The DOI matches its Crossref record; 90 of the 92 references it cites were found in a registry or an index.
Semaphorin 3A displays a punctate distribution on the surface of neuronal cells and interacts with proteoglycans in the extracellular matrix
Abstract
Secreted semaphorins are essential for neural development and continue to be expressed in subpopulations of adult neurons, where they subserve as yet unknown functions. We employed functional myc- and GFP-tagged Sema3A proteins to obtain insight in the localization of Sema3A in neuronal cells. Sema3A localized to both axons and dendrites of cortical neurons. GFP-Sema3A exhibited a characteristic punctate distribution on the surface of Neuro-2a cells, localized to migratory pathways of cultured cells, and co-localized with and induced clustering of its receptor component neuropilin-1. Treatment with excess glycosaminoglycans and chondroitinase ABC resulted in the removal of cell surface Sema3A. Heparin enhanced Sema3A's binding to neuropilin-1-expressing cells and potentiated its growth cone collapsing activity. Together, these results indicate that association with proteoglycans in the extracellular matrix of neuronal cells plays an important role in the localization of the chemorepulsive guidance cue Sema3A, and that this interaction may enhance its biological activity.
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“Specifically, CSPGs, and particularly their GAG moieties, may act by i) binding to a specific receptor; ii) blocking the growth-promoting activity of integrins; iii) presenting growth-inhibitory proteins.”
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 De Wit et al., 2005
In the citing paper
“Another potential mechanism of action of PNNs may rely on the binding of GAG chains to ligands harboring growth-inhibitory or repulsive effects.”
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 De Wit et al., 2005
In the citing paper
“Recently, the repulsive guidance molecule semaphorin3A (Sema3A) has been identified as a PNN component (De Wit et al., 2005;Vo et al., 2013).”
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 De Wit et al., 2005
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Self-citation
Metadata
- Authors
- De Wit, J., De Winter, F., Klooster, J., & Verhaagen, J.
- Corresponding author
- Verhaagen, Joost
- ORCID
- Verhaagen, Joost
- Venue
- Molecular and Cellular Neuroscience
- Publisher
- Elsevier BV
- Published
- 2005-05
- Volume
- 29
- Issue
- 1
- Pages
- 40-55
- ISSN
- 1044-7431 (ISSN-L)
- OpenAlex
- W2078936926
- Cited by
- 154
- References
- 92
- Citations by year
- 2026: 5 · 2025: 2 · 2024: 7 · 2023: 7 · 2022: 5 · 2021: 9 · 2020: 6 · 2019: 4 · 2018: 4 · 2017: 4 · 2016: 9 · 2015: 11 · 2014: 9 · 2013: 14 · 2012: 8
- FWCI
- 3.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular and Cellular Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- KNAW research portal (Royal Academy of Art and Sciences (KNAW)) (publishedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Lirias (KU Leuven) (submittedVersion)
- KNAW Research Portal (The Royal Netherlands Academy of Arts and Sciences) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Axon Guidance and Neuronal Signaling
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Keywords
- semaphorin 3A, neuropilin-1, proteoglycans, extracellular matrix, glycosaminoglycans, chondroitinase ABC, cell surface localization, growth cone collapse, axons and dendrites, cortical neurons, N2a cells, heparin binding
- MeSH terms
- Animals, Anticoagulants, Epitopes, Cerebral Cortex, Heparin, Membrane Proteins, Neuroblastoma, Neurons, Protein Binding, Proteoglycans, Tumor Cells, Cultured, Proto-Oncogene Proteins c-myc, Extracellular Matrix Proteins, Rats, Wistar, Growth Cones, Neuropilin-1, Semaphorin-3A, Green Fluorescent Proteins, Mice, Rats
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