Phosphorylation-dependent immunoreactivity of neurofilaments and the rate of slow axonal transport in the central and peripheral axons of the rat dorsal root ganglion

• Published in: Journal of neurochemistry Vol. 62; no. 3; p. 1119
• Main Authors: Archer, D R, Watson, D F, Griffin, J W
• Format: Journal Article
• Language: English
• Published: England 01.03.1994
• Subjects: Animals; Axons - metabolism; Biological Transport; Cytoskeletal Proteins - metabolism; Enzyme-Linked Immunosorbent Assay; Ganglia, Spinal - metabolism; Ganglia, Spinal - ultrastructure; Male; Neurofilament Proteins - metabolism; Phosphorylation; Rats; Rats, Sprague-Dawley
• ISSN: 0022-3042
• DOI: 10.1046/j.1471-4159.1994.62031119.x

The rate of axonal transport of tubulin, actin, and the neurofilament proteins was measured in the peripheral and central projections of the rat L5 dorsal root ganglion (DRG). [35S]Methionine was injected into the DRG, and the "front" of the radiolabeled protein was located 7, 14, and 20 days postinjection. Transport rates calculated for the neurofilament triplet proteins, tubulin, and actin in the peripheral nerve were approximately 1.5-fold faster than those in the dorsal root. A progressive decrease in the rate of transport was observed from 7 to 20 days after radiolabeling in both the central and peripheral directions (neurofilaments, approximately 1.7-fold; tubulin/actin, 2.1-fold). A surgical preparation, leaving the peripheral sciatic nerve with predominantly sensory fibers, was the basis for ELISAs for phosphorylation-dependent immunoreactivity of the high-molecular-weight neurofilament protein. In both dorsal roots and peripheral sensory axons the degree of phosphorylation was greater in nerve segments further away from the cell bodies. The degree of phosphorylation-related immunoreactivity correlates with the slowing of transport of radiolabeled cytoskeletal protein.