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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1994-9-28
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pubmed:abstractText |
When human leukocyte elastase (HLE) activity (1.0 microgram/ml) was analysed in the presence of PAI-1 (0.15.0 micrograms/ml), HLE activity, measured with the low molecular weight paranitroanilide substrate L-pyroglutamyl-prolyl-L-valine-p-nitroanilide was increased time and dose dependently (a plateau of stimulation was reached after 30 minutes) with a simultaneous decrease in PAI-1 inhibitory activity. This effect was neither influenced by the presence of vitronectin nor heparin. When PAI-1 was converted into its latent form by incubation for 48 hours at 37 degrees C or incubated with an excess of recombinant t-PA to convert free PAI-1 into t-PA-PAI-1 complexes, the stimulatory effect of both the latent and the complexed form of PAI-1 was significantly greater than that of the active form. Analysing HLE PAI-1 interaction on a molecular level using SDS-PAGE, no SDS stable complex formation between HLE and PAI-1 could be observed but lower molecular weight cleavage products of PAI-1 were generated. The stimulatory effect of PAI-1 on HLE activity was not restricted to the low molecular weight pNA-substrate but was also revealed using a natural substrate assay (bovine neck ligament elastin solubilization). Therefore interaction of HLE and PAI-1 seems not to be restricted just to decrease PAI-1 activity but would simultaneously also increase HLE activity, thereby supporting enzymatic activity necessary for migration of leukocytes, dissolution of blood clots and tissue remodelling.
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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/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heparin,
http://linkedlifedata.com/resource/pubmed/chemical/Leukocyte Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Pancreatic Elastase,
http://linkedlifedata.com/resource/pubmed/chemical/Plasminogen Activator Inhibitor 1,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tissue Plasminogen Activator,
http://linkedlifedata.com/resource/pubmed/chemical/Vitronectin
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0049-3848
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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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 |
361-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7521069-Glycoproteins,
pubmed-meshheading:7521069-Heparin,
pubmed-meshheading:7521069-Humans,
pubmed-meshheading:7521069-Leukocyte Elastase,
pubmed-meshheading:7521069-Molecular Weight,
pubmed-meshheading:7521069-Pancreatic Elastase,
pubmed-meshheading:7521069-Plasminogen Activator Inhibitor 1,
pubmed-meshheading:7521069-Recombinant Proteins,
pubmed-meshheading:7521069-Tissue Plasminogen Activator,
pubmed-meshheading:7521069-Vitronectin
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pubmed:year |
1994
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pubmed:articleTitle |
Effect of type-1 plasminogen activator inhibitor on human leukocyte elastase.
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pubmed:affiliation |
Second Department of Internal Medicine, Kumamoto University Medical School, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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