tau protein

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Related to Tau proteins: Neurofibrillary tangles

tau protein

microtubule-associated protein that accumulates in neurons in neurofibrillary degeneration in a wide variety of disorders including Alzheimer disease; gene for tau protein situated on chromosome 17; normal role for tau protein is to stabilize microtubules; abnormal phosphorylation of tau protein destabilizes microtubules, which causes degenerative change.

tau protein

n.
Any of several proteins that act to stabilize neuronal microtubules in the axons of brain neurons and that form abnormal tangles in the brains of people with certain neurodegenerative disorders.

tau protein

A major structural protein associated with the microtubules that form the cytoskeleton of nerve cells. An abnormal form with a shorter molecule is found in the helical filaments in senile neural plaques and in the insoluble neurofibrillary tangles of ALZHEIMER'S DISEASE. It is found in the cerebrospinal fluid of people with DEMENTIA but is present in higher concentration in Alzheimer's disease than in other forms of dementia. Abnormal tau protein binds strongly to the normal protein and the latter then become shortened by nerve cell proteolytic enzymes into the abnormal form. The latter is not split by these enzymes. It was reported in 2005 that when expression of a mutant tau gene in mice was turned off with doxycycline, lost memory was recovered to a surprising degree in spite of the presence of extensive neurofibrillary tangles.
References in periodicals archive ?
Abnormal amounts of amyloid-[eth] and tau proteins are biomarkers of AD, and deposits of amyloid proteins in the brain begin many years prior to symptoms of the disease.
Study Selection: Literature search was based on the following keywords: Alzheimer's disease, tau protein, biomarker, cerebrospinal fluid (CSF), therapeutics, plasma, imaging, propagation, spreading, seeding, prion, conformational templating, and posttranslational modification.
Both neurodegenerative diseases and Alzheimer's disease may be diagnosed by clinical symptoms, medical imaging scanning and biomarkers, such us the accumulation of beta-amyloid plaques in the brain or of tau proteins (12).
"Early detection of tau proteins may help us understand what is happening sooner in the brains of these injured athletes," Small told Laboratory Equipment.
The low CSF concentrations of tau in healthy individuals and many diseased patients require advanced techniques in sample preparation and analysis, such as the use of immunoaffinity enrichment for concentrations of tau protein, as well as the use of robust ultraperformance LC microflow LC-MS/MS to enable measurements of low-abundance peptides.
At present, the analysis of tau proteins, one of the most active areas of Alzheimer's research, often requires the use of hundreds of animals and can produce results that may not translate beneficially to humans.
The Tau protein forms chains with other Tau proteins.
Recent studies show that the combination of ApoE genotyping with the measurement of A[beta] and tau proteins in the cerebrospinal fluid (CSF) may have a sensitivity for AD detection of 96.4%.
In healthy neurons, Tau proteins are well-known for their involvement in the outgrowth of neural processes, axonal transport, development of neuronal polarity, and maintenance of normal neuron morphology [14-16], whereas many neurodegenerative diseases are characterized by Tau hyperphosphorylation, Tau (mis)localisation in neurons, and, consequently, the development of neurofibrillary tangles [17].
The double-stain fluorescent method also demonstrated that HIgs held antagonistic effects on Ab-caused toxicity among nerve cells Through the exploration of the mechanism of HIgs' antagonistic effects on Ab-caused toxicity among nerve cells, it was found that HIg inhibited the cleavage of P35 to P25, prevented the over- activation of CDK5, and lowered the over- phosphorylation of tau proteins in the cytoskeletons of cerebral cells, thus avoiding the damages in cerebral nerve cells.
Josephs and his colleagues looked at the gross structure of the brain with volumetric MR imaging rather than by imaging amyloid-beta or tau proteins.