Tau Protein Phosphorylated at Threonine-231 is Expressed Abundantly in the Cerebellum in Prion Encephalopathies
| العنوان: | Tau Protein Phosphorylated at Threonine-231 is Expressed Abundantly in the Cerebellum in Prion Encephalopathies |
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| المؤلفون: | Miguel Ángel Ontiveros-Torres, Fidel de la Cruz, Mar Pacheco-Herrero, Marely Bravo-Muñoz, Vıctor Manuel Gómez-López, José Luna-Muñoz, Parménides Guadarrama-Ortíz, Petra Yescas, Ignacio Villanueva-Fierro, Amparo Viramontes-Pintos, Charles R. Harrington, Linda Garcés-Ramírez, Sandra Martínez-Robles, Mario Hernandes-Alejandro, Francisco Montiel-Sosa |
| المصدر: | Journal of Alzheimer's Disease |
| بيانات النشر: | IOS Press, 2021. |
| سنة النشر: | 2021 |
| مصطلحات موضوعية: | Male, Threonine, 0301 basic medicine, Pathology, Cerebellum, animal diseases, Matrix metalloproteinase, Creutzfeldt-Jakob Syndrome, Prion Diseases, 0302 clinical medicine, Aged, 80 and over, Brain Diseases, Glial fibrillary acidic protein, biology, General Neuroscience, General Medicine, Middle Aged, neuronal death, Encephalopathy, Bovine Spongiform, Psychiatry and Mental health, Clinical Psychology, medicine.anatomical_structure, Phosphorylation, Female, medicine.symptom, Research Article, Adult, medicine.medical_specialty, Bovine spongiform encephalopathy, Tau protein, prion encephalopathy, tau Proteins, tau protein, 03 medical and health sciences, mental disorders, medicine, Animals, Humans, Aged, medicine.disease, nervous system diseases, 030104 developmental biology, nervous system, Gliosis, prion protein, biology.protein, Cattle, Geriatrics and Gerontology, 030217 neurology & neurosurgery, Spongiosis |
| الوصف: | 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. |
| تدمد: | 1875-8908 1387-2877 |
| DOI: | 10.3233/jad-201308 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d759c8142e4c916a166200762ee3049e https://doi.org/10.3233/jad-201308 |
| Rights: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....d759c8142e4c916a166200762ee3049e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 18758908 13872877 |
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| DOI: | 10.3233/jad-201308 |