Fast and Slow Components in Axonal Transport of Protein

McEwen, Bruce S.; Grafstein, Bernice

doi:10.1083/jcb.38.3.494

Cited by 335 publications

(89 citation statements)

References 21 publications

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“…This effect may be related to variations observed in the morphology of vesicles believed to be transported through adrenergic fibers. Finally, this effect should not be confused with the increased solubility of the material carried by slow transport (21), since only material carried by fast transport will be observed at either of these time periods.…”

Section: Differential Transport Of Protein In Axon Branches 1525mentioning

confidence: 99%

Differential Transport of Protein in Axons: Comparison Between the Sciatic Nerve and Dorsal Columns of Cats

Anderson

McClure

1973

Proc. Natl. Acad. Sci. U.S.A.

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Fast axoplasmic transport was studied in dorsal root ganglion cells of the cat. Proteins carried in the fast axoplasmic flow were labeled after an intraganglionic injection of L-[4,5-3Hlleucine. The rate of transport was 380 + 26 mm/day in both the central and peripheral branches of the bifurcating axons that arise from cells of the dorsal root ganglion. The amount of radioactivity transported centrally, through the dorsal roots into the spinal cord, was about 50% of that moving peripherally, through the sensory fibers of the sciatic nerve. Labeled material appears to be transported principally in a bound form, as 70-80% of the radioactivity was insoluble in 0.01 M potassium phosphate buffer at pH 7.4. With multiple extractions, a fractionation procedure was developed by which 94-96% of the total transported radioactivity could be solubilized. The proteins carried by fast axoplasmic transport through the dorsal columns and through the sciatic nerve were compared by electrophoresis of extracted fractions on Na dodecyl sulfate-polyacrylamide gels.Different patterns of radioactivity are seen in the electrophoretograms, suggesting that the cells of the dorsal root ganglion may possess the ability to commit different proteins to transport through two branches of a single bifurcating axon.Neurons elaborate various protein and particulate matter that is carried through the axon to the nerve terminals by fast axoplasmic transport (1, 2). This phenomenon has been demonstrated in sensory fibers of the sciatic nerve after injection of [3HIleucine into the seventh lumbar dorsal root ganglia (Lq DRG) of cats (3, 4). Labeled material also moves from the DRG through the dorsal root fibers into the central nervous system (3). Recent work has confirmed the importance of fast transport in the control and maintenance of synaptic function (5, 6).In this paper, we consider the question: Can different proteins be transported through different branches of a bifurcating axon? The cells of the Lq DRG in cats provide a useful experimental system. Each of these cells sends out a single bifurcating fiber (7). From the bifurcation, one branch extends toward the periphery as a sensory fiber in the sciatic nerve. The other branch travels through the dorsal roots and into the spinal cord, where the fiber either terminates within a short distance or extends up the dorsal columns to the dorsal column nuclei in the medulla. In this study, labeling with radioactive precursors was used to compare material transported through the peripheral fibers, in the sciatic nerve, with that transported through the central fibers, in the dorsal columns. Although the rate of movement and the general Abbreviations: DRG, dorsal root ganglia; L7, lumbar seventh. 1521 solubility characteristics of the labeled material were the same for material moving in both directions, different transported proteins were found in the two branches. MATERIALS AND METHODSCats (between 2.5 and 4.0 kg) were anesthetized by intraperitoneal injection of sodium pentobarbital (aver...

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Section: Differential Transport Of Protein In Axon Branches 1525mentioning

confidence: 99%

Differential Transport of Protein in Axons: Comparison Between the Sciatic Nerve and Dorsal Columns of Cats

Anderson

McClure

1973

Proc. Natl. Acad. Sci. U.S.A.

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“…The turnover of the axonal cytoskeleton requires active transport of newly synthesized cytoskeletal proteins from the cell body along the axon. The transport of NF and microtubule (MT) proteins, first documented more than 30 years ago (Weiss and Hiscoe, 1948;Lasek, 1967;Karlsson and Sjostrand, 1968;McEwen and Grafstein, 1968), takes place through an as yet unidentified mechanism (Nixon, 1998) at rates 100 times slower (0.1-1.0 mm/d) than conventional MT motor-driven vesicular cargoes (ϳ50 -100 mm/d).…”

Section: Introductionmentioning

confidence: 99%

Bidirectional Translocation of Neurofilaments along Microtubules Mediated in Part by Dynein/Dynactin

Shah

Flanagan

Janmey

et al. 2000

MBoC

157

141

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Neuronal cytoskeletal elements such as neurofilaments, F-actin, and microtubules are actively translocated by an as yet unidentified mechanism. This report describes a novel interaction between neurofilaments and microtubule motor proteins that mediates the translocation of neurofilaments along microtubules in vitro. Native neurofilaments purified from spinal cord are transported along microtubules at rates of 100-1000 nm/s to both plus and minus ends. This motion requires ATP and is partially inhibited by vanadate, consistent with the activity of neurofilament-bound molecular motors. Motility is in part mediated by the dynein/dynactin motor complex and several kinesin-like proteins. This reconstituted motile system suggests how slow net movement of cytoskeletal polymers may be achieved by alternating activities of fast microtubule motors.

