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PTPσ Is a Receptor for Chondroitin Sulfate Proteoglycan, an Inhibitor of Neural Regeneration
Open accessAbstract
Toward Neuronal Regeneration: Neurons in the central nervous system that are severed or crushed do not regenerate well. Part of the problem derives from the glial scars left behind after such damage. The scar tissue contains sulfated proteoglycans that seem to inhibit axon regeneration. Shen et al. (p. 592 , published online 15 October) have now identified a protein tyrosine phosphatase (PTP) in mouse neuronal membranes that functions as a receptor for the proteoglycans. Neurons that lacked this particular PTP showed improved regeneration. Regeneration remained incomplete, presumably due to other inhibitory factors in the way of complete axon regeneration.
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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 Shen et al., 2009
In the citing paper
“Known CS/CSPG receptors are: contactin-1 (Mikami et al., 2009), receptor protein tyrosine phosphatase sigma (RPTPσ; Shen et al., 2009), leukocyte common antigen-related phosphatase (LAR; Fisher et al., 2011) and Nogo receptor (NgR) 1 and 3 (Dickendesher et al., 2012).”
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 Shen et al., 2009
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“RPTPσ can bind with high affinity to neurocan and aggrecan and strongly inhibits axon outgrowth and regeneration (Sapieha et al., 2005;Shen et al., 2009;Fry et al., 2010;Lang et al., 2015).”
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 Shen et al., 2009
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Metadata
- Authors
- Shen, Y., Tenney, A. P., Busch, S. A., Horn, K. P., Cuascut, F. X., Liu, K., He, Z., Silver, J., & Flanagan, J. G.
- Affiliations
- Harvard University (US)
- Case Western Reserve University (US)
- Boston Children's Hospital (US)
- Corresponding author
- Shen, Yingjie
- Tenney, Alan P.
- Flanagan, John G.
- Venue
- Science
- Published
- 2009-10-23
- Volume
- 326
- Issue
- 5952
- Pages
- 592-596
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2811318
- OpenAlex
- W2043930451
- Cited by
- 682
- References
- 36
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 31 · 2023: 30 · 2022: 34 · 2021: 41 · 2020: 40 · 2019: 32 · 2018: 45 · 2017: 43 · 2016: 35 · 2015: 53 · 2014: 63 · 2013: 57 · 2012: 59
- FWCI
- 17.27
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Eye Institute (R01EY011559)
- National Institute of Neurological Disorders and Stroke (R37NS025713, R01NS025713)
- Eunice Kennedy Shriver National Institute of Child Health and Human Development (R37HD029417)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Health Sciences › Medicine › Clinical Neurology › Spinal Cord Injury Research
- Keywords
- PTPσ, chondroitin sulfate proteoglycans, axon regeneration, nerve regeneration, spinal cord injury, immunoglobulin-like domains, gene disruption, neuroprotection
- MeSH terms
- Animals, Astrocytes, Axons, Binding Sites, Cells, Cultured, Chondroitin Sulfates, Female, Ganglia, Spinal, Ligands, Nerve Regeneration, Nerve Tissue Proteins, Neurons, Protein Binding, Chondroitin Sulfate Proteoglycans, Proteoglycans, Recombinant Fusion Proteins, Spinal Cord, Spinal Cord Injuries, Neurites, Mice, Aggrecans, Receptor-Like Protein Tyrosine Phosphatases, Class 2, Protein Interaction Domains and Motifs, Neurocan
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