![]() ![]() Scientists have long pointed to the importance of tau in AD because of evidence linking the spread of tau with disease progression. They are found in brains that are developing AD decades before the disease blossoms clinically. The smaller forms of tau circulate among the neurons, interfering with cellular function. Instead, the fabric of connected tau proteins comes apart and reassembles in a disorganized, messy tangle that accumulates in brain cells and is not effectively disposed of through the cell’s usual ways of removing “trash.” Besides the microtubular form, which is composed of many tau molecules, tau also exists in smaller versions, called oligomers, which are made up of a few tau proteins. This form of tau no longer sticks together in the same way. ![]() No longer fit to carry out its usual job, it takes on characteristics that are potentially very damaging. These chemical alterations of tau change its properties. Then, after tau has been created from DNA, chemical activities in the brain further modify it in several ways. ![]() The other diseases mentioned feature variants of tau protein created by splicing together tau’s smaller components in different patterns to create the six different human forms. A genetically mutant form of tau can wreak havoc and does so in FTDP-17. The abnormal tau proteins found in these neurodegenerative diseases are not identical, although they are related. Although each of these forms of dementia are different, they are all severe and progressive. Some other serious brain diseases associated with abnormal tau protein are chronic traumatic encephalopathy, Pick disease, frontotemporal dementia with parkinsonism-17 (FTDP-17), progressive supranuclear Palsy (PSP), and corticobasal degeneration (CBD). Video courtesy of the National Institute on Aging/National Institutes of Health Brain Diseases Associated with TauĪlzheimer’s disease is well known to feature neurofibrillary tangles that are composed of modified tau protein. ![]()
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