evidence that activated PMN are able to degrade ET-1 through the release of proteases. Because physiologic concentrations of PMN can destroy high amounts (up to 100 nmol/L) of ET-1 within a few minutes, we propose that this mechanism of ET-1 inactivation has biologic relevance.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CTSG protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin G,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Culture Media,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Endothelins,
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Nov
|
| pubmed:issn |
0006-4971
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
78
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
2715-20
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:1824263-Animals,
pubmed-meshheading:1824263-Aorta,
pubmed-meshheading:1824263-Cathepsin G,
pubmed-meshheading:1824263-Cathepsins,
pubmed-meshheading:1824263-Cattle,
pubmed-meshheading:1824263-Cells, Cultured,
pubmed-meshheading:1824263-Culture Media,
pubmed-meshheading:1824263-Endopeptidases,
pubmed-meshheading:1824263-Endothelins,
pubmed-meshheading:1824263-Endothelium, Vascular,
pubmed-meshheading:1824263-Humans,
pubmed-meshheading:1824263-Kinetics,
pubmed-meshheading:1824263-Muscle, Smooth, Vascular,
pubmed-meshheading:1824263-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:1824263-Neutrophils,
pubmed-meshheading:1824263-Pancreatic Elastase,
pubmed-meshheading:1824263-Protease Inhibitors,
pubmed-meshheading:1824263-Rabbits,
pubmed-meshheading:1824263-Serine Endopeptidases,
pubmed-meshheading:1824263-Vasoconstriction
|
| pubmed:year |
1991
|
| pubmed:articleTitle |
Inactivation of endothelin by polymorphonuclear leukocyte-derived lytic enzymes.
|
| pubmed:affiliation |
University of Chieti G. D'Annunzio, School of Medicine, Italy.
|
| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|