Detection of d-aspartate in tau proteins associated with Alzheimer paired helical filaments
| Autor: | Xiao Ran Yang, David S. Dunlop, Wan Kyng Liu, Agnes Kenessey, Shu Hui Yen |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Pathology
medicine.medical_specialty Microtubule-associated protein Proteolysis Immunoblotting Tau protein tau Proteins chemistry.chemical_compound Degenerative disease Alzheimer Disease Pregnancy mental disorders medicine Humans Amino Acids Neurotransmitter Molecular Biology Racemization Brain Chemistry Aspartic Acid biology medicine.diagnostic_test Chemistry Hydrolysis General Neuroscience Neurofibrillary Tangles medicine.disease Molecular biology biology.protein Phosphorylation Electrophoresis Polyacrylamide Gel Female Neurology (clinical) Alzheimer's disease Developmental Biology |
| Zdroj: | Brain Research. 675:183-189 |
| ISSN: | 0006-8993 |
| DOI: | 10.1016/0006-8993(95)00061-t |
| Popis: | Paired helical filaments (PHF) characteristic of Alzheimer neurofibrillary lesions are known to contain a modified form of microtubule associated protein tau. These proteins, PHF-tau, differ from normal tau in the extent and the site of phosphorylation. To determine whether PHF-tau, tau proteins from normal adult brains (N-tau), tau proteins from Alzheimer brains not associated with PHF (A-tau), and tau proteins from fetal brains (F-tau) differ in racemization, these proteins were compared for their d -aspartate content. The results demonstrated that PHF-tau contain more d -aspartate than N-tau, A-tau and F-tau. The average percentage d -aspartate for these proteins, after a correction for background, are 4.9%, 2.8%, 1.6%, and 1% for PHF-tau, N-tau, A-tau and F-tau, respectively. It remains to be determined if the increase in d -aspartate is a consequence of PHF formation. It is also unknown if the change in d -aspartate content in PHF-tau is associated with phosphorylation, which alters the susceptibility of tau to proteolysis. |
| Databáze: | OpenAIRE |
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