Linked Life Data

1911857

Source:http://linkedlifedata.com/resource/pubmed/id/1911857

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-11-8
pubmed:abstractText
The effect of the anionic detergent sodium dodecyl sulfate (SDS) on human PAI-1 present in plasma, platelet extracts and endothelial cell cultures, was examined. Using the dye partitional extraction method of Mukerjee [1956) Anal. Chem. 28, 870-873) to quantitate ionic surfactants, and a discontinuous spectrophotometric assay for the titration of PAI-1 based on the measurement of residual active t-PA, we found (i) that SDS remains tightly bound to PAI-1 after equilibrium dialysis and (ii) that the activity of the latter was closely related to the amount of SDS carried over by the PAI-1 solution. The highest concentrations of SDS (ratio of SDS to protein greater than 0.1) were detected in the platelet-derived sources of PAI-1 which also showed the lowest residual t-PA activity. Moreover, it is demonstrated by SDS-PAGE and autoradiography that the tight binding of SDS to PAI-1 decreases its ability to form complexes with t-PA. Similar results were obtained with PAI-1 previously inactivated at 37 degrees C: the inability of PAI-1 to form complexes with t-PA was unchanged after SDS treatment. These observations suggest that the decrease in the residual activity of t-PA observed with the SDS-treated PAI-1 preparations is not related to an increase in the inhibitory activity of PAI-1. In fact, SDS was able to produce a decrease in both the binding of t-PA to fibrin and the activation of plasminogen by fibrin-bound t-PA. Bovine PAI-1 has been shown to exist in a latent SDS-activatable form. Our data indicate that such a form might not be present in the human sources of PAI-1 we have tested.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
1079
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-9
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The formation of complexes between human plasminogen activator inhibitor-1 (PAI-1) and sodium dodecyl sulfate: possible implication in the functional properties of PAI-1.
pubmed:affiliation
Institut National de la Santé et de la Recherche Médicale, Hôpital de Bicêtre, France.
pubmed:publicationType
Journal Article