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Journal articles on the topic 'Fast axonal transport'

Author: Grafiati

Published: 4 June 2021

Last updated: 6 February 2022

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1

Miller, Kyle E., and Michael P. Sheetz. "Direct evidence for coherent low velocity axonal transport of mitochondria." Journal of Cell Biology 173, no. 3 (May 8, 2006): 373–81. http://dx.doi.org/10.1083/jcb.200510097.

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Axonal growth depends on axonal transport. We report the first global analysis of mitochondrial transport during axonal growth and pauses. In the proximal axon, we found that docked mitochondria attached to the cytoskeletal framework that were stationary relative to the substrate and fast axonal transport fully accounted for mitochondrial transport. In the distal axon, we found both fast mitochondrial transport and a coherent slow transport of the mitochondria docked to the axonal framework (low velocity transport [LVT]). LVT was distinct from previously described transport processes; it was coupled with stretching of the axonal framework and, surprisingly, was independent of growth cone advance. Fast mitochondrial transport decreased and LVT increased in a proximodistal gradient along the axon, but together they generated a constant mitochondrial flux. These findings suggest that the viscoelastic stretching/creep of axons caused by tension exerted by the growth cone, with or without advance, is seen as LVT that is followed by compensatory intercalated addition of new mitochondria by fast axonal transport.

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2

Brady, S. T. "Molecular motors and fast axonal transport." Proceedings, annual meeting, Electron Microscopy Society of America 52 (1994): 22–23. http://dx.doi.org/10.1017/s0424820100167846.

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When video microscopy was first used to study fast axonal transport in isolated axoplasm from squid giant axons, a torrent of membrane traffic was seen to move in both directions. Images of membrane bounded organelles (MBOs) moving along individual microtubules (MTs) in axoplasm opened the way for characterization of the microscopic properties of fast axonal transport and led to the characterization of two molecular motors involved in fast axonal transport. The pharmacology of MBO movement ruled out previously identified molecular motors and a biochemical dissection of fast axonal transport in axoplasm demonstrated the existence of a new class of molecular motors. Subsequently, the polypeptides comprising a new class of molecular motor, kinesin, were discovered initiating a new era in the study of molecular motors and intracellular motility.The effects of ATP analogues on fast axonal transport led to dicovery of kinesin. When the nonhydrolyzable ATP analogue, adenylyl 5′-imidodiphosphate (AMP-PNP), was perfused into isolated axoplasm, all MBOs moving in both anterograde and retrograde directions stopped moving and remained attached to MTs. Unlike the effects of AMP-PNP on myosin and dynein, inhibition by AMP-PNP was rapid even in the presence of equimolar ATP, but was reversed by excess ATP.

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3

Daniel, Gina R., Patricia J. Sollars, Gary E. Pickard, and Gregory A. Smith. "Pseudorabies Virus Fast Axonal Transport Occurs by a pUS9-Independent Mechanism." Journal of Virology 89, no. 15 (May 20, 2015): 8088–91. http://dx.doi.org/10.1128/jvi.00771-15.

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Reactivation from latency results in transmission of neurotropic herpesviruses from the nervous system to body surfaces, referred to as anterograde axonal trafficking. The virus-encoded protein pUS9 promotes axonal dissemination by sorting virus particles into axons, but whether it is also an effector of fast axonal transport within axons is unknown. To determine the role of pUS9 in anterograde trafficking, we analyzed the axonal transport of pseudorabies virus in the presence and absence of pUS9.

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4

Brown, Anthony. "Axonal transport of membranous and nonmembranous cargoes." Journal of Cell Biology 160, no. 6 (March 17, 2003): 817–21. http://dx.doi.org/10.1083/jcb.200212017.

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Membranous and nonmembranous cargoes are transported along axons in the fast and slow components of axonal transport, respectively. Recent observations on the movement of cytoskeletal polymers in axons suggest that slow axonal transport is generated by fast motors and that the slow rate is due to rapid movements interrupted by prolonged pauses. This supports a unified perspective for fast and slow axonal transport based on rapid movements of diverse cargo structures that differ in the proportion of the time that they spend moving. A Flash feature accompanies this Mini-Review.

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5

Schroer, Trina A. "Motors for fast axonal transport." Current Opinion in Neurobiology 2, no. 5 (October 1992): 618–21. http://dx.doi.org/10.1016/0959-4388(92)90028-j.

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6

Dahlström, Annica B., Andrew J. Czernik, and Jia-Yi Li. "Organelles in fast axonal transport." Molecular Neurobiology 6, no. 2-3 (June 1992): 157–77. http://dx.doi.org/10.1007/bf02780550.

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7

Schroer, Trina A. "Motors for fast axonal transport." Current Biology 2, no. 11 (November 1992): 600. http://dx.doi.org/10.1016/0960-9822(92)90167-9.

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8

Martinat, Cécile, Nadine Jarousse, Marie-Christine Prévost, and Michel Brahic. "The GDVII Strain of Theiler’s Virus Spreads via Axonal Transport." Journal of Virology 73, no. 7 (July 1, 1999): 6093–98. http://dx.doi.org/10.1128/jvi.73.7.6093-6098.1999.

