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Tau PET imaging in neurodegenerative tauopathies—still a challenge

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GDW ball screw pmi linear guide for the machine. Ball Screw Repair Services and Remanufacturing Sometimes a new ball screw is the right choice depending on price and availability, but usually it is wiser to have it reconditioned, saving you money and down time. Introduction The misfolding and accumulation of proteins in the brain is a feature common to a range of neurodegenerative disorders, including a collective characterized by the accumulation of pathological tau.

Referred to as tauopathies, the accurate identification of these disorders is a challenge clinically, particularly early on in the symptomatic course, because of overlapping clinical phenotypes.

In this review, we describe and discuss in vitro and in vivo findings in the brain from investigation of various tau ligands, other biomarkers and cognitive measures, and with respect to methodological considerations tied to the quantification of tau PET. Tau deposits A phosphoprotein involved in the stabilization of microtubules, tau is natively unfolded, with six isoforms divided into two functional groups based on the number of repeats [three 3R or four 4R ] of the microtubule-binding domain [ 1 ].

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Tau is normally phosphorylated, but hyperphosphorylation weakens its binding to the microtubules and increases its cytosolic levels [ 2 ]; following a migration from axonal to somatodendritic compartments, hyperphosphorylated tau assembles into protofibrils [ 3 ].

These assemblies are classified as straight, twisted or paired helical filaments PHFs , based on the absence or periodicity of twists; they are found in neurons, astrocytes, and oligodendroglia [ 4 ].

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Tau aggregates can assume a range of ultrastructural polymorphisms on the basis of isoform predominance and post-translational modifications [ 5 , 6 , 7 , 8 , 9 ]. Although the mechanisms leading to tau pathology are as yet unclear, experimental evidence implicates abnormalities in kinase and phosphatase activity [ 10 ], as well as chronic cerebral hypoperfusion [ 11 ], in the hyperphosphorylation of tau; once hyperphosphorylated, decreased microtubule binding results in the increased release of soluble tau species [ 12 ].

Transfer of such species between cells has then been shown to occur via synaptic [ 13 , 14 ] and nonsynaptic pathways [ 12 , 15 ], resulting in seeding and the induction of tau aggregation in recipient cells.

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The accumulation of tau pathology, however, has been postulated to follow stereotypical spatiotemporal patterns. According to pathological investigations of tau at autopsy, in vivo tau PET imaging is expected to shed further light on the time course of tau accumulation in relation to other biomarkers and clinical symptomatology. The color coding and the size of the spheres distinguishes between brain areas affected at early yellow; large size , middle shades of red; mid size and late purple; small size stages of tau propagation.

The scheme for AD is adapted from Braak and Braak [ 60 ]. The scheme for PSP is adapted from Williams et al.