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Crutchley, D.J. et al.

Endotoxin-induced secretion of an active plasminogen activator inhibitor from bovine pulmonary arterial and aortic endothelial cells.

Treatment of bovine pulmonary arterial and aortic endothelial cells for 24 h with 10-20 ng/ml endotoxin appeared to suppress urokinase secretion by over 90%. Immunodepletion of urokinase from conditioned medium revealed high levels of a fully active plasminogen activator inhibitor ( PAI). In contrast, medium from aortic cells not treated with endotoxin expressed low levels of a latent PAI. The endotoxin-induced PAI from both cell types was not immunoprecipitated by incubation with IgG directed against the endothelial-type inhibitor, PAI-1, or antiserum directed against the placental-type inhibitor, PAI-2. Endotoxin-induced PAI was inactivated by 0.2-1.0 M of 2-mercaptoethanol, but unaffected by treatment with up to 500 microM of chloramine-T. We conclude that the exposure of bovine endothelial cells to endotoxin causes the secretion of a fully active PAI with properties different from those reported for PAI-1.[1]

References

Endotoxin-induced secretion of an active plasminogen activator inhibitor from bovine pulmonary arterial and aortic endothelial cells. Crutchley, D.J., Conanan, L.B., Ryan, U.S. Biochem. Biophys. Res. Commun. (1987) [Pubmed]

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