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ABSTRACT Following intracerebral inoculation, the DA strain of Theiler’s virus sequentially infects neurons in the gray matter and glial cells in the white matter of the spinal cord. It persists in the latter throughout the life of the animal. Several observations suggest that the virus spreads from the gray to the white matter by axonal transport. In contrast, the neurovirulent GDVII strain causes a fatal encephalitis with lytic infection of neurons. It does not infect the white matter of the spinal cord efficiently and does not persist in survivors. The inability of this virus to infect the white matter could be due to a defect in axonal transport. Using footpad inoculations, we showed that the GDVII strain is, in fact, transported in axons. Transport was prevented by sectioning the sciatic nerve. The kinetics of transport and experiments using colchicine suggested that the virus uses microtubule-associated fast axonal transport. Our results show that a cardiovirus can spread by fast axonal transport and suggest that the inability of the GDVII strain to infect the white matter is not due to a defect in axonal transport.

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9

Hurd, Daryl D., and William M. Saxton. "Kinesin Mutations Cause Motor Neuron Disease Phenotypes by Disrupting Fast Axonal Transport in Drosophila." Genetics 144, no. 3 (November 1, 1996): 1075–85. http://dx.doi.org/10.1093/genetics/144.3.1075.

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Abstract Previous work has shown that mutation of the gene that encodes the microtubule motor subunit kinesin heavy chain (Khc) in Drosophila inhibits neuronal sodium channel activity, action potentials and neurotransmitter secretion. These physiological defects cause progressive distal paralysis in larvae. To identify the cellular defects that cause these phenotypes, larval nerves were studied by light and electron microscopy. The axons of Khc mutants develop dramatic focal swellings along their lengths. The swellings are packed with fast axonal transport cargoes including vesicles, synaptic membrane proteins, mitochondria and prelysosomal organelles, but not with slow axonal transport cargoes such as cytoskeletal elements. Khc mutations also impair the development of larval motor axon terminals, causing dystrophic morphology and marked reductions in synaptic bouton numbers. These observations suggest that as the concentration of maternally provided wild-type KHC decreases, axonal organelles transported by kinesin periodically stall. This causes organelle jams that disrupt retrograde as well as anterograde fast axonal transport, leading to defective action potentials, dystrophic terminals, reduced transmitter secretion and progressive distal paralysis. These phenotypes parallel the pathologies of some vertebrate motor neuron diseases, including some forms of amyotrophic lateral sclerosis (ALS), and suggest that impaired fast axonal transport is a key element in those diseases.

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10

Hammerschlag, Richard, Franci A. Bolen, and George C. Stone. "Metalloendoprotease Inhibitors Block Fast Axonal Transport." Journal of Neurochemistry 52, no. 1 (January 1989): 268–73. http://dx.doi.org/10.1111/j.1471-4159.1989.tb10927.x.

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11

Blum, J. J., and M. C. Reed. "A model for fast axonal transport." Cell Motility 5, no. 6 (1985): 507–27. http://dx.doi.org/10.1002/cm.970050607.

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12

Bray, Dennis. "Cell motility: Fast axonal transport dissected." Nature 315, no. 6016 (May 1985): 178–79. http://dx.doi.org/10.1038/315178b0.

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13

Carmichael, Stephen W., and W. Stephen Brimijoin. "Looking at Slow Axonal Transport." Microscopy Today 4, no. 9 (November 1996): 3–5. http://dx.doi.org/10.1017/s1551929500065299.

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Neurons are about as polarized as cells ever get. Their axonal process can extend a distance that is up to a million times the diameter of the nerve cell body. Axons have none of the ribosomal machinery responsible for protein synthesis, so all neuronal proteins and peptides must be manufactured near the nucleus and carried out to the periphery. This distribution involves at least two distinct mechanisms, fast axonal transport, moving at almost 500 mm per day, and slow axonal transport, moving only 0.1 to 3 mm per day. It turns out that proteins of the neuronal cytoskeleton, along with many soluble cytosolic proteins, are transported exclusively by the slower process.

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14

Xia, Chun-Hong, Elizabeth A. Roberts, Lu-Shiun Her, Xinran Liu, David S. Williams, Don W. Cleveland, and Lawrence S. B. Goldstein. "Abnormal neurofilament transport caused by targeted disruption of neuronal kinesin heavy chain KIF5A." Journal of Cell Biology 161, no. 1 (April 7, 2003): 55–66. http://dx.doi.org/10.1083/jcb.200301026.

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To test the hypothesis that fast anterograde molecular motor proteins power the slow axonal transport of neurofilaments (NFs), we used homologous recombination to generate mice lacking the neuronal-specific conventional kinesin heavy chain, KIF5A. Because null KIF5A mutants die immediately after birth, a synapsin-promoted Cre-recombinase transgene was used to direct inactivation of KIF5A in neurons postnatally. Three fourths of such mutant mice exhibited seizures and death at around 3 wk of age; the remaining animals survived to 3 mo or longer. In young mutant animals, fast axonal transport appeared to be intact, but NF-H, as well as NF-M and NF-L, accumulated in the cell bodies of peripheral sensory neurons accompanied by a reduction in sensory axon caliber. Older animals also developed age-dependent sensory neuron degeneration, an accumulation of NF subunits in cell bodies and a reduction in axons, loss of large caliber axons, and hind limb paralysis. These data support the hypothesis that a conventional kinesin plays a role in the microtubule-dependent slow axonal transport of at least one cargo, the NF proteins.

