Protease prion protein sensitive

Caughey, B., Brown, K., Raymond, G.J., Katzenstein, G.E., and Thresher, W. (1994). Binding of the protease-sensitive form of PrP (prion protein) to sulfated gly-cosaminoglycan and Congo red [corrected] [published erratum appears in /. Virol. 1994Jun 68(6) 4107]./ Virol. 68, 2135-2141. 

The combined term prion protein (PrP) refers to tbe protein ratber than tbe infectious agent. However, it is increasingly apparent tbat PrP exists in a wide variety of forms tbat are normal (e.g., PrP -), TSE-associated (e.g., PrP , PrPflJ, PrP ), neither (e.g., various recombinant and/or mutated versions of tbe PrP structure), or both. This structural diversity complicates the use of Prusiner s original terms PrP " (cellular PrP) and PrP (scrapie PrP). These terms are still useful under many circumstances, but often need further, more operational and/or functional qualification as the sophistication of current studies increases. Eor instance, since protease resistance is most commonly used to discriminate normal and TSE-associated forms of PrP, the operational terms PrP-sen (protease-sensitive PrP) and PrP-res (protease-... 

Prion diseases resulting in encephalopathy can be transmitted between individuals within species (more rarely between species) [26-28], A conformational variant of the normal cellular protein PrPs (PrPc) (protease-sensitive or cellular) is believed to catalyze [29] or nucleate [30-33] conversion to the pathological form, PrPR (protease-resistant). This highly unusual nongenetic mode of transmission of an infectious agent has been strongly debated [29]. The observation of multiple examples of nucleated catalysis of aberrant polymerization of protein subunits has... 

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