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Fig. 1. Tau and 
-synuclein transport depends on an intact microtubule cytoskeleton. (A) Rat cortical neurons were either not treated or treated with cytochalasin B to disrupt the actin cytoskeleton or with nocodazole to depolymerise microtubules. Tubulin was visualised with antibody to -tubulin and FITC-conjugated secondary antibody (green) and actin was detected with phalloidin-TRITC (red). Merged images of tubulin and actin are shown on the right. Bar, 10 µm. (B,C) Neurons were transfected with -synuclein (B) or tau-EGFP (C) and cells were fixed at 30-minute intervals after transfection. Neurons were either not treated (
) or treated with nocodazole 3 hours after transfection (
) or cytochalasin B (
). Neurons transfected with -synuclein were immunostained for -synuclein using 90 antibody and tau was detected by direct fluorescence of EGFP. The distance travelled by the exogenous protein was measured from the perimeter of the cell body along the axon to the limit of the fluorescent front. Each point represents the mean±s.e.m. (n=60-130 measurements). Treatment with nocodazole inhibited the transport of both proteins (*P<0.01 using one-way ANOVA), whereas transport of neither of the proteins was affected by treatment with cytochalasin B (P>0.05), indicating that an intact microtubule network is essential for the transport of tau and -synuclein.
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