Plasminogen binds to disease-associated prion protein of multiple species

The protein-only hypothesis states that the causative agent of transmissible spongiform encephalopathies is PrP Sc, a conformer of the cellular protein PrP c. Therefore, reagents differentiating between PrP c and PrPS c could be diagnostically useful. Plasminogen, when immobilised onto magnetic bead...

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Veröffentlicht in:The Lancet (British edition) 2001-06, Vol.357 (9273), p.2026-2028
Hauptverfasser: Maissen, Manuela, Roeckl, Christiane, Glatzel, Markus, Goldmann, Wilfred, Aguzzi, Adriano
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Sprache:eng
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Zusammenfassung:The protein-only hypothesis states that the causative agent of transmissible spongiform encephalopathies is PrP Sc, a conformer of the cellular protein PrP c. Therefore, reagents differentiating between PrP c and PrPS c could be diagnostically useful. Plasminogen, when immobilised onto magnetic beads, selectively precipitates PrPSc from mice with prion infected brains. We have shown that human plasminogen also precipitates PrPSc from brain homogenate of patients with sporadic Creutzfeldt-Jakob disease, as well as from sheep with scrapie and cows of various breeds with bovine spongiform encephalophathy (BSE). Our findings suggest that the binding of plasminogen to PrP Sc could have diagnostic application.
ISSN:0140-6736
1474-547X
DOI:10.1016/S0140-6736(00)05110-2