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Fig. 3 | Cell & Bioscience

Fig. 3

From: Microglia degrade Tau oligomers deposit via purinergic P2Y12-associated podosome and filopodia formation and induce chemotaxis

Fig. 3

P2Y12-associated podosome modulates microglial migration and invasion. A Purinergic P2Y12 receptors were colocalized with F-actin-rich podosome in lamellipodia during Tau-induced microglia migration. Similarly, the activation of P2Y12 signaling by ADP has also induced the colocalization of P2Y12 in podosome-rich microglial lamella, as seen by the IF study (scale bar 10 μm). B Fluorescence quantification of podosome-rich lamella near the membrane (box marked area) showed the colocalization of P2Y12 and F-actin at the distances of 14 μm, in Tau monomer, oligomers-exposed microglia. C, D The wound scratch assay showed that the extracellular Tau and ADP, together and separately induced the microglial migration as quantified by %wound closure at 24 h. The blockage of P2Y12 signaling by Clopidogrel has reduced the microglial migration. But, Tau oligomers restored the microglial migration even upon clopidogrel-induced blockage, as observed and quantified by phase contrast imaging. (No. of experiment = 3) (n = 12) (Scale bar 100 μm). E, F In trans-well migration assay, Tau oligomers have induced the microglial invasion more than Tau monomer treatment. P2Y12 activation by ADP has induced microglial trans-migration in both Tau monomer and oligomers exposure. The quantification of microscopic images revealed that Clopidogrel exposure has significantly reduced the microglial invasion, which was eventually restored by Tau oligomers exposure. These emphasize that Tau oligomers were better chemoattractants and can intervene P2Y12 signaling during migration/invasion. (No. of experiment = 2) (n = 12) (scale bar 100 μm)

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