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A proteomic approach to rapidly elucidate oligodendrocyte‐associated proteins expressed in the myelinating rat optic nerve
Author(s) -
Colello Raymond J.,
Fuss Babette,
Fox Michael A.,
Alberti James
Publication year - 2002
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/1522-2683(200201)23:1<144::aid-elps144>3.0.co;2-p
Subject(s) - oligodendrocyte , remyelination , optic nerve , myelin , biology , proteomics , microbiology and biotechnology , gel electrophoresis , two dimensional gel electrophoresis , chemistry , biochemistry , neuroscience , central nervous system , gene
The lack of cDNA libraries derived from myelinating oligodendrocytes has hampered attempts to identify proteins associated with myelination during normal development or with remyelination after insult or disease. We, therefore, established a new method to elucidate such proteins by coupling the techniques of X‐irradiation, two‐dimensional (2‐D) gel electrophoresis, and mass spectrometry. Specifically, 2‐D gel protein profiles of normal optic nerves were compared with those of X‐irradiated rat optic nerves, which were absent of oligodendrocytes, to elucidate oligodendrocyte‐associated proteins. The subsequent identification of these oligodendrocyte‐associated proteins was accomplished by mass spectrometry. The results presented in this paper demonstrate the potential of the X‐irradiated optic nerve model system combined with proteomic techniques to rapidly elucidate oligodendrocyte‐associated proteins expressed in vivo .