Identification of versican as an isolectin B4-binding glycoprotein from mammalian spinal cord tissue.
FEBS J
; 272(5): 1090-102, 2005 Mar.
Article
in En
| MEDLINE
| ID: mdl-15720384
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) 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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Chondroitin Sulfate Proteoglycans
/
Spinal Cord
/
Glycoproteins
/
Lectins
Type of study:
Diagnostic_studies
/
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
FEBS J
Journal subject:
BIOQUIMICA
Year:
2005
Document type:
Article
Affiliation country:
Germany