Differential Axonal Transport of Soluble and Insoluble τ in the Rat Sciatic Nerve

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Abstract
Axonal transport of microtubule-associated protein tau was studied in the motor fibers of the rat sciatic nerve 1-4 weeks after labeling of the spinal cord with [35S]methionine. As 60-70% of low molecular weight tau in this system was found to be insoluble in 1% Triton-containing buffer, labeled proteins in 6-mm consecutive nerve segments were first separated into Triton-soluble and insoluble fractions. Two-dimensional gel electrophoresis and immunoblotting with anti-tau antibody confirmed the presence of tau among labeled, transported proteins in both fractions. Isoform composition of labeled tau was similar to that of bulk axonal tau, the most acidic species with apparent molecular mass of 66 kDa being the major component. Transport profiles obtained by measuring radioactivities associated with this major isoform showed that soluble and insoluble tau were transported at different rates. Insoluble tau, which contained the majority of tau-associated radioactivity, was transported at 1.7 mm/day in slow component a (SCa), whereas soluble tau was transported faster, at 3 mm/day, corresponding to the rate of slow component b (SCb). Cotransport of insoluble tau with insoluble tubulin in SCa suggests its association with stable microtubules.

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