We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Identification of versican as an isolectin B4-binding glycoprotein from mammalian spinal cord tissue.
- Authors
Bogen, Oliver; Dreger, Mathias; Gillen, Clemens; Schröder, Wolfgang; Hucho, Ferdinand
- Abstract
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) fromGriffonia 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.
- Subjects
NOCICEPTORS; SPINAL cord; TISSUES; GLYCOPROTEINS; PROTEOGLYCANS; GLYCOCONJUGATES
- Publication
FEBS Journal, 2005, Vol 272, Issue 5, p1090
- ISSN
1742-464X
- Publication type
Article
- DOI
10.1111/j.1742-4658.2005.04543.x