Neurofilament and tubulin mRNA expression in schwann cells

Roberson, Mya L.; Toews, Arrel D.; Goodrum, Jeffry F.; Morell, Pierre

doi:10.1002/jnr.490330120

Cited by 38 publications

(25 citation statements)

References 33 publications

(34 reference statements)

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“…In mammalian peripheral nerves, the identification of the mRNAs coding for neuron-specific NF proteins in Schwann cells (95,170,271,286) is consistent with a glial transcription of axonal mRNAs, and with their transcellular transfer to the axon. More recently, the latter process has been elegantly demonstrated in the myelinated axons of mouse Wld s mutants (55).…”

Section: A Axonsmentioning

confidence: 60%

“…The mRNAs of the medium and light NF proteins were unexpectedly detected in the Schwann cells of young rats examined under a variety of conditions, including differentiation (170), demyelination, or unilateral nerve transection (271). In the latter condition, the light NF mRNA was also detected in the contralateral nerve, implying that it also occurred in normal nerves.…”

Section: Vertebrate Axonsmentioning

confidence: 97%

See 1 more Smart Citation

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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Section: A Axonsmentioning

confidence: 60%

Section: Vertebrate Axonsmentioning

confidence: 97%

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

Giuditta¹,

Chun²,

Eyman³

et al. 2008

Physiological Reviews

View full text Add to dashboard Cite

show abstract

“…36 However, Schwann cells, particularly nonmyelinating cells, also express both NF160 and ␤-tubulin. 37 We see that markers for undifferentiated glia (BLBP and GLAST) appear to be coexpressed with neural markers (NF160 and TUJ1) in NCCs in the His bundle and bundle branches. Although it is possible that NCCs form the neural marker labeled conducting myocardium, it is unlikely, as this labeling pattern occurs only at late developmental stages.…”

Section: Discussionmentioning

confidence: 80%

Neural Crest Cells Retain Multipotential Characteristics in the Developing Valves and Label the Cardiac Conduction System

Nakamura

Colbert

Robbins

2006

Circulation Research

307

357

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Abstract-Multipotent neural crest cells (NCCs) are a major extracardiac component of cardiovascular development.Although recognized as contributing cells to the arterial valves at early developmental stages, NCC persistence in the valves at later times or in the adult heart is controversial. We analyzed NCC persistence and contributions to both semilunar and atrioventricular (AV) valves in the mature heart. Two NCC-specific promoters driving Cre recombinase, Wnt1-Cre and P0-Cre, were mated with floxed reporter mice, R26R or CAG-CAT-EGFP, to map NCC fate. Hearts were analyzed before aorticopulmonary (AP) septation through adult stages. As previously demonstrated, strong NCC labeling was detected in ventral and dorsal outflow cushions before AP septation. In contrast to previous reports, we found that substantial numbers of labeled cells persisted in the semilunar valves in late fetal, neonatal, and adult hearts. Furthermore, NCCs were also found in the AV valves, almost exclusively in the septal leaflets. NCCs in the AV valves expressed melanocytic and neurogenic markers. However, cells labeled in the proximal cardiac conduction system exhibited neurogenic and gliagenic markers, whereas some NCCs expressed no differentiation specific markers. These results suggest that cardiac NCCs contribute to the mature valves and the cardiac conduction system and retain multipotent characteristics late in development.

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“…We have also not excluded genes according to prior knowledge of spatiotemporal expression, as several disease-causing genes are expressed in both neurons and Schwann cells, such as GARS (Cuesta et al, 2002;Verheijen et al, 2003) and NEFL (Roberson et al, 1992;Previtali et al, 2003). For 543 (of 545) proteins in our compendium, we were able to determine the chromosomal localization of the corresponding human homologous gene using SNPper (snpper.chip.org), the University of California, Santa Cruz, Genome Bioinformatics Suite (genome.ucsc.edu), Entrez Gene (ncbi.nlm.nih.gov/gene), and blast search validation (when required).…”

Section: Integrated Proteomics and Genetics Data Suggest Novel Positimentioning

confidence: 99%

Quantitative and Integrative Proteome Analysis of Peripheral Nerve Myelin Identifies Novel Myelin Proteins and Candidate Neuropathy Loci

Patzig¹,

Jahn²,

Tenzer³

et al. 2011

J. Neurosci.

157

190

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Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia-axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relative abundance was previously misestimated due to technical limitations regarding protein separation and visualization. Focusing on tetraspan-transmembrane proteins, we validated novel myelin constituents using immunobased methods. Bioinformatic comparison with mRNA-abundance profiles allowed the categorization in functional groups coregulated during myelin biogenesis and maturation. By differential myelin proteome analysis, we found that the abundance of septin 9, the protein affected in hereditary neuralgic amyotrophy, is strongly increased in a novel mouse model of demyelinating neuropathy caused by the loss of prion protein. Finally, the systematic comparison of our compendium with the positions of human disease loci allowed us to identify several candidate genes for hereditary demyelinating neuropathies. These results illustrate how the integration of unbiased proteome, transcriptome, and genome data can contribute to a molecular dissection of the biogenesis, cell biology, metabolism, and pathology of myelin. Peripheral nerve myelin facilitates rapid impulse conduction and normal motor and sensory functions. Many aspects of myelin biogenesis, glia-axonal interactions, and nerve homeostasis are poorly understood at the molecular level. We therefore hypothesized that only a fraction of all relevant myelin proteins has been identified so far. Combining gel-based and gel-free proteomic approaches, we identified 545 proteins in purified mouse sciatic nerve myelin, including 36 previously known myelin constituents. By mass spectrometric quantification, the predominant P0, periaxin, and myelin basic protein constitute 21, 16, and 8% of the total myelin protein, respectively, suggesting that their relative abundance was previously misestimated due to technical limitations regarding protein separation and visualization. Focusing on tetraspan-transmembrane proteins, we validated novel myelin constituents using immuno-based methods. Bioinformatic comparison with mRNA-abundance profiles allowed the categorization in functional groups coregulated during myelin biogenesis and maturation. By differential myelin proteome analysis, we found that the abundance of septin 9, the protein affected in hereditary neuralgic amyotrophy, is strongly increased in a novel mouse model of demyelinating neuropathy caused by the loss of prion pr...

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Neurofilament and tubulin mRNA expression in schwann cells

Cited by 38 publications

References 33 publications

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

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

Neural Crest Cells Retain Multipotential Characteristics in the Developing Valves and Label the Cardiac Conduction System

Quantitative and Integrative Proteome Analysis of Peripheral Nerve Myelin Identifies Novel Myelin Proteins and Candidate Neuropathy Loci

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