Abnormal phosphorylation, aggregation and ultimately functional alteration of the main microtubule-associated protein, tau, is the major cause of neurodegenerative disorders known as tauopathies [22, 23].Tau aggregates are found in AD,Pick’s disease, corticobasal degeneration, Down’s syndrome and frontotemporal dementia with parkinsonism chromosome 17 type (FTDP-17) [24]. The most common tauopathy is AD.To analyze the role of tau modification during AD progression, human tau and a pseudohyperphosphorylated tau (PHP tau; in which ten serine/threonine residues were changed to glutamates),which mimics AD-relevant tau modification,were brought under the control of a pan neuronal (a 3.4 kb upstream of the gene F25B3.3) promoter. Transgenic worms expressing
either tau or PHP tau developed a phenotype of uncoordinated (Unc) locomotion, characteristic of a variety of C. elegans nervous system defects.
Abnormal phosphorylation, aggregation and ultimately functional alteration of the main microtubule-associated protein, tau, is the major cause of neurodegenerative disorders known as tauopathies [22, 23].Tau aggregates are found in AD,Pick’s disease, corticobasal degeneration, Down’s syndrome and frontotemporal dementia with parkinsonism chromosome 17 type (FTDP-17) [24]. The most common tauopathy is AD.To analyze the role of tau modification during AD progression, human tau and a pseudohyperphosphorylated tau (PHP tau; in which ten serine/threonine residues were changed to glutamates),which mimics AD-relevant tau modification,were brought under the control of a pan neuronal (a 3.4 kb upstream of the gene F25B3.3) promoter. Transgenic worms expressingeither tau or PHP tau developed a phenotype of uncoordinated (Unc) locomotion, characteristic of a variety of C. elegans nervous system defects.
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