Abstract
(a) Axoplasmic transport of tritium-labeled proteins in crayfish nerve cord was confirmed at a slow rate of 1 mm/day. A second proteinaceous component which moves at a rate of 10 mm/day was also detected. Radioautography and biochemical analysis indicate that proteins migrating at these velocities have a perikaryal origin and move caudad within axons as sharply defined peaks. (b) Evidence is presented for the blockage of the slow and the fast movement of proteins by intraganglionic injection of the anti-mitotic agent vinblastine sulfate (0.1 mM). (c) Electron microscope observations of vinblastine-treated ganglia revealed a reduction in the number of axonal microtubules and the formation of intracellular aggregates presumably composed of microtubular protein. (d) These findings would be compatible with the involvement of microtubules in both slow and fast axoplasmic transport. However, the block induced by vinblastine was detected in regions of the cord (up to 10 mm away from the injection site) where the number and morphology of microtubules appeared unaltered. In addition, axons showing effects of vinblastine occasionally contained mitochondria with remarkably dense and thickened membranes. (e) In association with the surfaces of axonal microtubules are lateral filamentous elements (40–80 A in diameter) which also showed vinblastine-induced alterations. Our observations indicate that such filiform structures, associated with microtubules, may be a necessary component in the transport mechanism(s).
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- BENNETT H. S., LUFT J. H. zeta-Collidine as a basis for buffering fixatives. J Biophys Biochem Cytol. 1959 Aug;6(1):113–114. doi: 10.1083/jcb.6.1.113. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bensch K. G., Malawista S. E. Microtubular crystals in mammalian cells. J Cell Biol. 1969 Jan;40(1):95–107. doi: 10.1083/jcb.40.1.95. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Borisy G. G., Taylor E. W. The mechanism of action of colchicine. Binding of colchincine-3H to cellular protein. J Cell Biol. 1967 Aug;34(2):525–533. doi: 10.1083/jcb.34.2.525. [DOI] [PMC free article] [PubMed] [Google Scholar]
- CAULFIELD J. B. Effects of varying the vehicle for OsO4 in tissue fixation. J Biophys Biochem Cytol. 1957 Sep 25;3(5):827–830. doi: 10.1083/jcb.3.5.827. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Creasey W. A., Markiw M. E. Biochemical effects of the vinca alkaloids. 3. The synthesis of ribonucleic acid and the incorporation of amino acids in Ehrlich ascites cells in vitro. Biochim Biophys Acta. 1965 Aug 10;103(4):635–645. [PubMed] [Google Scholar]
- Dahlström A. Effect of colchicine on transport of amine storage granules in sympathetic nerves of rat. Eur J Pharmacol. 1968 Dec;5(1):111–113. doi: 10.1016/0014-2999(68)90165-9. [DOI] [PubMed] [Google Scholar]
- Echandia E. L., Piezzi R. S. Microtubules in the nerve fibers of the toad Bufo arenarum Hensel. Effect of low temperature on the sciatic nerve. J Cell Biol. 1968 Nov;39(2):491–497. doi: 10.1083/jcb.39.2.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fernandez H. L., Davison P. F. Axoplasmic transport in the crayfish nerve cord. Proc Natl Acad Sci U S A. 1969 Oct;64(2):512–519. doi: 10.1073/pnas.64.2.512. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fernandez H. L., Huneeus F. C., Davison P. F. Studies on the mechanism of axoplasmic transport in the crayfish cord. J Neurobiol. 1970;1(4):395–409. doi: 10.1002/neu.480010404. [DOI] [PubMed] [Google Scholar]
- Grafstein B. Axonal transport: communication between soma and synapse. Adv Biochem Psychopharmacol. 1969;1:11–25. [PubMed] [Google Scholar]
