| First Author | Sala-Jarque J | Year | 2024 |
| Journal | Sci Rep | Volume | 14 |
| Issue | 1 | Pages | 21622 |
| PubMed ID | 39284839 | Mgi Jnum | J:355385 |
| Mgi Id | MGI:7732676 | Doi | 10.1038/s41598-024-72232-2 |
| Citation | Sala-Jarque J, et al. (2024) The cellular prion protein does not affect tau seeding and spreading of sarkosyl-insoluble fractions from Alzheimer's disease. Sci Rep 14(1):21622 |
| abstractText | The cellular prion protein (PrP(C)) plays many roles in the developing and adult brain. In addition, PrP(C) binds to several amyloids in oligomeric and prefibrillar forms and may act as a putative receptor of abnormal misfolded protein species. The role of PrP(C) in tau seeding and spreading is not known. In the present study, we have inoculated well-characterized sarkosyl-insoluble fractions of sporadic Alzheimer's disease (sAD) into the brain of adult wild-type mice (Prnp(+/+)), Prnp(0/0) (ZH3 strain) mice, and mice over-expressing the secreted form of PrP(C) lacking their GPI anchor (Tg44 strain). Phospho-tau (ptau) seeding and spreading involving neurons and oligodendrocytes were observed three and six months after inoculation. 3Rtau and 4Rtau deposits from the host tau, as revealed by inoculating Mapt(0/0) mice and by using specific anti-mouse and anti-human tau antibodies suggest modulation of exon 10 splicing of the host mouse Mapt gene elicited by exogenous sAD-tau. However, no tau seeding and spreading differences were observed among Prnp genotypes. Our results show that PrP(C) does not affect tau seeding and spreading in vivo. |
