Developmental changes in tau phosphorylation: fetal tau is transiently phosphorylated in a manner similar to paired helical filament-tau characteristic of Alzheimer's disease
| Autor: | A M Couck, Carthage J. Smith, Brian H. Anderton, Jean Pierre Brion, Jean-Marc Gallo |
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| Rok vydání: | 1993 |
| Předmět: |
Gene isoform
Adult Pathology medicine.medical_specialty medicine.drug_class Tau protein Blotting Western tau Proteins Biology Monoclonal antibody Biochemistry Epitope Cellular and Molecular Neuroscience Phosphoserine Degenerative disease Fetus Alzheimer Disease Reference Values mental disorders medicine Serine Animals Humans Amino Acid Sequence Phosphorylation Gel electrophoresis Brain medicine.disease Cell biology Rats biology.protein Electrophoresis Polyacrylamide Gel Alzheimer's disease |
| Zdroj: | Journal of neurochemistry. 61(6) |
| ISSN: | 0022-3042 |
| Popis: | Rat and human fetal brain tau were probed with a panel of monoclonal antibodies (tau-1, AT8, 8D8, RT97, SMI31, SMI34) that distinguish between paired helical filament (PHF)-tau of Alzheimer's disease and normal adult brain tau. These antibodies discriminate between normal and PHF-tau because their epitopes are phosphorylated in PHF-tau. Although only one molecular isoform of tau was shown to be expressed in fetal brain, two fetal tau species could be distinguished on sodium dodecyl sulfate-polyacrylamide gel electrophoresis and the slower migrating species was recognized by all of the PHF-tau-specific antibodies. Moreover, this immunoreactivity was shown to be phosphorylation dependent. Our observations suggest that the abnormal phosphorylation of tau in Alzheimer's disease may be the result of reactivation of pathways governing the phosphorylation of tau in the developing brain. |
| Databáze: | OpenAIRE |
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