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Cited by 15Axon Guidance and Neuronal SignalingNeurogenesis and neuroplasticity mechanismsNeuroscience and Neuropharmacology Research

Glutamatergic cerebellar granule neurons synthesize and secrete reelin in vitro

Sinagra, Mélanie, Gonzalez Campo, Cecilia, Verrier, Danièle, Moustié, Olivier, Manzoni, Olivier J., Chavis, Pascale·2008·Neuron Glia Biology
DOI 10.1017/s1740925x09990214
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Abstract

In the postnatal forebrain, the extracellular matrix protein reelin is expressed and secreted by subsets of GABAergic neurons, whereas in the cerebellum reelin is detected in glutamatergic cells of the granule cell layer. Thus, various regions of the postnatal brain present different patterns of reelin expression, whose significance remains unknown. We combined immunocytochemical and pharmacological approaches to characterize the phenotypic and temporal profiles of reelin expression in dissociated cultures of cerebellar granule neurons. A single type of reelin immunoreactivity, identified by a punctate labelling, was present in the somata of the majority of neurons. This immunoreactivity was observed throughout maturation and was exclusively present in glutamatergic neurons expressing the vesicular glutamate transporter 1. Neurons containing the reelin receptors apolipoprotein E receptor 2 (Apoer2) and very low-density lipoprotein receptor (Vldlr) represented about 80% of cerebellar neurons. The vast majority of reelin-positive neurons coexpressed Apoer2, suggesting that reelin immunoreactivity resulted in part from receptor-bound reelin. Inhibition of protein synthesis with cycloheximide completely abolished reelin immunoreactivity. In contrast, blocking protein secretion with brefeldin A did not affect the proportion of punctate neurons but revealed a subpopulation of neurons characterized by a solid reelin staining. These data show for the first time that a homogeneous population of glutamatergic neurons can synthesize and secrete reelin in cerebellar granule cells in vitro.

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Crossref · 10.1017/s1740925x09990214

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  • Reelin is expressed in GABAergic and glutamatergic cells.

    “Reelin is an important protein expressed in GABAergic and glutamatergic cells [133, 134].”

    From Consensus Paper: Pathological Role of the Cerebellum in Autism (2012) · cites this paper as [134]

  • Reelin's function relies on proteolytic activity on extracellular matrix proteins, which is inhibited by organophosphate pesticides.

    “Among several mechanisms, this function also relies on a proteolytic activity exerted by reelin on extracellular matrix proteins, which is inhibited by organophosphate (OP) pesticides [134].”

    From Consensus Paper: Pathological Role of the Cerebellum in Autism (2012) · cites this paper as [134]

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Authors
Sinagra, M., Gonzalez Campo, C., Verrier, D., Moustié, O., Manzoni, O. J., & Chavis, P.
Affiliations
  • Université de Bordeaux (FR)
  • Inserm (FR)
Corresponding author
Chavis, Pascale
ORCID
Venue
Neuron Glia Biology
Publisher
Cambridge University Press (CUP)
Published
2008-08
Volume
4
Issue
3
Pages
189-196
ISSN
  • 1740-925X (ISSN-L)
  • 1741-0533
DOI
10.1017/s1740925x09990214
OpenAlex
W2034552196
Cited by
15
References
32
Citations by year
2026: 1 · 2023: 2 · 2022: 1 · 2016: 1 · 2015: 1 · 2013: 4 · 2012: 3
FWCI
0.29
Type
journal article
Language
en
Open access
closed
Licence
www.cambridge.org/core/terms (unspecified, 377 d)
Locations
  • Neuron Glia Biology (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
  • Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
reelin, cerebellar granule cells, glutamatergic neurons, VGLUT1, ApoER2, VLDLR, protein synthesis, brefeldin A, postnatal cerebellum, neuronal maturation
MeSH terms
Reelin Protein, Animals, Animals, Newborn, Cell Count, Cerebellum, Cycloheximide, Glutamate Decarboxylase, Nerve Tissue Proteins, Neurons, Protein Synthesis Inhibitors, Receptors, LDL, Serine Endopeptidases, Time Factors, Cell Adhesion Molecules, Neuronal, Extracellular Matrix Proteins, Receptors, Lipoprotein, Glutamic Acid, Brefeldin A, LDL-Receptor Related Proteins, Vesicular Inhibitory Amino Acid Transport Proteins, Vesicular Glutamate Transport Protein 1, Mice

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