2019
DOI: 10.1007/s12035-018-1459-0
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Abstract: Both sporadic variably protease-sensitive prionopathy (VPSPr) and familial Creutzfeldt-Jakob disease linked to the prion protein (PrP) V180I mutation (fCJD V180I ) have been found to share a unique pathological prion protein (PrP Sc ) that lacks the protease-resistant PrP Sc glycosylated at residue 181 because two of four PrP glycoforms are apparently not converted into the PrP Sc from their cellular PrP (PrP … Show more

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Cited by 7 publications
(12 citation statements)
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“…We also examined seeding activity of fCJD V180I as another control since fCJD V180I exhibited a similar PrP Sc electrophoretic profile to VPSPr [ 17 , 27 , 28 , 34 ]. Although the PrP Sc ThT aggregation fluorescent intensity of sCJDMV2 brain homogenates was significantly decreased until 10 −8 dilution, weak ThT fluorescent reaction was still detectable as low as 10 −10 ( Figure 7 A), consistent with our previous observations [ 44 ]. In contrast, of the three genotypes of VPSPr cases, while the PrP Sc -fluorescence from VPSPr129VV and 129MV only reached approximately 80% of maximal fluorescence even at the lowest dilutions of 10 −3 –10 −4 , the PrP Sc -ThT fluorescence from VPSPr129MM could reach the plateau after 40 h at dilution of 10 −3 to 10 −5 and significantly decreased after 10 −6 dilution ( Figure 7 B–D).…”
Section: Resultssupporting
confidence: 92%
“…We also examined seeding activity of fCJD V180I as another control since fCJD V180I exhibited a similar PrP Sc electrophoretic profile to VPSPr [ 17 , 27 , 28 , 34 ]. Although the PrP Sc ThT aggregation fluorescent intensity of sCJDMV2 brain homogenates was significantly decreased until 10 −8 dilution, weak ThT fluorescent reaction was still detectable as low as 10 −10 ( Figure 7 A), consistent with our previous observations [ 44 ]. In contrast, of the three genotypes of VPSPr cases, while the PrP Sc -fluorescence from VPSPr129VV and 129MV only reached approximately 80% of maximal fluorescence even at the lowest dilutions of 10 −3 –10 −4 , the PrP Sc -ThT fluorescence from VPSPr129MM could reach the plateau after 40 h at dilution of 10 −3 to 10 −5 and significantly decreased after 10 −6 dilution ( Figure 7 B–D).…”
Section: Resultssupporting
confidence: 92%
“…However, when PrP Q227X was used to seed amplification by PMCA in the presence of PrP Wt from the humanized Tg mouse brain homogenate, the gel profile of the amplified PrP Sc virtually was similar to that of PrP Sc amplified from sCJD controls. This phenomenon was also observed when PrP Sc from VPSPr was amplified by PMCA, which also generated a PrP res similar to that of sCJD controls [23]. It seems that the atypical PrP Sc does not follow the template-directed refolding hypothesis instead of the seeddirected refolding hypothesis.…”
Section: Discussionmentioning
confidence: 83%
“…Next, we determined whether PrP Sc from GSS linked to PrP Q227X mutation is able to convert wild-type human PrP with either 129VV (PrP-129V) or 129MM (PrP-129M) polymorphism in vitro by protein misfolding cyclic amplification (PMCA). The wild-type human PrP C molecule used as a substrate in PMCA was from brain homogenates of humanized Tg mice expressing wild-type human PrP carrying 129VV (TgWV, mV) or PrP-129MM (Tg40h, mM), autopsy human brain homogenates carrying PrP-129VV (hV) or PrP-129MM (hM), or M17 cell lysates transfected with human PrP-129MM (cM) as described previously [ 22 , 23 ]. In the presence of PrP C from brain homogenates of humanized Tg mice (mV or mM) as the substrate, PMCA produced intense PrP res in the PMCA samples (Fig.…”
Section: Resultsmentioning
confidence: 99%
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