Phosphorylation and transport of neurofilament proteins in the rat spinal ganglion.

Neurofilament proteins (NFs) in rat spinal ganglia were labeled with [32P]orthophosphate injected into ganglia and analyzed by two-dimensional autoradiography and immunoblotting. Three polypeptides of NF were labeled irrespective of the extent of phosphorylation. Most of the labeled NFs were transported from cell bodies to proximal axons within 24 h. A major fraction of low phosphorylated NF-H changed to high phosphorylated form in intraganglionic nerve fibers and peripheral nerves adjacent to spinal ganglia. A small fraction of low phosphorylated NF-H appeared earlier than the high phosphorylated form in adjacent peripheral nerves, suggesting that newly synthesized NF-H in cell bodies migrate a long distance before they are extensively phosphorylated and assembled into the cytoskeleton in proximal axons.