Tau Protein Phosphorylated at Threonine-231 Is Expressed Abundantly in the Cerebellum in Prion Encephalopathies

Víctor Manuel Gómez-López, Amparo Viramontes-Pintos, Miguel Angel Ontiveros-Torres, Linda Garcés-Ramírez, Fidel De La Cruz-López, Ignacio Villanueva-Fierro, Marely Bravo-Muñoz, Charles Harrington, Sandra Martínez-Robles, Petra Yescas, Parménides Guadarrama-Ortíz, Mario Hernandes-Alejandro, José Francisco Montiel-Sosa, Mar Pacheco-Herrero, José Luna-Muñoz* (Corresponding Author)

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Background: Transmissible spongiform encephalopathies (TSEs) are rare neurodegenerative disorders that affect animals and humans. Bovine spongiform encephalopathy (BSE) in cattle, and Creutzfeld-Jakob Disease (CJD) in humans belong to this group. The causative agent of TSEs is called “prion”, which corresponds to a pathological form (PrPSc) of a normal cellular protein (PrPC) expressed in nerve cells. PrPSc is resistant to degradation and can induce abnormal folding of PrPC, and TSEs are characterized by extensive spongiosis and gliosis and the presence of PrPSc amyloid plaques. CJD presents initially with clinical symptoms similar to Alzheimer's disease (AD). In AD, tau aggregates and amyloid-β protein plaques are associated with memory loss and cognitive impairment in patients. Objective: In this work, we study the role of tau and its relationship with PrPSc plaques in CJD. Methods: Multiple immunostainings with specific antibodies were carried out and analyzed by confocal microscopy. Results: We found increased expression of the glial fibrillary acidic protein (GFAP) and matrix metalloproteinase (MMP-9), and an exacerbated apoptosis in the granular layer in cases with prion disease. In these cases, tau protein phosphorylated at Thr-231 was overexpressed in the axons and dendrites of Purkinje cells and the extensions of parallel fibers of the cerebellum. Conclusion: We conclude that phosphorylation of tau may be a response to the toxic and inflammatory environment generated by the pathological form of prion.
Original languageEnglish
Pages (from-to)769-785
Number of pages17
JournalJournal of Alzheimer's Disease
Volume81
Issue number2
Early online date2 Apr 2021
DOIs
Publication statusPublished - 18 May 2021

Keywords

  • Cerebellum
  • neuronal death
  • prion encephalopathy
  • prion protein
  • tau protein

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