Sala-Jarque, JuliaGil Fernández, VanessaAndrés-Benito, PolMartínez-Soria, InésPicón-Pagès, PolHernández, FélixÁvila, JesúsLanciego, José LuisNuvolone, MarioAguzzi, AdrianoGavín Marín, RosalinaFerrer, IsidroRío Fernández, José Antonio del2024-11-122024-11-122024-09-162045-2322https://hdl.handle.net/2445/216423The cellular prion protein (PrPC) plays many roles in the developing and adult brain. In addition, PrPC binds to several amyloids in oligomeric and prefibrillar forms and may act as a putative receptor of abnormal misfolded protein species. The role of PrPC 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+/+), Prnp0/0 (ZH3 strain) mice, and mice over-expressing the secreted form of PrPC 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 Mapt0/0 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 PrPC does not affect tau seeding and spreading in vivo.14 p.application/pdfengcc-by (c) Sala-Jarque, J. et al., 2024http://creativecommons.org/licenses/by/4.0/Malaltia d'AlzheimerMicrotúbulsPrionsAlzheimer's diseaseMicrotubulesPrionsinfo:eu-repo/semantics/article2024-11-12info:eu-repo/semantics/openAccessPMID: 39284839