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15

Kaether, Christoph, Paul Skehel, and Carlos G. Dotti. "Axonal Membrane Proteins Are Transported in Distinct Carriers: A Two-Color Video Microscopy Study in Cultured Hippocampal Neurons." Molecular Biology of the Cell 11, no. 4 (April 2000): 1213–24. http://dx.doi.org/10.1091/mbc.11.4.1213.

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Neurons transport newly synthesized membrane proteins along axons by microtubule-mediated fast axonal transport. Membrane proteins destined for different axonal subdomains are thought to be transported in different transport carriers. To analyze this differential transport in living neurons, we tagged the amyloid precursor protein (APP) and synaptophysin (p38) with green fluorescent protein (GFP) variants. The resulting fusion proteins, APP-yellow fluorescent protein (YFP), p38-enhanced GFP, and p38-enhanced cyan fluorescent protein, were expressed in hippocampal neurons, and the cells were imaged by video microscopy. APP-YFP was transported in elongated tubules that moved extremely fast (on average 4.5 μm/s) and over long distances. In contrast, p38-enhanced GFP-transporting structures were more vesicular and moved four times slower (0.9 μm/s) and over shorter distances only. Two-color video microscopy showed that the two proteins were sorted to different carriers that moved with different characteristics along axons of doubly transfected neurons. Antisense treatment using oligonucleotides against the kinesin heavy chain slowed down the long, continuous movement of APP-YFP tubules and increased frequency of directional changes. These results demonstrate for the first time directly the sorting and transport of two axonal membrane proteins into different carriers. Moreover, the extremely fast-moving tubules represent a previously unidentified type of axonal carrier.

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16

Brown, Anthony, Lei Wang, and Peter Jung. "Stochastic Simulation of Neurofilament Transport in Axons: The “Stop-and-Go” Hypothesis." Molecular Biology of the Cell 16, no. 9 (September 2005): 4243–55. http://dx.doi.org/10.1091/mbc.e05-02-0141.

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According to the “stop-and-go” hypothesis of slow axonal transport, cytoskeletal and cytosolic proteins are transported along axons at fast rates but the average velocity is slow because the movements are infrequent and bidirectional. To test whether this hypothesis can explain the kinetics of slow axonal transport in vivo, we have developed a stochastic model of neurofilament transport in axons. We propose that neurofilaments move in both anterograde and retrograde directions along cytoskeletal tracks, alternating between short bouts of rapid movement and short “on-track” pauses, and that they can also temporarily disengage from these tracks, resulting in more prolonged “off-track” pauses. We derive the kinetic parameters of the model from a detailed analysis of the moving and pausing behavior of single neurofilaments in axons of cultured neurons. We show that the model can match the shape, velocity, and spreading of the neurofilament transport waves obtained by radioisotopic pulse labeling in vivo. The model predicts that axonal neurofilaments spend ∼8% of their time on track and ∼97% of their time pausing during their journey along the axon.

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17

Bloom, G. S., B. W. Richards, P. L. Leopold, D. M. Ritchey, and S. T. Brady. "GTP gamma S inhibits organelle transport along axonal microtubules." Journal of Cell Biology 120, no. 2 (January 15, 1993): 467–76. http://dx.doi.org/10.1083/jcb.120.2.467.

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Movements of membrane-bounded organelles through cytoplasm frequently occur along microtubules, as in the neuron-specific case of fast axonal transport. To shed light on how microtubule-based organelle motility is regulated, pharmacological probes for GTP-binding proteins, or protein kinases or phosphatases were perfused into axoplasm extruded from squid (Loligo pealei) giant axons, and effects on fast axonal transport were monitored by quantitative video-enhanced light microscopy. GTP gamma S caused concentration-dependent and time-dependent declines in organelle transport velocities. GDP beta S was a less potent inhibitor. Excess GTP, but not GDP, masked the effects of coperfused GTP gamma S. The effects of GTP gamma S on transport were not mimicked by broad spectrum inhibitors of protein kinases (K-252a) or phosphatases (microcystin LR and okadaic acid), or as shown earlier, by ATP gamma S. Therefore, suppression of organelle motility by GTP gamma S was guanine nucleotide-specific and evidently did not involve irreversible transfer of thiophosphate groups to protein. Instead, the data imply that organelle transport in the axon is modulated by cycles of GTP hydrolysis and nucleotide exchange by one or more GTP-binding proteins. Fast axonal transport was not perturbed by AlF4-, indicating that the GTP gamma S-sensitive factors do not include heterotrimeric G-proteins. Potential axoplasmic targets of GTP gamma S include dynamin and multiple small GTP-binding proteins, which were shown to be present in squid axoplasm. These collective findings suggest a novel strategy for regulating microtubule-based organelle transport and a new role for GTP-binding proteins.

