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A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate.
Umeå University, Faculty of Medicine, Department of Medical Biochemistry and Biophysics.
1992 (English)In: European Journal of Biochemistry, ISSN 0014-2956, E-ISSN 1432-1033, Vol. 209, no 3, 985-92 p.Article in journal (Refereed) Published
Abstract [en]

Recombinant plasminogen-activator-inhibitor type 1 (PAI-1) purified in an active form from Escherichia coli and eucaryotic cells was found to contain a mixture of three functionally distinct forms: an active form that forms complexes with plasminogen activators (PAs), an inactive (latent) form that remains intact after incubation with PAs, and a substrate-like form which is easily cleaved by PAs. Since active PAI-1 purified from bacteria (rpPAI-1) contains only trace amounts of the inactive latent and the substrate-like forms, this material was used to study the effect of sodium dodecyl sulphate (SDS) on the structure and function of active PAI-1. After treatment with 0.01% SDS, active rpPAI-1 was converted to an inactive form that did not form complexes with PAs, but exhibited characteristics similar to those of latent PAI-1. After treatment with 0.1% SDS, PAI-1 lost its inhibitory activity and was cleaved as a substrate in the reactive center. Circular dichroism spectral analysis reveals that SDS changed the conformation of PAI-1 dramatically, mainly by increasing its alpha-helical content.

Place, publisher, year, edition, pages
1992. Vol. 209, no 3, 985-92 p.
National Category
Medical and Health Sciences
URN: urn:nbn:se:umu:diva-59905PubMedID: 1425706OAI: diva2:557006
Available from: 2012-09-26 Created: 2012-09-26 Last updated: 2012-09-26

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