期刊
SCIENCE
卷 326, 期 5952, 页码 592-596出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1178310
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资金
- NEI NIH HHS [R01 EY011559] Funding Source: Medline
- NICHD NIH HHS [R37 HD029417] Funding Source: Medline
- NINDS NIH HHS [R37 NS025713, R37 NS025713-22, R01 NS025713] Funding Source: Medline
Chondroitin sulfate proteoglycans (CSPGs) present a barrier to axon regeneration. However, no specific receptor for the inhibitory effect of CSPGs has been identified. We showed that a transmembrane protein tyrosine phosphatase, PTP sigma, binds with high affinity to neural CSPGs. Binding involves the chondroitin sulfate chains and a specific site on the first immunoglobulin-like domain of PTP sigma. In culture, PTP sigma(-/-) neurons show reduced inhibition by CSPG. A PTP sigma fusion protein probe can detect cognate ligands that are up-regulated specifically at neural lesion sites. After spinal cord injury, PTP sigma gene disruption enhanced the ability of axons to penetrate regions containing CSPG. These results indicate that PTP sigma can act as a receptor for CSPGs and may provide new therapeutic approaches to neural regeneration.
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