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Potent glycan inhibitors of myelin-associated glycoprotein enhance axon outgrowth in vitro

Academic Article
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Overview

authors

  • Vyas, A. A.
  • Blixt, O.
  • Paulson, James
  • Schnaar, R. L.

publication date

  • April 2005

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Myelin-associated glycoprotein (MAG, Siglec-4) is one of several endogenous axon regeneration inhibitors that limit recovery from central nervous system injury and disease. Molecules that block such inhibitors may enhance axon regeneration and functional recovery. MAG, a member of the Siglec family of sialic acid-binding lectins, binds to sialoglycoconjugates on axons and particularly to gangliosides GD1a and GT1b, which may mediate some of the inhibitory effects of MAG. In a prior study, we identified potent monovalent sialoside inhibitors of MAG using a novel screening platform. In the current study, the most potent of these were tested for their ability to reverse MAG-mediated inhibition of axon outgrowth from rat cerebellar granule neurons in vitro. Monovalent sialoglycans enhanced axon regeneration in proportion to their MAG binding affinities. The most potent glycoside was disialyl T antigen (NeuAcalpha2-3Galbeta1-3[NeuAcalpha2-6]GalNAc-R), followed by 3-sialyl T antigen (NeuAcalpha2-3Galbeta1-3GalNAc-R), structures expressed on O-linked glycoproteins as well as on gangliosides. Prior studies indicated that blocking gangliosides reversed MAG inhibition. In the current study, blocking O-linked glycoprotein sialylation with benzyl-alpha-GalNAc had no effect. The ability to reverse MAG inhibition with monovalent glycosides encourages further exploration of glycans and glycan mimetics as blockers of MAG-mediated axon outgrowth inhibition.

subject areas

  • Animals
  • Axons
  • Cerebellum
  • Ligands
  • Myelin-Associated Glycoprotein
  • N-Acetylneuraminic Acid
  • Polysaccharides
  • Rats
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Identity

PubMed Central ID

  • PMC1852507

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M500250200

PubMed ID

  • 15701648
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Additional Document Info

start page

  • 16305

end page

  • 16310

volume

  • 280

issue

  • 16

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