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18

Morfini, Gerardo, Gustavo Pigino, Uwe Beffert, Jorge Busciglio, and Scott T. Brady. "Fast Axonal Transport Misregulation and Alzheimer's Disease." NeuroMolecular Medicine 2, no. 2 (2002): 089–100. http://dx.doi.org/10.1385/nmm:2:2:089.

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19

Vallee, R. B., and G. S. Bloom. "Mechanisms of Fast and Slow Axonal Transport." Annual Review of Neuroscience 14, no. 1 (March 1991): 59–92. http://dx.doi.org/10.1146/annurev.ne.14.030191.000423.

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20

Breuer, A. C., and M. B. Atkinson. "Calcium dependent modulation of fast axonal transport." Cell Calcium 9, no. 5-6 (October 1988): 293–301. http://dx.doi.org/10.1016/0143-4160(88)90010-3.

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21

Edgar, Julia M., Mark McLaughlin, Donald Yool, Su-Chun Zhang, Jill H. Fowler, Paul Montague, Jennifer A. Barrie, et al. "Oligodendroglial modulation of fast axonal transport in a mouse model of hereditary spastic paraplegia." Journal of Cell Biology 166, no. 1 (June 28, 2004): 121–31. http://dx.doi.org/10.1083/jcb.200312012.

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Oligodendrocytes are critical for the development of the plasma membrane and cytoskeleton of the axon. In this paper, we show that fast axonal transport is also dependent on the oligodendrocyte. Using a mouse model of hereditary spastic paraplegia type 2 due to a null mutation of the myelin Plp gene, we find a progressive impairment in fast retrograde and anterograde transport. Increased levels of retrograde motor protein subunits are associated with accumulation of membranous organelles distal to nodal complexes. Using cell transplantation, we show categorically that the axonal phenotype is related to the presence of the overlying Plp null myelin. Our data demonstrate a novel role for oligodendrocytes in the local regulation of axonal function and have implications for the axonal loss associated with secondary progressive multiple sclerosis.

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22

Kuznetsov, I. A., and A. V. Kuznetsov. "What tau distribution maximizes fast axonal transport toward the axonal synapse?" Mathematical Biosciences 253 (July 2014): 19–24. http://dx.doi.org/10.1016/j.mbs.2014.04.001.

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23

Martin, MaryAnn, Stanley J. Iyadurai, Andrew Gassman, Joseph G. Gindhart, Thomas S. Hays, and William M. Saxton. "Cytoplasmic Dynein, the Dynactin Complex, and Kinesin Are Interdependent and Essential for Fast Axonal Transport." Molecular Biology of the Cell 10, no. 11 (November 1999): 3717–28. http://dx.doi.org/10.1091/mbc.10.11.3717.

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In axons, organelles move away from (anterograde) and toward (retrograde) the cell body along microtubules. Previous studies have provided compelling evidence that conventional kinesin is a major motor for anterograde fast axonal transport. It is reasonable to expect that cytoplasmic dynein is a fast retrograde motor, but relatively few tests of dynein function have been reported with neurons of intact organisms. In extruded axoplasm, antibody disruption of kinesin or the dynactin complex (a dynein activator) inhibits both retrograde and anterograde transport. We have tested the functions of the cytoplasmic dynein heavy chain (cDhc64C) and the p150Glued(Glued) component of the dynactin complex with the use of genetic techniques in Drosophila.cDhc64C and Glued mutations disrupt fast organelle transport in both directions. The mutant phenotypes, larval posterior paralysis and axonal swellings filled with retrograde and anterograde cargoes, were similar to those caused by kinesin mutations. Why do specific disruptions of unidirectional motor systems cause bidirectional defects? Direct protein interactions of kinesin with dynein heavy chain and p150Glued were not detected. However, strong dominant genetic interactions between kinesin, dynein, and dynactin complex mutations in axonal transport were observed. The genetic interactions between kinesin and either Glued orcDhc64C mutations were stronger than those betweenGlued and cDhc64C mutations themselves. The shared bidirectional disruption phenotypes and the dominant genetic interactions demonstrate that cytoplasmic dynein, the dynactin complex, and conventional kinesin are interdependent in fast axonal transport.

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24

Kondo, S., R. Sato-Yoshitake, Y. Noda, H. Aizawa, T. Nakata, Y. Matsuura, and N. Hirokawa. "KIF3A is a new microtubule-based anterograde motor in the nerve axon." Journal of Cell Biology 125, no. 5 (June 1, 1994): 1095–107. http://dx.doi.org/10.1083/jcb.125.5.1095.

