Open AccessTau Protein Phosphorylated at Threonine-231 is Expressed Abundantly in the Cerebellum in Prion Encephalopathies
Author(s) -
Vıctor Manuel Gómez-López,
Amparo ViramontesPintos,
Miguel Ángel Ontiveros-Torres,
Linda GarcésRamírez,
Fidel de la Cruz,
Ignacio Villanueva-Fierro,
Marely Bravo-Muñoz,
Charles R. Harrington,
Sandra Martínez-Robles,
Petra Yescas,
Parménides Guadarrama-Ortíz,
Mario Hernándes-Alejandro,
Francisco Montiel-Sosa,
Mar Pacheco-Herrero,
José LunaMuñoz
Publication year - 2021
Publication title -
journal of alzheimer's disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.677
H-Index - 139
eISSN - 1875-8908
pISSN - 1387-2877
DOI - 10.3233/jad-201308
Subject(s) - gliosis , pathology , neurodegeneration , cerebellum , bovine spongiform encephalopathy , glial fibrillary acidic protein , fatal familial insomnia , biology , medicine , neuroscience , disease , immunohistochemistry , prion protein
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 in the cerebellum. Conclusion: We conclude that phosphorylation of tau may be a response to a toxic and inflammatory environment generated by the pathological form of prion.