Truncated tau protein as a new marker for Alzheimer's disease.
Molecular analysis of histological hallmarks (neurofibrillary tangles, neuritic plaques, neuropil threads and dystrophic neurites) of Alzheimer diseased brain tissues showed that these lesions contain paired helical filaments. Their major constituent is microtubule associated protein tau that is in an abnormally hyperphosphorylated and truncated state. These diseased forms of tau protein are unable to promote full microtubule assembly. Understanding of the molecular basis of the processes leading to the modifications of tau proteins and paired helical filament formation will form a firm step toward rational drug development and the cure of the Alzheimer's disease.
Novák
M
M
Department of Molecular Neurobiology and Immunology, Slovak Academy of Sciences, Bratislava.
D000368:Aged; D000544:Alzheimer Disease / Q000378:metabolism / Q000473:pathology*; D000595:Amino Acid Sequence; D016564:Amyloid beta-Protein Precursor / Q000096:biosynthesis; D015415:Biomarkers / Q000032:analysis; D001921:Brain / Q000378:metabolism / Q000473:pathology*; D006801:Humans; D008969:Molecular Sequence Data; D016501:Neurites / Q000473:pathology; D016874:Neurofibrillary Tangles / Q000473:pathology; D010766:Phosphorylation; D017386:Sequence Homology, Amino Acid; D016875:tau Proteins / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism
D016564:Amyloid beta-Protein Precursor; D015415:Biomarkers; D016875:tau Proteins