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Myelin proteolipid DM20: evidence for function independent of myelination
Author(s) -
Nadon Nancy L.,
Miller Shirley,
Draeger Karen,
Salvaggio Michelle
Publication year - 1997
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/s0736-5748(97)00009-9
Subject(s) - proteolipid protein 1 , myelin , biology , peripheral nervous system , central nervous system , nervous system , myelin proteolipid protein , immunology , microbiology and biotechnology , myelin basic protein , neuroscience
DM20 is a proteolipid protein that has been extensively studied for its role in central nervous system myelination. We demonstrate that DM20 expression is wide‐spread and independent of myelination. In the Schwann cells and neurons of the peripheral nervous system, DM20 is not incorporated into the membrane as it is in the central nervous system (CNS), but remains cytoplasmic. Mutations that severely reduce the amount of DM20 mRNA in CNS myelinating cells have little effect on DM20 expression in nonmyelinating cells of the peripheral nervous system and embryonic CNS. Most importantly, the combination of wild‐type DM20 from the endogenous X‐linked gene and mutant DM20 expressed from an autosomal transgene results in embryonic lethality. We propose a function for DM20 to explain these diverse findings based on the ability of DM20 to form multimeric complexes, and hypothesize that the DM20 complex participates in intracellular molecular transport.