000147178 001__ 147178
000147178 005__ 20241212141913.0
000147178 0247_ $$2doi$$a10.1080/01652176.2024.2424837
000147178 0248_ $$2sideral$$a140948
000147178 037__ $$aART-2024-140948
000147178 041__ $$aeng
000147178 100__ $$0(orcid)0000-0002-2079-0711$$aPérez-Lázaro, Sonia$$uUniversidad de Zaragoza
000147178 245__ $$aNew preclinical biomarkers for prion diseases in the cerebrospinal fluid proteome revealed by mass spectrometry
000147178 260__ $$c2024
000147178 5060_ $$aAccess copy available to the general public$$fUnrestricted
000147178 5203_ $$aCurrent diagnostic methods for prion diseases only work in late stages of the disease when neurodegeneration is irreversible. Therefore, biomarkers that can detect the disease before the onset of clinical symptoms are necessary. High-throughput discovery proteomics is of great interest in the search for such molecules. Here we used mass spectrometry to analyse the cerebrospinal fluid proteome in an animal prion disease: preclinical and clinical sheep affected with natural scrapie, and healthy sheep. Interestingly, we found 46 proteins in the preclinical stage that were significantly altered (p < 0.01) compared to healthy sheep, mainly associated with biological processes such as stress and inflammatory responses. Five of them were selected for validation by enzyme-like immunosorbent assay: synaptotagmin binding, cytoplasmic RNA interacting protein (SYNCRIP), involved in nucleic acid metabolism; phospholipase D3 (PLD3) and cathepsin D (CTSD), both related to lysosomal apoptosis; complement component 4 (C4), an element of the classical immune response; and osteopontin (SPP1), a proinflammatory cytokine. These proteins significantly increased in the preclinical stage and maintained their levels in the clinical phase, except for CTSD, whose concentration returned to basal levels in the clinical group. Further research is ongoing to explore their potential as preclinical biomarkers of prion diseases.
000147178 536__ $$9info:eu-repo/grantAgreement/ES/MICINN/PID2021-125398OB-I00$$9info:eu-repo/grantAgreement/ES/MICINN/RTI2018-098711-B-I00
000147178 540__ $$9info:eu-repo/semantics/openAccess$$aby-nc$$uhttp://creativecommons.org/licenses/by-nc/3.0/es/
000147178 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000147178 700__ $$aBarrio, Tomás
000147178 700__ $$aBravo, Susana B.
000147178 700__ $$0(orcid)0000-0002-4213-2904$$aSevilla, Eloisa$$uUniversidad de Zaragoza
000147178 700__ $$0(orcid)0000-0001-9075-2764$$aOtero, Alicia$$uUniversidad de Zaragoza
000147178 700__ $$aChantada-Vázquez, María del Pilar
000147178 700__ $$0(orcid)0000-0001-6016-4726$$aMartín-Burriel, Inmaculada$$uUniversidad de Zaragoza
000147178 700__ $$aRequena, Jesús R.
000147178 700__ $$0(orcid)0000-0002-7173-7216$$aBadiola, Juan J.$$uUniversidad de Zaragoza
000147178 700__ $$0(orcid)0000-0002-2746-3932$$aBolea, Rosa$$uUniversidad de Zaragoza
000147178 7102_ $$11001$$2420$$aUniversidad de Zaragoza$$bDpto. Anatom.,Embri.Genét.Ani.$$cÁrea Genética
000147178 7102_ $$11009$$2773$$aUniversidad de Zaragoza$$bDpto. Patología Animal$$cÁrea Sanidad Animal
000147178 773__ $$g44, 1 (2024), 1-15$$pVet. q.$$tVETERINARY QUARTERLY$$x0165-2176
000147178 787__ $$tProteomeXchange Consortium - Mass spectrometry proteomic data$$wPXD050656
000147178 8564_ $$s2193486$$uhttps://zaguan.unizar.es/record/147178/files/texto_completo.pdf$$yVersión publicada
000147178 8564_ $$s3096801$$uhttps://zaguan.unizar.es/record/147178/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000147178 909CO $$ooai:zaguan.unizar.es:147178$$particulos$$pdriver
000147178 951__ $$a2024-12-12-12:44:28
000147178 980__ $$aARTICLE