Ribosomes and polyribosomes are present in the squid giant axon: an immunocytochemical study

Sotelo, Julio; Kun, Alejandra; Benech, Juan Claudio; Giuditta, Antonio; Morillas, José Manuel Martín; Benech, Claudio R.

doi:10.1016/s0306-4522(98)00587-9

Cited by 30 publications

(18 citation statements)

References 25 publications

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“…The second argument is that many components of translation machinery are found in axons, including in squid giant axoplasm, and therefore this serves as prima facie evidence that translation must be occurring in this cellular compartment (Alvarez et al 2000;Giuditta et al 2008). These data include reports of abundant tRNAs (Black and Lasek 1977;Ingoglia et al 1983), mRNAs (Capano et al 1987;Gioio et al 1994;Kaplan et al 1992;Rapallino et al 1988), various elongation and initiation factors (Giuditta et al 1980;Giuditta et al 1986;Giuditta et al 1991;Kar et al 2013), rRNA (Giuditta et al 1980;Perrone-Capano et al 1999), and even polyribosomes that can be translated in vitro to produce various proteins (Giuditta et al 1991;Sotelo et al 1999). Given this apparent translation capacity of squid axoplasm it should then be possible for isolated axoplasm to synthesize proteins directly from radioactive amino acids.…”

Section: Discussionmentioning

confidence: 99%

“…These putative subaxolemmal ribosomes are detected by various indirect assays which include staining with a sensitive RNA biding dye, YOYO-1 (Koenig and Martin 1996), electron microscopic imaging (ESI) that detects ribosomal phosphate signals (Bleher and Martin 2001;Martin et al 1989), and immunohistochemistry using the Y-10B antibody specific or rRNA (Sotelo et al 1999). If such subaxolemmal ribosomes are present in the squid giant axon it is then argued that they might not be included in the axoplasm following extrusion (Alvarez et al 2000), and that this could explain why isolated axoplasm could not be shown to synthesize proteins.…”

Section: Discussionmentioning

confidence: 99%

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Squid Giant Axon Contains Neurofilament Protein mRNA but does not Synthesize Neurofilament Proteins

et al. 2016

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When isolated squid giant axons are incubated in radioactive amino acids, abundant newly synthesized proteins are found in the axoplasm. These proteins are translated in the adaxonal Schwann cells and subsequently transferred into the giant axon. The question as to whether any de novo protein synthesis occurs in the giant axon itself is difficult to resolve because the small contribution of the proteins possibly synthesized intra-axonally is not easily distinguished from the large amounts of the proteins being supplied from the Schwann cells. In this paper we reexamine this issue by studying the synthesis of endogenous neurofilament (NF) proteins in the axon. Our laboratory previously showed that NF mRNA and protein is present in the squid giant axon, but not in the surrounding adaxonal glia. Therefore, if the isolated squid axon could be shown to contain newly synthesized NF protein de novo, it could not arise from the adaxonal glia. The results of experiments in this paper show that abundant 3H-labeled NF protein is synthesized in the squid giant fiber lobe containing the giant axon's neuronal cell bodies, but despite the presence of NF mRNA in the giant axon, no labeled NF protein is detected in the giant axon. This lends support to the Glia-Axon Protein Transfer Hypothesis which posits that the squid giant axon obtains newly synthesized protein by Schwann cell transfer and not through intra-axonal protein synthesis, and further suggests that the NF mRNA in the axon is in a translationally repressed state.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Squid Giant Axon Contains Neurofilament Protein mRNA but does not Synthesize Neurofilament Proteins

et al. 2016

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“…TEM experimental evidences have demonstrated the presence of ribosomes in normal peripheral axons in different species including invertebrates (Kun et al, 1998 and2007;Koenig and Martin, 1996;Zelena, 1972aZelena, , 1972bZelena, and 1970Martin et al, 1989;Sotelo et al, 1999;). Axonal translational machinery could play an important role in structural and physiological maintenance, especially considering renewal and turn-over of proteins.…”

Section: Schwann Cell Organization Characterization Of Normal Human mentioning

confidence: 99%

“…After pre-treatment, the procedure was done basically as described by Kun et al (2007) and Sotelo et al (1999), with some modifications. The sections were incubated 1 h at 37ºC with the specific antibodies in IB (see above) in a wet chamber.…”

Section: Immunostainingmentioning

confidence: 99%

The Schwann Cell-Axon Link in Normal Condition or Neuro-Degenerative Diseases: An Immunocytochemical Approach

Kun¹,

Rosso²,

Canclini³

et al. 2012

Applications of Immunocytochemistry

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“…Recent data have shown the existence of protein synthesis and RNA translation not only in the cell body of neurons but also in neurites and synaptic sites (Kang and Schuman, 1996;Martin et al, 1998;Sotelo et al, 1999;Alvarez et al, 2000;Sigrist et al, 2000;Schacher and Wu, 2002). The presence of local protein synthesis in terminals could explain the rapidity of the anisomycin effect in increasing neurotransmitter release in C1C3 cocultures (Sherff and Carew, 2000;Wang et al, 2002;Zhang and Poo, 2002).…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Neurotransmitter Release by a Nonphysiological Target Requires Protein Synthesis and Involves cAMP-Dependent and Mitogen-Activated Protein Kinases

Ghirardi¹,

Benfenati²,

Giovedì³

et al. 2004

J. Neurosci.

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During the development of neuronal circuits, axonal growth cones can contact many inappropriate targets before they reach an appropriate postsynaptic partner. Although it is well known that the contact with synaptic partners upregulates the secretory machinery of the presynaptic neuron, little is known about the signaling mechanisms involved in preventing the formation of connections with inappropriate target cells. Here, we show that the contact with a nonphysiological postsynaptic target inhibits neurotransmitter release from axonal terminals of the Helix serotonergic neuron C1 by means of an active mechanism requiring ongoing protein synthesis and leading to the inhibition of cAMP-dependent protein kinase (PKA) and mitogen-activated protein kinase (MAPK)-extracellular signal-related kinase (Erk) pathways. The reversal of the inhibitory effect of the nonphysiological target by blockade of protein synthesis was prevented by cAMP-PKA or MAPK-Erk inhibitors, whereas disinhibition of neurotransmitter release promoted by cAMP-PKA activation was not affected by MAPK-Erk inhibitors. The data indicate that the inhibitory effect of the nonphysiological target on neurotransmitter release is an active process that requires protein synthesis and involves the downregulation of the MAPK-Erk and cAMP-PKA pathways, the same protein kinases that are activated after contact with a physiological target neuron. These mechanisms could play a relevant role in the prevention of synapse formation between inappropriate partners by modulating the neurotransmitter release capability of growing nerve terminals according to the nature of the targets contacted during their development.

show abstract

Ribosomes and polyribosomes are present in the squid giant axon: an immunocytochemical study

Cited by 30 publications

References 25 publications

Squid Giant Axon Contains Neurofilament Protein mRNA but does not Synthesize Neurofilament Proteins

Squid Giant Axon Contains Neurofilament Protein mRNA but does not Synthesize Neurofilament Proteins

The Schwann Cell-Axon Link in Normal Condition or Neuro-Degenerative Diseases: An Immunocytochemical Approach

Inhibition of Neurotransmitter Release by a Nonphysiological Target Requires Protein Synthesis and Involves cAMP-Dependent and Mitogen-Activated Protein Kinases

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