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Oligodendrocyte‐specific protein (OSP) is a major component of CNS myelin
Author(s) -
Bronstein J.M.,
Micevych P.E.,
Chen K.
Publication year - 1997
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19971201)50:5<713::aid-jnr8>3.0.co;2-k
Subject(s) - myelin , proteolipid protein 1 , oligodendrocyte , myelin associated glycoprotein , myelin basic protein , biology , myelin oligodendrocyte glycoprotein , microbiology and biotechnology , glycoprotein , peptide , white matter , central nervous system , biochemistry , endocrinology , medicine , radiology , magnetic resonance imaging
An oligodendrocyte‐specific protein (OSP) cDNA was recently identified and found to be expressed primarily in oligodendrocytes and has a deduced amino acid sequence similar to that of peripheral myelin protein 22 (PMP‐22). We raised antibodies against a synthetic peptide corresponding to OSP amino acid residues 179–194 which reacted with a 22 kd protein in mouse CNS. OSP immunoreactivity localized to spinal cord white matter tracts using immunohistochemistry in a similar distribution to that of MBP. OSP localized to CNS myelin biochemically with more than a 30‐fold enrichment measured in purified myelin. We further purified the proteolipid fraction of myelin and determined that OSP contributes approximately 7% of total myelin protein making it the third most abundant protein in CNS myelin. No binding was found to several agglutinins or a HNK1‐specific antibody suggesting that OSP is not a glycoprotein. J. Neurosci. Res. 50:713–720, 1997. © 1997 Wiley‐Liss, Inc.