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Neurons are highly polarized cells composed of dendrites, cell bodies, and long axons. Because of the lack of protein synthesis machinery in axons, materials required in axons and synapses have to be transported down the axons after synthesis in the cell body. Fast anterograde transport conveys different kinds of membranous organelles such as mitochondria and precursors of synaptic vesicles and axonal membranes, while organelles such as endosomes and autophagic prelysosomal organelles are conveyed retrogradely. Although kinesin and dynein have been identified as good candidates for microtubule-based anterograde and retrograde transporters, respectively, the existence of other motors for performing these complex axonal transports seems quite likely. Here we characterized a new member of the kinesin super-family, KIF3A (50-nm rod with globular head and tail), and found that it is localized in neurons, associated with membrane organelle fractions, and accumulates with anterogradely moving membrane organelles after ligation of peripheral nerves. Furthermore, native KIF3A (a complex of 80/85 KIF3A heavy chain and a 95-kD polypeptide) revealed microtubule gliding activity and baculovirus-expressed KIF3A heavy chain demonstrated microtubule plus end-directed (anterograde) motility in vitro. These findings strongly suggest that KIF3A is a new motor protein for the anterograde fast axonal transport.

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25

Elluru, R. G., G. S. Bloom, and S. T. Brady. "Fast axonal transport of kinesin in the rat visual system: functionality of kinesin heavy chain isoforms." Molecular Biology of the Cell 6, no. 1 (January 1995): 21–40. http://dx.doi.org/10.1091/mbc.6.1.21.

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The mechanochemical ATPase kinesin is thought to move membrane-bounded organelles along microtubules in fast axonal transport. However, fast transport includes several classes of organelles moving at rates that differ by an order of magnitude. Further, the fact that cytoplasmic forms of kinesin exist suggests that kinesins might move cytoplasmic structures such as the cytoskeleton. To define cellular roles for kinesin, the axonal transport of kinesin was characterized. Retinal proteins were pulse-labeled, and movement of radiolabeled kinesin through optic nerve and tract into the terminals was monitored by immunoprecipitation. Heavy and light chains of kinesin appeared in nerve and tract at times consistent with fast transport. Little or no kinesin moved with slow axonal transport indicating that effectively all axonal kinesin is associated with membranous organelles. Both kinesin heavy chain molecular weight variants of 130,000 and 124,000 M(r) (KHC-A and KHC-B) moved in fast anterograde transport, but KHC-A moved at 5-6 times the rate of KHC-B. KHC-A cotransported with the synaptic vesicle marker synaptophysin, while a portion of KHC-B cotransported with the mitochondrial marker hexokinase. These results suggest that KHC-A is enriched on small tubulovesicular structures like synaptic vesicles and that at least one form of KHC-B is predominantly on mitochondria. Biochemical specialization may target kinesins to appropriate organelles and facilitate differential regulation of transport.

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26

Pilling, Aaron D., Dai Horiuchi, Curtis M. Lively, and William M. Saxton. "Kinesin-1 and Dynein Are the Primary Motors for Fast Transport of Mitochondria in Drosophila Motor Axons." Molecular Biology of the Cell 17, no. 4 (April 2006): 2057–68. http://dx.doi.org/10.1091/mbc.e05-06-0526.

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To address questions about mechanisms of filament-based organelle transport, a system was developed to image and track mitochondria in an intact Drosophila nervous system. Mutant analyses suggest that the primary motors for mitochondrial movement in larval motor axons are kinesin-1 (anterograde) and cytoplasmic dynein (retrograde), and interestingly that kinesin-1 is critical for retrograde transport by dynein. During transport, there was little evidence that force production by the two opposing motors was competitive, suggesting a mechanism for alternate coordination. Tests of the possible coordination factor P150Glued suggested that it indeed influenced both motors on axonal mitochondria, but there was no evidence that its function was critical for the motor coordination mechanism. Observation of organelle-filled axonal swellings (“organelle jams” or “clogs”) caused by kinesin and dynein mutations showed that mitochondria could move vigorously within and pass through them, indicating that they were not the simple steric transport blockades suggested previously. We speculate that axonal swellings may instead reflect sites of autophagocytosis of senescent mitochondria that are stranded in axons by retrograde transport failure; a protective process aimed at suppressing cell death signals and neurodegeneration.

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27

Viancour, Terry A., and Nancy A. Kreiter. "Vesicular fast axonal transport rates in young and old rat axons." Brain Research 628, no. 1-2 (November 1993): 209–17. http://dx.doi.org/10.1016/0006-8993(93)90957-o.

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28

Sickles, Dale W., J. Derek Stone, and Marvin A. Friedman. "Fast Axonal Transport: A Site of Acrylamide Neurotoxicity?" NeuroToxicology 23, no. 2 (July 2002): 223–51. http://dx.doi.org/10.1016/s0161-813x(02)00025-6.

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29

Popovic, Lea, Scott A. McKinley, and Michael C. Reed. "A Stochastic Compartmental Model for Fast Axonal Transport." SIAM Journal on Applied Mathematics 71, no. 4 (January 2011): 1531–56. http://dx.doi.org/10.1137/090775385.

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30

Mitsumoto, Hiroshi, Kozo Kurahashi, Jane M. Jacob, and Irvine G. McQuarrie. "Retardation of fast axonal transport in wobbler mice." Muscle & Nerve 16, no. 5 (May 1993): 542–47. http://dx.doi.org/10.1002/mus.880160517.

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31

Koschorke, G. M., R. A. Meyer, and J. N. Campbell. "The Development of Mechanosensitivity Requires Fast Axonal Transport." Clinical Journal of Pain 7, no. 1 (March 1991): 47. http://dx.doi.org/10.1097/00002508-199103000-00034.

