Identification of versican as an isolectin B4-binding glycoprotein from mammalian spinal cord tissue

FEBS J. 2005 Mar;272(5):1090-102. doi: 10.1111/j.1742-4658.2005.04543.x.


Nociceptors are specialized nerve fibers that transmit noxious pain stimuli to the dorsal horn of the spinal cord. A subset of nociceptors, the nonpeptidergic C-fibers, is characterized by its reactivity for the plant isolectin B4 (IB4) from Griffonia simplicifolia. The molecular nature of the IB4-reactive glycoconjugate, although used as a neuroanatomical marker for more than a decade, has remained unknown. We here present data which strongly suggest that a splice variant of the extracellular matrix proteoglycan versican is the IB4-reactive glycoconjugate associated with these nociceptors. We isolated (by subcellular fractionation and IB4 affinity chromatography) a glycoconjugate from porcine spinal cord tissue that migrated in SDS/PAGE as a single distinct protein band at an apparent molecular mass of > 250 kDa. By using MALDI-TOF/TOF MS, we identified this glycoconjugate unambiguously as a V2-like variant of versican. Moreover, we demonstrate that the IB4-reactive glycoconjugate and the versican variant can be co-released from spinal cord membranes by hyaluronidase, and that the IB4-reactive glycoconjugate and the versican variant can be co-precipitated by an anti-versican immunoglobulin and perfectly co-migrate in SDS/PAGE. Our findings shed new light on the role of the extracellular matrix, which is thought to be involved in plastic changes underlying pain-related phenomena such as hyperalgesia and allodynia.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chondroitin Sulfate Proteoglycans / chemistry
  • Chondroitin Sulfate Proteoglycans / isolation & purification
  • Chondroitin Sulfate Proteoglycans / metabolism*
  • Chromatography, Affinity
  • Glycoproteins / chemistry
  • Glycoproteins / isolation & purification
  • Glycoproteins / metabolism*
  • Hyaluronoglucosaminidase / metabolism
  • Lectins / metabolism*
  • Lectins, C-Type
  • Molecular Sequence Data
  • Peptide Fragments / metabolism
  • Proteoglycans / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Spinal Cord / chemistry
  • Spinal Cord / metabolism*
  • Subcellular Fractions
  • Swine
  • Versicans


  • Chondroitin Sulfate Proteoglycans
  • Glycoproteins
  • Lectins
  • Lectins, C-Type
  • Peptide Fragments
  • Proteoglycans
  • Versicans
  • Hyaluronoglucosaminidase