Could New Alzheimer’s Marker p-Tau212 Rival p-Tau217?
In preliminary studies in five cohorts, the two markers have similar diagnostic accuracy, and stain tangles in postmortem brain equally well.
In preliminary studies in five cohorts, the two markers have similar diagnostic accuracy, and stain tangles in postmortem brain equally well.
Two studies describe how small peptides that latch onto tau have an outsize impact on fibrillization of the protein. Both point to therapeutic strategies.
Preclinical studies and early phase trials target microglial receptors CD33 and TREM2, and amyloid-stoking ASC specks.
Reactive astrocytes spell trouble for synapses, while microglial transform from protective to destructive as disease progresses.
The addition of SUMO2 to tau prevents its phosphorylation and aggregation, preserving synapses and memory in tauopathy mouse models.
An antibody against the inhibitory receptor LILRB4 prevented its binding to ApoE. The upshot? Microglia engulfed more Aβ fibrils and plaque load fell.
Two antibodies—one against the phosphoprotein, the other to tau’s N-terminus—restored proteostasis in the brain.
At AD/PD, scientists presented small molecules that break up fibrils and antibodies that target pathogenic forms of α-synuclein or hinder spread in iPSCs and mice.
Plasma p-Tau217 has enjoyed the spotlight as the best fluid biomarker for diagnosing AD, but it may have to make room for a new contender. The closely related phospho-tau, 212, identified AD patients with equal accuracy as p-Tau217 in five small cohorts. Like p-Tau217, p-Tau212 works as well in blood as in CSF. While the two markers mostly occur together, a few AD patients had only one or the other, hinting that combining the p-Taus could bring additive diagnostic value.
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