ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007
The inhibition site on myelin-associated glycoprotein is within Ig-domain 5 and is distinct from the sialic acid binding site.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- A Novel Siglec-4 Derived Spacer Improves the Functionality of CAR T Cells Against Membrane-Proximal Epitopes.Frontiers in immunology · 2020Article
- Myelin-Associated Glycoprotein Inhibits Schwann Cell Migration and Induces Their Death.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Structural basis of myelin-associated glycoprotein adhesion and signalling.Nature communications · 2016Article
- Neurologic syndrome associated with homozygous mutation at MAG sialic acid binding site.Annals of clinical and translational neurology · 2016Article
- Sialic Acid Is Required for Neuronal Inhibition by Soluble MAG but not for Membrane Bound MAG.Frontiers in molecular neuroscience · 2016Article
- Antibodies against gangliosides in patients with dementia.American journal of Alzheimer's disease and other dementias · 2014Article
- Lipid rafts in neurodegeneration and neuroprotection.Molecular neurobiology · 2014Review
- 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
- A novel role for PTEN in the inhibition of neurite outgrowth by myelin-associated glycoprotein in cortical neurons.Molecular and cellular neurosciences · 2011Article
- Guidance molecules in axon regeneration.Cold Spring Harbor perspectives in biology · 2010Review
- Deregulated sphingolipid metabolism and membrane organization in neurodegenerative disorders.Molecular neurobiology · 2010Review
- Myelin-associated glycoprotein and its axonal receptors.Journal of neuroscience research · 2009Review
- 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.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Axonal protective effects of the myelin-associated glycoprotein.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Article
- A hypothesis about the relationship of myelin-associated glycoprotein's function in myelinated axons to its capacity to inhibit neurite outgrowth.Neurochemical research · 2009Review
- beta1-integrin mediates myelin-associated glycoprotein signaling in neuronal growth cones.Molecular brain · 2008Article
- Mechanisms of CNS myelin inhibition: evidence for distinct and neuronal cell type specific receptor systems.Restorative neurology and neuroscience · 2008Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Myelin-associated glycoprotein (MAG) is a potent inhibitor of axonal regeneration. It contains five Ig-like domains and is a sialic binding protein. Previously, we showed that the sialic acid binding site on MAG maps to arginine 118 in Ig domain 1 (Kelm et al., 1994). However, sialic acid binding was neither necessary nor sufficient for MAG to bring about inhibition of neurite outgrowth. Consistent with this, we now map a distinct inhibition site on MAG to Ig domain 5 (Ig-5). We show that when a truncated form of MAG missing Ig domains 1 and 2 is expressed by Chinese hamster ovary (CHO) cells, it does not bind sialic acid, but still inhibits neurite outgrowth almost as effectively as full-length MAG. To determine whether the inhibition site mapped to Ig-3, Ig-4, or Ig-5, we made chimeric molecules of various combinations of these three MAG Ig domains fused to Ig domains from another Ig family member, sialoadhesin (Sn), which also binds to sialic acid in the same linkage as MAG. The MAG-Sn molecules were expressed in CHO cells and all contained five Ig domains and were able to bind sialic acid. However, only the chimeric molecules containing MAG Ig-5 inhibited neurite outgrowth. Furthermore, peptides corresponding to sequences in MAG Ig-5, but not Ig-4 or Sn Ig-5, are able to block inhibition of neurite outgrowth by both wild-type MAG and CNS myelin. We conclude that the inhibition site on MAG is carried by Ig domain 5 and that this site is distinct from the sialic-acid binding site.
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Registered trials
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