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Distribution of Myelin Basic Protein and P 2 mRNAs in Rabbit Spinal Cord Oligodendrocytes
Author(s) -
Gillespie C. S.,
Trapp B. D.,
Colman D. R.,
Brophy P. J.
Publication year - 1990
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1990.tb01204.x
Subject(s) - myelin , myelin basic protein , spinal cord , proteolipid protein 1 , polysome , cytoplasm , microbiology and biotechnology , oligodendrocyte , membrane protein , biology , translation (biology) , membrane , chemistry , biochemistry , central nervous system , messenger rna , rna , neuroscience , ribosome , gene
Myelin basic protein (MBP) and P 2 protein are small positively charged proteins found in oligodendrocytes of rabbit spinal cord. Both proteins become incorporated into compact myelin. We have begun investigations into the mechanisms by which MBP and P 2 become incorporated into the myelin membrane. We find that P 2 , like the MBPs, is synthesized on free polysomes in rabbit spinal cord. Cell fractionation experiments reveal that rabbit MBP mRNAs are preferentially segregated to the peripheral myelinating regions whereas P 2 mRNAs are predominantly localized within the perikaryon of the cell. In vitro synthesized rabbit MBP readily associates with membranes added to translation mixtures, whereas P 2 protein does not. It is possible that P 2 requires a “receptor” molecule, perhaps a membrane‐anchored protein, for association with the cytoplasmic face of the myelin membrane.