- Grafstein B., McEwen B. S., Shelanski M. L. Axonal transport of neurotubule protein. Nature. 1970 Jul 18;227(5255):289–290. doi: 10.1038/227289a0. [DOI] [PubMed] [Google Scholar]
- James K. A., Bray J. J., Morgan I. G., Austin L. The effect of colchicine on the transport of axonal protein in the chicken. Biochem J. 1970 May;117(4):767–771. doi: 10.1042/bj1170767. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Karlsson J. O., Sjöstrand J. The effect of colchicine on the axonal transport of protein in the optic nerve and tract of the rabbit. Brain Res. 1969 May;13(3):617–619. doi: 10.1016/0006-8993(69)90274-1. [DOI] [PubMed] [Google Scholar]
- Karlsson J. O., Sjöstrand J. Transport of labelled proteins in the optic nerve and tract of the rabbit. Brain Res. 1968 Nov;11(2):431–439. doi: 10.1016/0006-8993(68)90035-8. [DOI] [PubMed] [Google Scholar]
- Kreutzberg G. W. Neuronal dynamics and axonal flow. IV. Blockage of intra-axonal enzyme transport by colchicine. Proc Natl Acad Sci U S A. 1969 Mar;62(3):722–728. doi: 10.1073/pnas.62.3.722. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Krishan A., Hsu D. Observations on the association of helical polyribosomes and filaments with vincristine-induced crystals in Earle's L-cell fibroblasts. J Cell Biol. 1969 Dec;43(3):553–563. doi: 10.1083/jcb.43.3.553. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lasek R. Axoplasmic transport in cat dorsal root ganglion cells: as studied with [3-H]-L-leucine. Brain Res. 1968 Mar;7(3):360–377. doi: 10.1016/0006-8993(68)90003-6. [DOI] [PubMed] [Google Scholar]
- Malawista S. E., Sato H., Bensch K. G. Vinblastine and griseofulvin reversibly disrupt the living mitotic spindle. Science. 1968 May 17;160(3829):770–772. doi: 10.1126/science.160.3829.770. [DOI] [PubMed] [Google Scholar]
- Ochs S., Ranish N. Characteristics of the fast transport system in mammalian nerve fibers. J Neurobiol. 1969;1(2):247–261. doi: 10.1002/neu.480010211. [DOI] [PubMed] [Google Scholar]
- Ochs S., Ranish N. Metabolic dependence of fast axoplasmic transport in nerve. Science. 1970 Feb 6;167(3919):878–879. doi: 10.1126/science.167.3919.878. [DOI] [PubMed] [Google Scholar]
- Olmsted J. B., Carlson K., Klebe R., Ruddle F., Rosenbaum J. Isolation of microtubule protein from cultured mouse neuroblastoma cells. Proc Natl Acad Sci U S A. 1970 Jan;65(1):129–136. doi: 10.1073/pnas.65.1.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
- REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rosenbaum J. L., Moulder J. E., Ringo D. L. Flagellar elongation and shortening in Chlamydomonas. The use of cycloheximide and colchicine to study the synthesis and assembly of flagellar proteins. J Cell Biol. 1969 May;41(2):600–619. doi: 10.1083/jcb.41.2.600. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Sjöstrand J. Fast and slow components of axoplasmic transport in the hypoglossal and vagus nerves of the rabbit. Brain Res. 1970 Mar 17;18(3):461–467. doi: 10.1016/0006-8993(70)90129-0. [DOI] [PubMed] [Google Scholar]
- Tilney L. G., Gibbins J. R. Microtubules in the formation and development of the primary mesenchyme in Arbacia punctulata. II. An experimental analysis of their role in development and maintenance of cell shape. J Cell Biol. 1969 Apr;41(1):227–250. doi: 10.1083/jcb.41.1.227. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tilney L. G., Porter K. R. Studies on the microtubules in heliozoa. II. The effect of low temperature on these structures in the formation and maintenance of the axopodia. J Cell Biol. 1967 Jul;34(1):327–343. doi: 10.1083/jcb.34.1.327. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamada K. M., Spooner B. S., Wessells N. K. Axon growth: roles of microfilaments and microtubules. Proc Natl Acad Sci U S A. 1970 Aug;66(4):1206–1212. doi: 10.1073/pnas.66.4.1206. [DOI] [PMC free article] [PubMed] [Google Scholar]