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Journal of Neuroscience, Vol 7, 453-462, Copyright © 1987 by Society for Neuroscience
Cytotypic differences in the protein composition of the axonally transported cytoskeleton in mammalian neurons
MM Oblinger, ST Brady, IG McQuarrie and RJ Lasek
Many of the structural and functional differences between axons are thought
to reflect underlying differences in the biochemical composition and
dynamic aspects of the axonal cytoskeleton and cytomatrix. In this study we
investigated how the composition of the 2 slow components of axonal
transport, SCa and SCb, which convey the cytoskeleton and cytomatrix,
differs in axons that are structurally and functionally distinct. For this
comparison we analyzed axons of retinal ganglion cells in the optic nerve
(ON), axons of dorsal root ganglion (DRG) cells, and axons of ventral motor
neurons (VMN) in adult rats. 35S-Methionine-labeled proteins transported
with the peak of SCa and SCb were analyzed using high-resolution
2-dimensional polyacrylamide gels (2D-PAGE) and fluorography, and the
amounts of major SCa and SCb proteins were quantified. The polypeptide
composition of both SCa and SCb was found to be largely similar in DRG and
VMN axons, but major qualitative as well as quantitative differences
between these axons and ON axons were found. Notable among these were
higher ratios of neurofilament protein to tubulin in SCa in DRG and VMN
axons compared to ON axons, and significantly larger amounts of 2
microtubule- associated proteins relative to tubulin in SCa of ON axons
than in both VMN and DRG axons. Tubulin was the major SCb protein in VMN
and DRG axons, but it was not present in SCb in ON axons. Additionally,
relatively larger amounts of 2 metabolic enzymes, creatine phosphokinase
and nerve-specific enolase, were present in SCb in ON axons than in DRG or
VMN axons. The results indicate that significant biochemical heterogeneity
among different types of axons can be identified by examining the slow
components of axonal transport.
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