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Platelets retain high levels of active plasminogen activator inhibitor 1

Artikel i vetenskaplig tidskrift
Författare Helén Brogren
Karin Wallmark
J. Deinum
Lena Karlsson
Sverker Jern
Publicerad i PloS one
Volym 6
Nummer/häfte 11
Sidor e26762
ISSN 1932-6203
Publiceringsår 2011
Publicerad vid Institutionen för medicin, avdelningen för akut och kardiovaskulär medicin
Sidor e26762
Språk en
Länkar dx.doi.org/10.1371/journal.pone.002...
Ämneskategorier Medicin och Hälsovetenskap

Sammanfattning

The vascular fibrinolytic system is crucial for spontaneous lysis of blood clots. Plasminogen activator inhibitor 1 (PAI-1), the principal inhibitor of the key fibrinolytic enzyme tissue-type plasminogen activator (tPA), is present in platelets at high concentrations. However, the majority of PAI-1 stored in platelets has been considered to be inactive. Our recent finding (Brogren H, et al. Blood 2004) that PAI-1 de novo synthesized in platelets remained active for over 24 h, suggested that PAI-1 stored in the alpha-granules might be active to a larger extent than previously reported. To re-evaluate this issue, we performed experiments where the fraction of active PAI-1 was estimated by analyzing the tPA-PAI-1 complex formation. In these experiments platelets were lysed with Triton X-100 in the presence of serial dilutions of tPA and subsequently the tPA-PAI-1 complex was evaluated by Western blot. Also, using a non-immunologic assay, tPA was labeled with (125)I, and (125)I-tPA and (125)I-tPA-PAI-1 was quantified by scintigraphy. Interestingly, both methods demonstrated that the majority (>50%) of platelet PAI-1 is active. Further analyses suggested that pre-analytical procedures used in previous studies (sonication or freezing/thawing) may have substantially reduced the activity of platelet PAI-1, which has lead to an underestimation of the proportion of active PAI-1. Our in vitro results are more compatible with the role of PAI-1 in clot stabilization as demonstrated in physiological and pathophysiological studies.

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