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“…The quantity ofFC radioactivity in the terminals due to axonal transport was considered to be the difference between the total quantity of radioactivity in the contralateral (experimental) and the ipsilateral (control) tecta (or E -C). Since severa1 different batches of isotope were used, data were normalized essentiallv as described in McEwen and Grafstein (1968). The data are presentkd as experimental minus control values fbr tot& radioactivity per tectum, divided by the control value [(E -C')/c].…”

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confidence: 99%

Rapid axonal transport of the neural cell adhesion molecule

Garner¹,

Watanabe²,

Rutishauser³

1986

J. Neurosci.

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The neural cell adhesion molecule (NCAM) is a cell-surface glycoprotein that mediates cell-cell interactions in the nervous system during development. In the present study, we demonstrate that NCAM is axonally transported in 3-d-old chick retinal ganglion cells and that it travels within the fast component of axonal transport (FC). Proteins were radiolabeled in retinal ganglion cell bodies after intraocular injection of %-methionine. The presence of radiolabeled NCAM in the optic nerves and contralateral tecta was detected by specific immunoadsorption to a monoclonal antibody. Major radioactive polypeptide bands at relative mobilities of approximately 200,000, 150,000, and 120,000 Mr (after SDS-PAGE) were recognized by the anti-NCAM antibody. These bands comigrated in l-dimensional gels with components of purified NCAM from chick brain. The 2 largest NCAM polypeptides (at 200,000 and 150,000 Mr) were found to be transported in this system, while the 120,000 Mr form was apparently not transported. The ratio and electrophoretie profiles of the 2 transported forms of NCAM remained similar in the retina, optic nerve, chiasm, tract, and tectum, suggesting that there is no interconversion of the 2 major polypeptides. The fraction of NCAM in the %-labeled FC proteins appears to be at least an order of magnitude less than in the plasma membrane, suggesting that the turnover rate of NCAM at this age is slower than for other membrane proteins of the CNS.The neural cell adhesion molecule (NCAM), a cell-surface glycoprotein, mediates cell-cell adhesion during development of nerve tissue (for review, see Rutishauser, 1983). NCAM plays an important role during neurite fasciculation (Rutishauser et al., 1978a), in axon-muscle interaction , and in the association of nerve growth cones with glial precursors (Silver and Rutishauser, 1984).In the present study, we have examined the axonal transport characteristics of the neural cell adhesion molecule. Since there is no protein synthetic machinery within the axon, the molecule must be supplied to the neurite and its terminal by transport within 1 of the 3 major axonal transport rate-components. Each of the 3 major rate-components is thought to convey a cytoplasmic structure within the axon: the fast component (FC) (moving at approximately 250 mm/d) provides membranes and membrane proteins, while the 2 slow components (moving at 0.2 and 2 mm/d) convey cytoplasmic matrix and cytoskeleton, respectively (Lasek, 1980;Lasek et al., 1984).Received Dec. 30, 1985; revised May 8, 1986; accepted May 30, 1986. We wish to thank R. J. , 1983; Gennarini et al., 1984a, b) with a largely uniform distribution on the growth cone, axon shaft, and cell soma (Rutishauser et al., 1978b). It was therefore predicted that NCAM would be transported within the FC of axonal transport.Although the FC of axonal transport has been the subject of study for a number of years, only a few rapidly transported proteins have been well characterized: notably the Na+-K+ ATPase (Baittinger and Willard, 1981;Specht and...

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Fast and Slow Components in Axonal Transport of Protein

Cited by 335 publications

References 21 publications

Differential Transport of Protein in Axons: Comparison Between the Sciatic Nerve and Dorsal Columns of Cats

Differential Transport of Protein in Axons: Comparison Between the Sciatic Nerve and Dorsal Columns of Cats

Bidirectional Translocation of Neurofilaments along Microtubules Mediated in Part by Dynein/Dynactin

Rapid axonal transport of the neural cell adhesion molecule

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