Migration of ribosomes along the axons of the chick visual pathway

Bondy, Stephen C.; Purdy, Janet L.

doi:10.1016/0005-2787(75)90354-8

Cited by 19 publications

(7 citation statements)

References 35 publications

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“…It is possible that a proximodistal gradient exists in the distribution of ribosomes along the axon and that the paucity of these structures in more distal segments of the axon may account for their sporadic detection by electron microscopy. The report that ribosomal particles are axonally transported (Bondy and Purdy, 1975) is consistent with this view. The possibility that a limited degree of endogenous protein synthesis does occur in the giant axon in vivo (Giuditta, 1980) is supported by the presence in squid axoplasm of all the components required for protein synthesis (Lasek et al, 1973;Giuditta et al, 1977Giuditta et al, , 1980, including mRNA (Giuditta et al, 1986a).…”

Section: Discussionsupporting

confidence: 79%

“…Clearly, they represent a small minority of the sequences found in the giant fiber lobe (Giuditta et al, 1986b) or optic lobe. It bears mention that some evidence exists for the axoplasmic transport of ribosomes, ribosomal proteins, and poly(A)+ RNAs in the avian visual system (Bondy and Purdy, 1975;Bondy et al, 1977). Alternatively, some species of axoplasmic poly(A)+ RNA could derive from the periaxonal glia in analogy (or in association) to the glia transported proteins postulated by Lasek and associates Tytell and Lasek, 1984).…”

Section: Discussionmentioning

confidence: 90%

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Occurrence and Sequence Complexity of Polyadenylated RNA in Squid Axoplasm

Perrone-Capano

Giuditta

Castigli

et al. 1987

Journal of Neurochemistry

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Axoplasmic RNA from the giant axon of the squid (Loligo pealii) comprises polyadenylated [poly (A)+] RNA, as judged, in part, by hybridization to [3H]polyuridine and by in situ hybridization analyses using the same probe. The polyadenylate content of axoplasm (0.24 ng/microgram of total RNA) suggests that the poly(A)+ RNA population makes up approximately 0.4% of total axoplasmic RNA. Axoplasmic poly(A)+ RNA can serve as a template for the synthesis of cDNA using a reverse transcriptase and oligo(deoxythymidine) as primer. The size of the cDNA synthesized is heterogeneous, with most fragments greater than 450 nucleotides. The hybridization of axoplasmic cDNA to its template RNA reveals two major kinetic classes: a rapidly hybridizing component (abundant sequences) and a slower-reacting component (moderately abundant and rare sequences). The latter component accounts for approximately 56% of the total cDNA mass. The rapidly and slowly hybridizing kinetic components have a sequence complexity of approximately 2.7 kilobases and 3.1 X 10(2) kilobases, respectively. The diversity of the abundant and rare RNA classes is sufficient to code for one to two and 205, respectively, different poly(A)+ RNAs averaging 1,500 nucleotides in length. Overall, the sequence complexity of axoplasmic poly(A)+ RNA represents approximately 0.4% that of poly(A)+ mRNA of the optic lobe, a complex neural tissue used as a standard. Taken together, these findings indicate that the squid giant axon contains a heterogeneous population of poly(A)+ RNAs.

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 90%

Occurrence and Sequence Complexity of Polyadenylated RNA in Squid Axoplasm

Perrone-Capano

Giuditta

Castigli

et al. 1987

Journal of Neurochemistry

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“…On the other hand, earlier experiments designed to verify the cell body origin of axonal RNAs using radiolabeled precursors consistently yielded controversial results (13,34,36,106,107,160,258,263). More recently, RNA granules were identified and characterized in neurons (reviewed in Ref.…”

Section: Origin Of Axonal and Presynaptic Proteins: The Cell Bodymentioning

confidence: 99%

“…However, the experimental demonstration of this hypothesis by radiolabeling perikaryal RNA and monitoring its displacement toward distal axonal sites was met by considerable difficulties in the interpretation of the data. Indeed, at variance with the axonal transport of radiolabeled somatic proteins, the wave of radiolabeled RNA invading the nerve was generally associated with, and often preceded by, a wave of radiolabeled RNA precursors (16,34,36,106,107,160,258,263). Under these circumstances, the RNA precursors entered periaxonal glia and were incorporated into radiolabeled RNA that was retained in the glial cells and partly transferred to the axon.…”

