ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2009
Molecular basis of the interactions of the Nogo-66 receptor and its homolog NgR2 with myelin-associated glycoprotein: development of NgROMNI-Fc, a novel antagonist of CNS myelin inhibition.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 55 citations in OpenAlex.
- Targeting the αVβ3/NgR2 pathway in neuroendocrine prostate cancer.Matrix biology : journal of the International Society for Matrix Biology · 2023Article
- How does Nogo receptor influence demyelination and remyelination in the context of multiple sclerosis?Frontiers in cellular neuroscience · 2023Review
- The NOGO receptor NgR2, a novel αVβ3 integrin effector, induces neuroendocrine differentiation in prostate cancer.Scientific reports · 2022Article
- Article
- A Novel Siglec-4 Derived Spacer Improves the Functionality of CAR T Cells Against Membrane-Proximal Epitopes.Frontiers in immunology · 2020Article
- Optic nerve regeneration: A long view.Restorative neurology and neuroscience · 2019Review
- The nociceptin receptor inhibits axonal regeneration and recovery from spinal cord injury.Science signaling · 2018Article
- Spatiotemporal and Long Lasting Modulation of 11 Key Nogo Signaling Genes in Response to Strong Neuroexcitation.Frontiers in molecular neuroscience · 2017Article
- Nogo receptor blockade overcomes remyelination failure after white matter stroke and stimulates functional recovery in aged mice.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The 3 Rs of Stroke Biology: Radial, Relayed, and Regenerative.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2016Review
- Myelin-associated glycoprotein modulates apoptosis of motoneurons during early postnatal development via NgR/p75(NTR) receptor-mediated activation of RhoA signaling pathways.Cell death & disease · 2015Article
- The Neural Stem Cell Microenvironment: Focusing on Axon Guidance Molecules and Myelin-Associated Factors.Journal of molecular neuroscience : MN · 2015Review
- Targeted inhibition of the Shroom3-Rho kinase protein-protein interaction circumvents Nogo66 to promote axon outgrowth.BMC neuroscience · 2015Article
- Lentivirus vector-mediated gene transduction of CNGRC peptide in rat adipose stem cells.Molecular medicine reports · 2015Article
- Insights into the physiological role of CNS regeneration inhibitors.Frontiers in molecular neuroscience · 2015Review
- Semaphorin 5A inhibits synaptogenesis in early postnatal- and adult-born hippocampal dentate granule cells.eLife · 2014Article
- LDL receptor-related protein-1 is a sialic-acid-independent receptor for myelin-associated glycoprotein that functions in neurite outgrowth inhibition by MAG and CNS myelin.Journal of cell science · 2013Article
- Axonal regeneration induced by blockade of glial inhibitors coupled with activation of intrinsic neuronal growth pathways.Experimental neurology · 2012Article
- Small-molecule-induced Rho-inhibition: NSAIDs after spinal cord injury.Cell and tissue research · 2012Review
- Myelin associated inhibitors: a link between injury-induced and experience-dependent plasticity.Experimental neurology · 2012Review
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 1 country.
Funding
Abstract
Myelin-associated glycoprotein (MAG) is a sialic acid-binding Ig-family lectin that functions in neuronal growth inhibition and stabilization of axon-glia interactions. The ectodomain of MAG is comprised of five Ig-like domains and uses neuronal cell-type-specific mechanisms to signal growth inhibition. We show that the first three Ig-like domains of MAG bind with high affinity and in a sialic acid-dependent manner to the Nogo-66 receptor-1 (NgR1) and its homolog NgR2. Domains Ig3-Ig5 of MAG are sufficient to inhibit neurite outgrowth but fail to associate with NgR1 or NgR2. Nogo receptors are sialoglycoproteins comprised of 8.5 canonical leucine-rich repeats (LRR) flanked by LRR N-terminal (NT) and C-terminal (CT)-cap domains. The LRR cluster is connected through a stalk region to a membrane lipid anchor. The CT-cap domain and stalk region of NgR2, but not NgR1, are sufficient for MAG binding, and when expressed in neurons, exhibit constitutive growth inhibitory activity. The LRR cluster of NgR1 supports binding of Nogo-66, OMgp, and MAG. Deletion of disulfide loop Cys(309)-Cys(336) of NgR1 selectively increases its affinity for Nogo-66 and OMgp. A chimeric Nogo receptor variant (NgR(OMNI)) in which Cys(309)-Cys(336) is deleted and followed by a 13 aa MAG-binding motif of the NgR2 stalk, shows superior binding of OMgp, Nogo-66, and MAG compared with wild-type NgR1 or NgR2. Soluble NgR(OMNI) (NgR(OMNI)-Fc) binds strongly to membrane-bound inhibitors and promotes neurite outgrowth on both MAG and CNS myelin substrates. Thus, NgR(OMNI)-Fc may offer therapeutic opportunities following nervous system injury or disease where myelin inhibits neuronal regeneration.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.