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32

Sickles, Dale W. "Toxic neurofilamentous axonopathies and fast anterograde axonal transport." Toxicology and Applied Pharmacology 108, no. 3 (May 1991): 390–96. http://dx.doi.org/10.1016/0041-008x(91)90085-s.

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33

Nemhauser, I., Y. Doron, and D. J. Goldberg. "Inhibition of fast axonal transport by DNase I." Ultramicroscopy 17, no. 2 (January 1985): 166. http://dx.doi.org/10.1016/0304-3991(85)90028-2.

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34

Sheetz, Michael P., Eric R. Steuer, and Trina A. Schroer. "The mechanism and regulation of fast axonal transport." Trends in Neurosciences 12, no. 11 (January 1989): 474–78. http://dx.doi.org/10.1016/0166-2236(89)90099-4.

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35

Hammerschlag, Richard, and Judy Bobinski. "Does nerve impulse activity modulate fast axonal transport?" Molecular Neurobiology 6, no. 2-3 (June 1992): 191–201. http://dx.doi.org/10.1007/bf02780552.

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36

Prahlad, V., B. T. Helfand, G. M. Langford, R. D. Vale, and R. D. Goldman. "Fast transport of neurofilament protein along microtubules in squid axoplasm." Journal of Cell Science 113, no. 22 (November 15, 2000): 3939–46. http://dx.doi.org/10.1242/jcs.113.22.3939.

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Using squid axoplasm as a model system, we have visualized the fast transport of non-filamentous neurofilament protein particles along axonal microtubules. This transport occurs at speeds of 0.5-1.0 microm/second and the majority of neurofilament particles stain with kinesin antibody. These observations demonstrate, for the first time, that fast (0.5-1.0 microm/second) transport of neurofilament proteins occurs along microtubules. In addition, our studies suggest that neurofilament protein can be transported as non-membrane bound, nonfilamentous subunits along axons, and that the transport is kinesin-dependent. Microtubule-based fast transport might therefore provide a mechanism for the distribution and turnover of neurofilament, and perhaps other cytoskeletal proteins, throughout neurons.

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37

Kuznetsov, I. A., and A. V. Kuznetsov. "A coupled model of fast axonal transport of organelles and slow axonal transport of tau protein." Computer Methods in Biomechanics and Biomedical Engineering 18, no. 13 (May 28, 2014): 1485–94. http://dx.doi.org/10.1080/10255842.2014.920830.

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38

Terada, Sumio, Masataka Kinjo, Makoto Aihara, Yosuke Takei, and Nobutaka Hirokawa. "Kinesin-1/Hsc70-dependent mechanism of slow axonal transport and its relation to fast axonal transport." EMBO Journal 29, no. 4 (January 28, 2010): 843–54. http://dx.doi.org/10.1038/emboj.2009.389.

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Terada, Sumio, Masataka Kinjo, Makoto Aihara, Yosuke Takei, and Nobutaka Hirokawa. "Kinesin-1/Hsc70-Dependent Mechanism of Slow Axonal Transport and its Relation to Fast Axonal Transport." Biophysical Journal 100, no. 3 (February 2011): 354a. http://dx.doi.org/10.1016/j.bpj.2010.12.2130.

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Ohka, Seii, Mai Sakai, Stephanie Bohnert, Hiroko Igarashi, Katrin Deinhardt, Giampietro Schiavo, and Akio Nomoto. "Receptor-Dependent and -Independent Axonal Retrograde Transport of Poliovirus in Motor Neurons." Journal of Virology 83, no. 10 (February 25, 2009): 4995–5004. http://dx.doi.org/10.1128/jvi.02225-08.

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ABSTRACT Poliovirus (PV), when injected intramuscularly into the calf, is incorporated into the sciatic nerve and causes an initial paralysis of the inoculated limb in transgenic (Tg) mice carrying the human PV receptor (hPVR/CD155) gene. We have previously demonstrated that a fast retrograde axonal transport process is required for PV dissemination through the sciatic nerves of hPVR-Tg mice and that intramuscularly inoculated PV causes paralytic disease in an hPVR-dependent manner. Here we showed that hPVR-independent axonal transport of PV was observed in hPVR-Tg and non-Tg mice, indicating that several different pathways for PV axonal transport exist in these mice. Using primary motor neurons (MNs) isolated from these mice or rats, we demonstrated that the axonal transport of PV requires several kinetically different motor machineries and that fast transport relies on a system involving cytoplasmic dynein. Unexpectedly, the hPVR-independent axonal transport of PV was not observed in cultured MNs. Thus, PV transport machineries in cultured MNs and in vivo differ in their hPVR requirements. These results suggest that the axonal trafficking of PV is carried out by several distinct pathways and that MNs in culture and in the sciatic nerve in situ are intrinsically different in the uptake and axonal transport of PV.

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Gan, Kathlyn J., and Michael A. Silverman. "Dendritic and axonal mechanisms of Ca2+ elevation impair BDNF transport in Aβ oligomer–treated hippocampal neurons." Molecular Biology of the Cell 26, no. 6 (March 15, 2015): 1058–71. http://dx.doi.org/10.1091/mbc.e14-12-1612.