Section: Synthesis Of Axonal and Presynaptic Rna: The Cell Body Hymentioning

confidence: 99%

Local Gene Expression in Axons and Nerve Endings: The Glia-Neuron Unit

Giuditta¹,

Chun²,

Eyman³

et al. 2008

Physiological Reviews

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Neurons have complex and often extensively elongated processes. This unique cell morphology raises the problem of how remote neuronal territories are replenished with proteins. For a long time, axonal and presynaptic proteins were thought to be exclusively synthesized in the cell body, which delivered them to peripheral sites by axoplasmic transport. Despite this early belief, protein has been shown to be synthesized in axons and nerve terminals, substantially alleviating the trophic burden of the perikaryon. This observation raised the question of the cellular origin of the peripheral RNAs involved in protein synthesis. The synthesis of these RNAs was initially attributed to the neuron soma almost by default. However, experimental data and theoretical considerations support the alternative view that axonal and presynaptic RNAs are also transcribed in the flanking glial cells and transferred to the axon domain of mature neurons. Altogether, these data suggest that axons and nerve terminals are served by a distinct gene expression system largely independent of the neuron cell body. Such a local system would allow the neuron periphery to respond promptly to environmental stimuli. This view has the theoretical merit of extending to axons and nerve terminals the marginalized concept of a glial supply of RNA (and protein) to the neuron cell body. Most long-term plastic changes requiring de novo gene expression occur in these domains, notably in presynaptic endings, despite their intrinsic lack of transcriptional capacity. This review enlightens novel perspectives on the biology and pathobiology of the neuron by critically reviewing these issues.

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“…Contamination by labeled proteins from the inevitable, and also variable, non-neuronal components of the cultured tissue is virtually excluded . However, no claim can be made as to the completeness of the representation of the axonal proteins : first, higher resolution techniques may permit detection of many more proteins on a single gel ; second, the use of one amino acid for labeling certainly excludes certain proteins from being visualized ; and third, possible synthesis of proteins within axons (24)(25)(26)(27)(28)(29) may be dependent on the local availability of necessary amino acids .…”

Section: Rapid Communicationsmentioning

confidence: 99%

A few axonal proteins distinguish ventral spinal cord neurons from dorsal root ganglion neurons.

Sonderegger¹,

Fishman²,

Bokoum³

et al. 1984

The Journal of Cell Biology

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A series of proteins putatively involved in the generation of axonal diversity was identified. Neurons from ventral spinal cord and dorsal root ganglia were grown in a compartmented cell-culture system which offers separate access to cell somas and axons. The proteins synthesized in the neuronal cell somas and subsequently transported into the axons were selectively analyzed by 2-dimensional gel electrophoresis. The patterns of axonal proteins were substantially less complex than those derived from the proteins of neuronal cell bodies. The structural and functional similarity of axons from different neurons was reflected in a high degree of similarity of the gel pattern of the axonal proteins from sensory ganglia and spinal cord neurons. Each axonal type, however, had several proteins that were markedly less abundant or absent in the other. These neuron-population enriched proteins may be involved in the implementation of neuronal diversity. One of the proteins enriched in dorsal root ganglia axons had previously been found to be expressed with decreased abundance when dorsal root ganglia axons were co-cultured with ventral spinal cord cells under conditions in which synapse formation occurs (P. Sonderegger, M. C. Fishman, M. Bokoum, H. C. Bauer, and P.G. Nelson, 1983, Science [Wash. DC], 221:1294-1297). This protein may be a candidate for a role in growth cone functions, specific for neuronal subsets, such as pathfinding and selective axon fasciculation or the initiation of specific synapses. The methodology presented is thus capable of demonstrating patterns of protein synthesis that distinguish different neuronal subsets. The accessibility of these proteins for structural and functional studies may contribute to the elucidation of neuron-specific functions at the molecular level.

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Migration of ribosomes along the axons of the chick visual pathway

Cited by 19 publications

References 35 publications

Occurrence and Sequence Complexity of Polyadenylated RNA in Squid Axoplasm

Occurrence and Sequence Complexity of Polyadenylated RNA in Squid Axoplasm

Local Gene Expression in Axons and Nerve Endings: The Glia-Neuron Unit

A few axonal proteins distinguish ventral spinal cord neurons from dorsal root ganglion neurons.

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