The tau proteins (abbreviated from tubulin associated unit[5]) form a group of six highly soluble protein isoforms produced by alternative splicing from the gene MAPT (microtubule-associated protein tau).[6][7] They have roles primarily in maintaining the stability of microtubules in axons and are abundant in the neurons of the central nervous system (CNS), where the cerebral cortex has the highest abundance.[8] They are less common elsewhere but are also expressed at very low levels in CNS astrocytes and oligodendrocytes.[9]
Pathologies and dementias of the nervous system such as Alzheimer's disease and Parkinson's disease[10] are associated with tau proteins that have become hyperphosphorylated insoluble aggregates called neurofibrillary tangles. The tau proteins were identified in 1975 as heat-stable proteins essential for microtubule assembly,[5][11] and since then they have been characterized as intrinsically disordered proteins.[12]
Neurons were grown in tissue culture and stained with antibody to MAP2 protein in green and MAP tau in red using the immunofluorescence technique. MAP2 is found only in dendrites and perikarya, while tau is found not only in the dendrites and perikarya but also in axons. As a result, axons appear red while the dendrites and perikarya appear yellow, due to superimposition of the red and green signals. DNA is shown in blue using the DAPI stain which highlights the nuclei. Image courtesy EnCor Biotechnology Inc.
^ abcGRCm38: Ensembl release 89: ENSMUSG00000018411 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ abWeingarten MD, Lockwood AH, Hwo SY, Kirschner MW (May 1975). "A protein factor essential for microtubule assembly". Proceedings of the National Academy of Sciences of the United States of America. 72 (5): 1858–62. Bibcode:1975PNAS...72.1858W. doi:10.1073/pnas.72.5.1858. PMC 432646. PMID 1057175.
^Goedert M, Wischik CM, Crowther RA, Walker JE, Klug A (June 1988). "Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau". Proceedings of the National Academy of Sciences of the United States of America. 85 (11): 4051–5. Bibcode:1988PNAS...85.4051G. doi:10.1073/pnas.85.11.4051. PMC 280359. PMID 3131773.
^Goedert M, Spillantini MG, Jakes R, Rutherford D, Crowther RA (October 1989). "Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease". Neuron. 3 (4): 519–26. doi:10.1016/0896-6273(89)90210-9. PMID 2484340. S2CID 19627629.
^Sjölin, Karl; Kultima, Kim; Larsson, Anders; Freyhult, Eva; Zjukovskaja, Christina; Alkass, Kanar; Burman, Joachim (December 2022). "Distribution of five clinically important neuroglial proteins in the human brain". Molecular Brain. 15 (1): 52. doi:10.1186/s13041-022-00935-6. ISSN 1756-6606. PMC 9241296. PMID 35765081.
^Shin RW, Iwaki T, Kitamoto T, Tateishi J (May 1991). "Hydrated autoclave pretreatment enhances tau immunoreactivity in formalin-fixed normal and Alzheimer's disease brain tissues". Laboratory Investigation; A Journal of Technical Methods and Pathology. 64 (5): 693–702. PMID 1903170.
^Lei P, Ayton S, Finkelstein DI, Adlard PA, Masters CL, Bush AI (November 2010). "Tau protein: relevance to Parkinson's disease". The International Journal of Biochemistry & Cell Biology. 42 (11): 1775–8. doi:10.1016/j.biocel.2010.07.016. PMID 20678581.
^Cleveland DW, Hwo SY, Kirschner MW (October 1977). "Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin". Journal of Molecular Biology. 116 (2): 207–25. doi:10.1016/0022-2836(77)90213-3. PMID 599557.
^Cleveland DW, Hwo SY, Kirschner MW (October 1977). "Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly". Journal of Molecular Biology. 116 (2): 227–47. doi:10.1016/0022-2836(77)90214-5. PMID 146092.
The tauproteins (abbreviated from tubulin associated unit) form a group of six highly soluble protein isoforms produced by alternative splicing from the...
diseases characterized by the aggregation of abnormal tauprotein. Hyperphosphorylation of tauproteins causes them to dissociate from microtubules and form...
Neurofibrillary tangles (NFTs) are intracellular aggregates of hyperphosphorylated tauprotein that are most commonly known as a primary biomarker of Alzheimer's disease...
of tauprotein depends on its phosphorylated state. In Alzheimer's disease, due to misfoldings and abnormal conformational changes in tauprotein structure...
interval in pharmacokinetics The core variable in general tau theory Tau in biochemistry, a protein associated with microtubules and implicated in neurodegenerative...
cause of the condition is uncertain, but involves the accumulation of tauprotein within the brain. Medications such as levodopa and amantadine may be...
with a molecular weight below 55-62 kDa, and are called τ (tau) proteins. In-vitro, tauproteins have been shown to directly bind microtubules, promote nucleation...
([pref. protein]; -pathy [suff. disease]; proteinopathies pl.; proteinopathic adj), or proteopathy, protein conformational disorder, or protein misfolding...
The oligomers are toxic to nerve cells. The other protein implicated in Alzheimer's disease, tauprotein, also forms such prion-like misfolded oligomers...
proteinopathies that are found in FTLD include the accumulation of tauproteins and TAR DNA-binding protein 43 (TDP-43). Mutations in the C9orf72 gene have been established...
believed due to the most common indicator of CBD being a faulty tauprotein. Tauproteins are integral in keeping microtubules stable; defective cells create...
compromised causing the neurons to degrade over time. In Alzheimer's disease, tauproteins which stabilize microtubules malfunction in the progression of the illness...
accumulations of tauprotein in Webster's brain, which affect mood, emotions, and executive functions similar to the way that clumps of beta-amyloid protein contribute...
been proposed that mTOR contributes to tau pathology by increasing the translation of tau and other proteins. Synaptic plasticity is a key contributor...
such techniques can be validated. PET tracers that bind specifically to tauprotein are desired to aid diagnosis of CTE in living individuals. One candidate...
neurons were also immunostained with an antibody for phosphorylated Tauprotein. Activated PKR was specifically found in the cytoplasm and nucleus, as...
plaques, along with neurofibrillary tangles consisting of aggregated tauprotein, are the two lesions that are required for the neuropathological diagnosis...
Global Information
