Examination of phosphorylated tau protein as a PHF-precursor at early stage Alzheimer's disease
| Autor: | Raúl Mena, Charles R. Harrington, Patricia C. Edwards, John H. Xuereb, Elizabeth B. Mukaetova-Ladinska, Carol Brayne, Claude Michel Wischik, Damon Wischik, Robert Y. K. Lai, Martin Roth, Felicia A. Huppert, Eugene S. Paykel, Herman N.-J. Gertz |
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| Rok vydání: | 1995 |
| Předmět: |
Aging
Pathology medicine.medical_specialty Microtubule-associated protein Proteolysis Tau protein Central nervous system Enzyme-Linked Immunosorbent Assay tau Proteins Pathogenesis Degenerative disease Alzheimer Disease mental disorders medicine Humans Phosphorylation Protein Precursors Aged Brain Chemistry biology medicine.diagnostic_test General Neuroscience Antibodies Monoclonal Brain Neurofibrillary Tangles medicine.disease medicine.anatomical_structure biology.protein Neurofibrils Neurology (clinical) Geriatrics and Gerontology Alzheimer's disease Developmental Biology |
| Zdroj: | Neurobiology of aging. 16(3) |
| ISSN: | 0197-4580 |
| Popis: | Hyperphosphorylated tau protein which can be isolated on the basis of insolubility in 1076 sarkosyl (A68-tau fraction) is thought to represent a precursor pool for PHF assembly, associated histologically with neuritic pathology, which feeds into a more resistant tangle-associated PHF pool via cross-linking and proteolysis. We examined these predictions at the earliest detectable stages of neurofibrillary pathology. We report that there is no evidence that neuritic pathology represents an early pathologic stage, no evidence of an association between neuritic pathology and phosphorylated tau, no evidence of selective accumulation of phosphorylated tau at early stages of pathology, and no evidence for a precursor/product relationship between phosphorylated tau and PHFs during progression of pathology. We conclude that altered phosphorylation is a secondary process affecting 5% of PHFs and does not explain PHF assembly in Alzheimer's disease. |
| Databáze: | OpenAIRE |
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