Source:http://linkedlifedata.com/resource/pubmed/id/15720384
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2005-2-21
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pubmed:abstractText |
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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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hyaluronoglucosaminidase,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Versicans
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1742-464X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1090-102
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15720384-Amino Acid Sequence,
pubmed-meshheading:15720384-Animals,
pubmed-meshheading:15720384-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:15720384-Chromatography, Affinity,
pubmed-meshheading:15720384-Glycoproteins,
pubmed-meshheading:15720384-Hyaluronoglucosaminidase,
pubmed-meshheading:15720384-Lectins,
pubmed-meshheading:15720384-Lectins, C-Type,
pubmed-meshheading:15720384-Molecular Sequence Data,
pubmed-meshheading:15720384-Peptide Fragments,
pubmed-meshheading:15720384-Proteoglycans,
pubmed-meshheading:15720384-Spectrometry, Mass, Matrix-Assisted Laser...,
pubmed-meshheading:15720384-Spinal Cord,
pubmed-meshheading:15720384-Subcellular Fractions,
pubmed-meshheading:15720384-Swine,
pubmed-meshheading:15720384-Versicans
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pubmed:year |
2005
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pubmed:articleTitle |
Identification of versican as an isolectin B4-binding glycoprotein from mammalian spinal cord tissue.
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pubmed:affiliation |
Freie Universität Berlin, Institut für Chemie-Biochemie, Thielallee, Berlin, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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