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Last Updated: 2 years ago

Possible Interaction: Uridine Triacetate and Iron, Dietary

Research Papers that Mention the Interaction

Exposure of the H63D and wild type (WT) cells to iron increased tau phosphorylation, but this response was decreased significantly when cells were treated with okra.
Neuroscience Letters  •  2015  |  View Paper
BACKGROUND Abnormally hyperphosphorylated tau is a defining pathological feature of tauopathies, such as Alzheimer's disease (AD), and accumulating evidence suggests a role for iron in mediating tau pathology that may lead to cognitive decline in these conditions.
Journal of Alzheimer's disease : JAD  •  2020  |  View Paper
Prior work has shown that iron interacts with hyperphosphorylated tau , which contributes to the formation of neurofibrillary tangles (NFTs) in Alzheimer's disease (AD), whereas iron chelator desferrioxamine (DFO) slows down the clinical progression of the cognitive decline associated with this disease.
Neurochemistry International  •  2013  |  View Paper
In the current paper we have shown that iron induces an imbalance in the function of Cdk5/p25 system of hippocampal neurons, resulting in a marked decrease in tau phosphorylation at the typical Alzheimer's epitopes.
Biometals  •  2004  |  View Paper
Iron is speculated to bind to tau and induce conformational changes of the protein, potentially leading to subsequent aggregation and cognitive decline.
Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics  •  2021  |  View Paper
Iron has been shown to promote aggregation and pathogenicity of the characteristic aberrant proteins, β-amyloid, tau , α-synuclein, and TDP43, in these diseases.
Frontiers in Aging Neuroscience  •  2020  |  View Paper
Iron is also reported to induce the aggregation of hyperphosphorylated tau , possibly through a direct interaction via a putative iron binding motif in the tau protein, facilitating the formation of neurofibrillary tangles (NFTs).
Studies have demonstrated that iron can regulate tau phosphorylation by inducing the activity of multiple kinases that promote tau hyperphosphorylation and potentially also by impacting protein phosphatase 2A activity.
Front. Mol. Neurosci.  •  2018  |  View Paper