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Disruption of fast axonal transport (FAT) and intracellular Ca2+ dysregulation are early pathological events in Alzheimer's disease (AD). Amyloid-β oligomers (AβOs), a causative agent of AD, impair transport of BDNF independent of tau by nonexcitotoxic activation of calcineurin (CaN). Ca2+-dependent mechanisms that regulate the onset, severity, and spatiotemporal progression of BDNF transport defects from dendritic and axonal AβO binding sites are unknown. Here we show that BDNF transport defects in dendrites and axons are induced simultaneously but exhibit different rates of decline. The spatiotemporal progression of FAT impairment correlates with Ca2+ elevation and CaN activation first in dendrites and subsequently in axons. Although many axonal pathologies have been described in AD, studies have primarily focused only on the dendritic effects of AβOs despite compelling reports of presynaptic AβOs in AD models and patients. Indeed, we observe that dendritic CaN activation converges on Ca2+ influx through axonal voltage-gated Ca2+ channels to impair FAT. Finally, FAT defects are prevented by dantrolene, a clinical compound that reduces Ca2+ release from the ER. This work establishes a novel role for Ca2+ dysregulation in BDNF transport disruption and tau-independent Aβ toxicity in early AD.

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Parton, R. G., K. Simons, and C. G. Dotti. "Axonal and dendritic endocytic pathways in cultured neurons." Journal of Cell Biology 119, no. 1 (October 1, 1992): 123–37. http://dx.doi.org/10.1083/jcb.119.1.123.

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The endocytic pathways from the axonal and dendritic surfaces of cultured polarized hippocampal neurons were examined. The dendrites and cell body contained extensive networks of tubular early endosomes which received endocytosed markers from the somatodendritic domain. In axons early endosomes were confined to presynaptic terminals and to varicosities. The somatodendritic but not the presynaptic early endosomes were labeled by internalized transferrin. In contrast to early endosomes, late endosomes and lysosomes were shown to be predominantly located in the cell body. Video microscopy was used to follow the transport of internalized markers from the periphery of axons and dendrites back to the cell body. Labeled structures in both domains moved unidirectionally by retrograde fast transport. Axonally transported organelles were sectioned for EM after video microscopic observation and shown to be large multivesicular body-like structures. Similar structures accumulated at the distal side of an axonal lesion. Multivesicular bodies therefore appear to be the major structures mediating transport of endocytosed markers between the nerve terminals and the cell body. Late endocytic structures were also shown to be highly mobile and were observed moving within the cell body and proximal dendritic segments. The results show that the organization of the endosomes differs in the axons and dendrites of cultured rat hippocampal neurons and that the different compartments or stages of the endocytic pathways can be resolved spatially.

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González, Carolina, José Cánovas, Javiera Fresno, Eduardo Couve, Felipe A. Court, and Andrés Couve. "Axons provide the secretory machinery for trafficking of voltage-gated sodium channels in peripheral nerve." Proceedings of the National Academy of Sciences 113, no. 7 (February 2, 2016): 1823–28. http://dx.doi.org/10.1073/pnas.1514943113.

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The regulation of the axonal proteome is key to generate and maintain neural function. Fast and slow axoplasmic waves have been known for decades, but alternative mechanisms to control the abundance of axonal proteins based on local synthesis have also been identified. The presence of the endoplasmic reticulum has been documented in peripheral axons, but it is still unknown whether this localized organelle participates in the delivery of axonal membrane proteins. Voltage-gated sodium channels are responsible for action potentials and are mostly concentrated in the axon initial segment and nodes of Ranvier. Despite their fundamental role, little is known about the intracellular trafficking mechanisms that govern their availability in mature axons. Here we describe the secretory machinery in axons and its contribution to plasma membrane delivery of sodium channels. The distribution of axonal secretory components was evaluated in axons of the sciatic nerve and in spinal nerve axons after in vivo electroporation. Intracellular protein trafficking was pharmacologically blocked in vivo and in vitro. Axonal voltage-gated sodium channel mRNA and local trafficking were examined by RT-PCR and a retention-release methodology. We demonstrate that mature axons contain components of the endoplasmic reticulum and other biosynthetic organelles. Axonal organelles and sodium channel localization are sensitive to local blockade of the endoplasmic reticulum to Golgi transport. More importantly, secretory organelles are capable of delivering sodium channels to the plasma membrane in isolated axons, demonstrating an intrinsic capacity of the axonal biosynthetic route in regulating the axonal proteome in mammalian axons.

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Breuer, A. C., M. P. Lynn, M. B. Atkinson, S. M. Chou, A. J. Wilbourn, K. E. Marks, J. E. Culver, and E. J. Fleegler. "Fast axonal transport in amyotrophic lateral sclerosis: An intra-axonal organelle traffic analysis." Neurology 37, no. 5 (May 1, 1987): 738. http://dx.doi.org/10.1212/wnl.37.5.738.

