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Neurons Produce a Neuronal Cell Surface-Associated Chondroitin Sulfate Proteoglycan
Open accessAbstract
Monoclonal antibody Cat-315 recognizes a chondroitin sulfate proteoglycan (CSPG) expressed on the surface of subsets of neurons in many areas of the mammalian CNS (Lander et al., 1997). The cell type-specific expression exhibited by the Cat-315 CSPG and other perineuronal net CSPGs imparts a distinct molecular surface identity to a neuron (Celio and Blumcke, 1994; Lander et al., 1997). The cell type(s) producing these surface-associated proteins and yielding this cellular diversity has remained in question. The expression of the Cat-315 CSPG in primary rat cortical cultures has permitted an examination of the cellular source of the Cat-315 antigen, as well as a determination of its spatial relationship to the neuronal surface. Live-cell labeling of primary neuronal cultures demonstrates that the Cat-315 CSPG is on the extracellular surface of neurons. Furthermore, extraction experiments demonstrate that the Cat-315 CSPG lacks a transmembrane domain and that the entire molecule is extracellular and, therefore, can be considered a constituent of brain extracellular matrix. Several lines of evidence indicate that neurons with cell surface staining produce the Cat-315 CSPG. First, neurons with cell surface staining also show intracellular Cat-315 immunoreactivity. Second, β-xyloside or monensin, reagents that inhibit the synthesis and transport of CSPGs, increase intracellular Cat-315 immunoreactivity within neurons that express cell surface Cat-315 immunoreactivity. Third, double labeling with Cat-315 and a polyclonal antibody for the Golgi complex demonstrates a precise colocalization of the intracellular Cat-315 immunoreactivity with the Golgi. Together, these observations demonstrate that neurons contribute to the extracellular matrix of brain and that the Cat-315 CSPG is produced by the neurons that carry Cat-315 cell surface immunoreactivity.
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“In addition to being a key inhibitory molecule in the diffuse ECM, CSPGs around some classes of neurons also interact with other brain ECM molecules, self-assembling into aggregate structures called perineuronal nets (PNNs) [12–14].”
From The extracellular matrix and perineuronal nets in memory (2022) · cites this paper as [12]
Experimental — accuracy not yet measuredIn the citing paper
“As to the cellular origin of PNN components, molecules that are crucial for PNN assembly, namely HAS, link proteins and aggrecan, are exclusively synthesized by neurons, whereas astrocytes, oligodendrocyte precursors and oligodendrocytes produce other ECM molecules, which are then likely incorporated into the PNN (Carulli et al., 2006(Carulli et al., , 2007;;Lander et al., 1998; see table I).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Lander et al., 1998
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Cites
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Perineuronal nets: past and present
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Aggrecan Glycoforms Contribute to the Molecular Heterogeneity of Perineuronal Nets
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Metadata
- Authors
- Lander, C., Zhang, H., & Hockfield, S.
- Affiliations
- Yale University (US)
- ORCID
- Zhang, Hong
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1998-01-01
- Volume
- 18
- Issue
- 1
- Pages
- 174-183
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6793429
- OpenAlex
- W2121360720
- Cited by
- 107
- References
- 62
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2022: 6 · 2021: 3 · 2020: 5 · 2019: 2 · 2018: 4 · 2017: 5 · 2016: 2 · 2015: 5 · 2014: 3 · 2013: 8 · 2012: 6
- FWCI
- 1.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Eye Institute (EY 06511)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- chondroitin sulfate proteoglycans, perineuronal nets, extracellular matrix, Golgi apparatus, primary cortical neurons, monensin
- MeSH terms
- Animals, Antibodies, Monoclonal, Epitopes, Antigens, Surface, Astrocytes, Brain Chemistry, Cells, Cultured, Cerebral Cortex, Extracellular Matrix, Neurons, Chondroitin Sulfate Proteoglycans, Rats, Sprague-Dawley, Rats
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