Tau protein phosphorylated at threonine-231 is expressed abundantly in the cerebellum in prion encephalopathies.
Fecha
2021-04-02Autor
Gómez López, Víctor Manuel
Viramontes Pintos, Amparo
Ontiveros Torres, Miguel Ángel
Garcés Ramírez, Linda
Cruz López, Fidel de la
Villanueva Fierro, Ignacio
Bravo Muñoz, Marely
Harrington, Charles R.
Martínez Robles, Sandra
Yescas, Petra
Guadarrama Ortíz, Parménides
Hernándes Alejandro, Mario
Montiel Sosa, Francisco
Pacheco Herrero, Mar
Luna Muñoz, José
Metadatos
Mostrar el registro completo del ítemResumen
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- 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.
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