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Barkus, Rosemarie V., Olga Klyachko, Dai Horiuchi, Barry J. Dickson, and William M. Saxton. "Identification of an Axonal Kinesin-3 Motor for Fast Anterograde Vesicle Transport that Facilitates Retrograde Transport of Neuropeptides." Molecular Biology of the Cell 19, no. 1 (January 2008): 274–83. http://dx.doi.org/10.1091/mbc.e07-03-0261.

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A screen for genes required in Drosophila eye development identified an UNC-104/Kif1 related kinesin-3 microtubule motor. Analysis of mutants suggested that Drosophila Unc-104 has neuronal functions that are distinct from those of the classic anterograde axonal motor, kinesin-1. In particular, unc-104 mutations did not cause the distal paralysis and focal axonal swellings characteristic of kinesin-1 (Khc) mutations. However, like Khc mutations, unc-104 mutations caused motoneuron terminal atrophy. The distributions and transport behaviors of green fluorescent protein-tagged organelles in motor axons indicate that Unc-104 is a major contributor to the anterograde fast transport of neuropeptide-filled vesicles, that it also contributes to anterograde transport of synaptotagmin-bearing vesicles, and that it contributes little or nothing to anterograde transport of mitochondria, which are transported primarily by Khc. Remarkably, unc-104 mutations inhibited retrograde runs by neurosecretory vesicles but not by the other two organelles. This suggests that Unc-104, a member of an anterograde kinesin subfamily, contributes to an organelle-specific dynein-driven retrograde transport mechanism.

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Lorenzo, Damaris Nadia, Alexandra Badea, Jonathan Davis, Janell Hostettler, Jiang He, Guisheng Zhong, Xiaowei Zhuang, and Vann Bennett. "A PIK3C3–Ankyrin-B–Dynactin pathway promotes axonal growth and multiorganelle transport." Journal of Cell Biology 207, no. 6 (December 22, 2014): 735–52. http://dx.doi.org/10.1083/jcb.201407063.

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Axon growth requires long-range transport of organelles, but how these cargoes recruit their motors and how their traffic is regulated are not fully resolved. In this paper, we identify a new pathway based on the class III PI3-kinase (PIK3C3), ankyrin-B (AnkB), and dynactin, which promotes fast axonal transport of synaptic vesicles, mitochondria, endosomes, and lysosomes. We show that dynactin associates with cargo through AnkB interactions with both the dynactin subunit p62 and phosphatidylinositol 3-phosphate (PtdIns(3)P) lipids generated by PIK3C3. AnkB knockout resulted in shortened axon tracts and marked reduction in membrane association of dynactin and dynein, whereas it did not affect the organization of spectrin–actin axonal rings imaged by 3D-STORM. Loss of AnkB or of its linkages to either p62 or PtdIns(3)P or loss of PIK3C3 all impaired organelle transport and particularly retrograde transport in hippocampal neurons. Our results establish new functional relationships between PIK3C3, dynactin, and AnkB that together promote axonal transport of organelles and are required for normal axon length.

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Le Roux, Lucia G., Xudong Qiu, Megan C. Jacobsen, Mark D. Pagel, Seth T. Gammon, David Piwnica-Worms, and Dawid Schellingerhout. "Axonal Transport as an In Vivo Biomarker for Retinal Neuropathy." Cells 9, no. 5 (May 22, 2020): 1298. http://dx.doi.org/10.3390/cells9051298.

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We illuminate a possible explanatory pathophysiologic mechanism for retinal cellular neuropathy by means of a novel diagnostic method using ophthalmoscopic imaging and a molecular imaging agent targeted to fast axonal transport. The retinal neuropathies are a group of diseases with damage to retinal neural elements. Retinopathies lead to blindness but are typically diagnosed late, when substantial neuronal loss and vision loss have already occurred. We devised a fluorescent imaging agent based on the non-toxic C fragment of tetanus toxin (TTc), which is taken up and transported in neurons using the highly conserved fast axonal transport mechanism. TTc serves as an imaging biomarker for normal axonal transport and demonstrates impairment of axonal transport early in the course of an N-methyl-D-aspartic acid (NMDA)-induced excitotoxic retinopathy model in rats. Transport-related imaging findings were dramatically different between normal and retinopathic eyes prior to presumed neuronal cell death. This proof-of-concept study provides justification for future clinical translation.

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Abbate, S. L., M. B. Atkinson, and A. C. Breuer. "Amount and Speed of Fast Axonal Transport in Diabetes." Diabetes 40, no. 1 (January 1, 1991): 111–17. http://dx.doi.org/10.2337/diab.40.1.111.

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Shah, Jagesh V., and Don W. Cleveland. "Slow axonal transport: fast motors in the slow lane." Current Opinion in Cell Biology 14, no. 1 (February 2002): 58–62. http://dx.doi.org/10.1016/s0955-0674(01)00294-0.

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Szebenyi, G., G. Morfini, M. Young, S. Sheridan, M. J. McPhaul, and S. T. Brady. "Proteins with pathogenic polyglutamine expansion inhibit fast axonal transport." Journal of Neurochemistry 81 (June 28, 2008): 76. http://dx.doi.org/10.1046/j.1471-4159.81.s1.44_4.x.

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