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000277807 1001_ $$0P:(DE-2719)9001954$$aFischer, Anna-Lisa$$b0$$eFirst author
000277807 245__ $$aAlpha-Synuclein Demonstrates Varying Binding Affinities With Different Tau Isoforms.
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000277807 520__ $$aThe hallmark of various neurodegenerative diseases is the accumulation and aggregation of amyloidogenic proteins, such as amyloid-beta (Aβ) and tau in Alzheimer's disease (AD) and alpha-synuclein (aSyn) in synucleinopathies. Many neurodegenerative diseases express mixed pathology. For instance, Lewy bodies are reported in tauopathies and neurofibrillary tau-tangles are detected in synucleinopathies, suggesting a potential co-existence or crosstalk of misfolded aSyn and tau. In the present study, we investigated the binding characteristics of monomeric aSyn with different tau isoforms by using surface plasmon resonance (SPR) spectroscopy allowing monitoring direct protein-protein interactions and their potential co-localization using SH-SY5Y cells. The calculation of the binding parameters (association and dissociation rate constants) indicated the strongest binding affinity between aSyn and tau isoform 1N3R followed by tau 2N3R and tau 2N4R. Co-localization studies in SH-SY5Y cells, treated with aSyn and all six tau isoforms revealed an intracellular co-localization of aSyn with different isoforms of tau. Subcellular fractionation confirmed the cellular uptake and colocalization of tau and aSyn in the same compartment, showing their expression in membrane, nuclear, and cytoskeletal fractions. Understanding the intricate interplay between aSyn and tau is crucial for unraveling the pathophysiology of PD, AD, and related neurodegenerative disorders, ultimately paving the way for the development of effective treatments targeting this interaction. In conclusion, our data indicate that aSyn and tau are direct interaction partners with varying binding affinities depending on the tau isoform. This interaction may be significant for understanding the pathophysiology of dementia with mixed pathologies.
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000277807 650_7 $$2Other$$aAlzheimer's disease
000277807 650_7 $$2Other$$aParkinson's disease
000277807 650_7 $$2Other$$aalpha‐synuclein
000277807 650_7 $$2Other$$ainteraction
000277807 650_7 $$2Other$$asynucleinopathies
000277807 650_7 $$2Other$$atau
000277807 650_7 $$2Other$$atauopathies
000277807 650_7 $$2NLM Chemicals$$atau Proteins
000277807 650_7 $$2NLM Chemicals$$aalpha-Synuclein
000277807 650_7 $$2NLM Chemicals$$aProtein Isoforms
000277807 650_2 $$2MeSH$$aHumans
000277807 650_2 $$2MeSH$$atau Proteins: metabolism
000277807 650_2 $$2MeSH$$aalpha-Synuclein: metabolism
000277807 650_2 $$2MeSH$$aProtein Isoforms: metabolism
000277807 650_2 $$2MeSH$$aProtein Binding: physiology
000277807 650_2 $$2MeSH$$aCell Line, Tumor
000277807 650_2 $$2MeSH$$aSurface Plasmon Resonance
000277807 7001_ $$0P:(DE-2719)9000287$$aSchmitz, Matthias$$b1$$udzne
000277807 7001_ $$0P:(DE-2719)9000851$$aThom, Tobias$$b2
000277807 7001_ $$0P:(DE-2719)9000358$$aZafar, Saima$$b3$$udzne
000277807 7001_ $$0P:(DE-2719)9001558$$aYounas, Neelam$$b4
000277807 7001_ $$0P:(DE-2719)9000766$$ada Silva Correia, Susana$$b5$$udzne
000277807 7001_ $$0P:(DE-2719)9000766$$aSilva-Correia, Susana$$b6$$udzne
000277807 7001_ $$0P:(DE-2719)9001944$$aCanaslan, Sezgi$$b7
000277807 7001_ $$0P:(DE-2719)2000058$$aZerr, Inga$$b8$$eLast author$$udzne
000277807 773__ $$0PERI:(DE-600)2020528-4$$a10.1111/jnc.70053$$gVol. 169, no. 4, p. e70053$$n4$$pe70053$$tJournal of neurochemistry$$v169$$x0022-3042$$y2025
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