Abstract
AbstractBackgroundTau protein that comprises neurofibrillary tangles in Alzheimer’s Disease (AD) interact with the abundant immunophilin protein Cyclophilin A (CypA) due to its peptidyl‐prolyl cis‐trans isomerase activity.MethodUsing surface plasmon resonance (SPR), nuclear magnetic resonance (NMR) and cell culture, structural details of CypA/tau interaction and its functional consequences are characterized.ResultUsing SPR, we observed a binding equilibrium constant (KD) of full‐length tau at ∼10 µM and identified the tau binding pocket on CypA using NMR. CypA and tau uptake by microglia was measured by immunofluorescence microscopy and flow cytometry. CypA‐tau interactions within microglia cell lines affect neuroinflammation by altering proinflammatory and anti‐inflammatory cytokine secretion responses.ConclusionCypA binds to tau with high affinity and specificity, which has functional significance in tau conformation, interaction, aggregation, and in neuroinflammation.
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